1. Sulfatide (d18:1/24:0)
2. 3'-O-Sulphogalactosylceramide
3. 3-O-Sulfogalactosylceramide
4. 3-O-Sulphogalactosylceramide
5. 3-O-sulfo-beta-D-galactosylceramide
6. Cerebroside 3-sulfate
7. Galactosylceramide-sulfate
8. Galactosylceramidesulfate
9. Sulfatide
10. 3-O-sulfo-beta-delta-galactosylceramide
11. N-[(1S,2R,3E)-2-hydroxy-1-[[(3-O-sulfo-b-D-galactopyranosyl)oxy]methyl]-3-heptadecen-1-yl]-Tetracosanamide
12. N-[(1S,2R,3E)-2-hydroxy-1-[[(3-O-sulfo-b-D-galactopyranosyl)oxy]methyl]-3-heptadecenyl]-Tetracosanamide
13. [R-[R*,S*-(E)]]-N-[2-hydroxy-1-[[(3-O-sulfo-b-D-galactopyranosyl)oxy]methyl]-3-heptadecenyl]-Tetracosanamide
14. N-[(1S,2R,3E)-2-hydroxy-1-[[(3-O-sulfo-beta-delta-galactopyranosyl)oxy]methyl]-3-heptadecen-1-yl]-Tetracosanamide
15. N-[(1S,2R,3E)-2-hydroxy-1-[[(3-O-sulfo-beta-delta-galactopyranosyl)oxy]methyl]-3-heptadecenyl]-Tetracosanamide
16. [R-[R*,S*-(E)]]-N-[2-hydroxy-1-[[(3-O-sulfo-beta-delta-galactopyranosyl)oxy]methyl]-3-heptadecenyl]-Tetracosanamide

• Lysosome
• membrane

• Urine

• 250100 (Metachromatic leukodystrophy)

1. Wenger DA, DeGala G, Williams C, Taylor HA, Stevenson RE, Pruitt JR, Miller J, Garen PD, Balentine JD: Clinical, pathological, and biochemical studies on an infantile case of sulfatide/GM1 activator protein deficiency. Am J Med Genet. 1989 Jun;33(2):255-65. [PubMed ]
2. Tamaoki A, Kikkawa Y: [The role of sulfatides in autoimmunity in children with various glomerular disease] Nippon Jinzo Gakkai Shi. 1991 Nov;33(11):1045-54. [PubMed ]
3. Eto Y, Kawame H, Hasegawa Y, Ohashi T, Ida H, Tokoro T: Molecular characteristics in Japanese patients with lipidosis: novel mutations in metachromatic leukodystrophy and Gaucher disease. Mol Cell Biochem. 1993 Feb 17;119(1-2):179-84. [PubMed ]
4. Monti E, Preti A, Novati A, Aleo MF, Clemente ML, Marchesini S: Uptake and metabolism of a fluorescent sulfatide analogue in cultured skin fibroblasts. Biochim Biophys Acta. 1992 Feb 20;1124(1):80-7. [PubMed ]
5. Tsaioun KI: Vitamin K-dependent proteins in the developing and aging nervous system. Nutr Rev. 1999 Aug;57(8):231-40. [PubMed ]
6. Nobile-Orazio E, Manfredini E, Carpo M, Meucci N, Monaco S, Ferrari S, Bonetti B, Cavaletti G, Gemignani F, Durelli L, et al.: Frequency and clinical correlates of anti-neural IgM antibodies in neuropathy associated with IgM monoclonal gammopathy. Ann Neurol. 1994 Sep;36(3):416-24. [PubMed ]
7. Natowicz MR, Prence EM, Chaturvedi P, Newburg DS: Urine sulfatides and the diagnosis of metachromatic leukodystrophy. Clin Chem. 1996 Feb;42(2):232-8. [PubMed ]
8. Hulyalkar AR, Nora R, Manowitz P: Arylsulfatase A variants in patients with alcoholism. Alcohol Clin Exp Res. 1984 May-Jun;8(3):337-41. [PubMed ]
9. Marchesini S, Preti A, Aleo MF, Casella A, Dagan A, Gatt S: Synthesis, spectral properties and enzymatic hydrolysis of fluorescent derivatives of cerebroside sulfate containing long-wavelength-emission probes. Chem Phys Lipids. 1990 Mar;53(2-3):165-75. [PubMed ]
10. Cheng H, Xu J, McKeel DW Jr, Han X: Specificity and potential mechanism of sulfatide deficiency in Alzheimer's disease: an electrospray ionization mass spectrometric study. Cell Mol Biol (Noisy-le-grand). 2003 Jul;49(5):809-18. [PubMed ]
11. Guchhait P, Lopez JA, Thiagarajan P: Characterization of autoantibodies against sulfatide from a V-gene phage-display library derived from patients with systemic lupus erythematosus. J Immunol Methods. 2004 Dec;295(1-2):129-37. Epub 2004 Oct 26. [PubMed ]
12. Eto Y, Tahara T, Koda N, Yamaguchi S, Ito F, Okuno A: Prenatal diagnosis of metachromatic leukodystrophy: a diagnosis by amniotic fluid and its confirmation. Arch Neurol. 1982 Jan;39(1):29-32. [PubMed ]
13. Inui K, Wenger DA: Concentrations of an activator protein for sphingolipid hydrolysis in liver and brain samples from patients with lysosomal storage diseases. J Clin Invest. 1983 Nov;72(5):1622-8. [PubMed ]
14. Li YT, Muhiudeen IA, DeGasperi R, Hirabayashi Y, Li SC: Presence of activator proteins for the enzymic hydrolysis of GM1 and GM2 gangliosides in normal human urine. Am J Hum Genet. 1983 Jul;35(4):629-34. [PubMed ]
15. Matzner U, Herbst E, Hedayati KK, Lullmann-Rauch R, Wessig C, Schroder S, Eistrup C, Moller C, Fogh J, Gieselmann V: Enzyme replacement improves nervous system pathology and function in a mouse model for metachromatic leukodystrophy. Hum Mol Genet. 2005 May 1;14(9):1139-52. Epub 2005 Mar 16. [PubMed ]
16. Wikipedia

1. Galactocerebrosidase precursor
2. Arylsulfatase D precursor
3. Galactosylceramide sulfotransferase
4. Arylsulfatase A precursor
5. Arylsulfatase E precursor
6. Globoside alpha-1,3-N-acetylgalactosaminyltransferase 1
7. N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
8. Sphingomyelin phosphodiesterase precursor
9. Ceramide glucosyltransferase
10. Lactosylceramide 4-alpha-galactosyltransferase
11. Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q
12. Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
13. Phosphatidylinositol N-acetylglucosaminyltransferase subunit H
14. Phosphatidylinositol N-acetylglucosaminyltransferase subunit P
15. Phosphatidylinositol N-acetylglucosaminyltransferase subunit C
16. Acid ceramidase precursor
17. Ectonucleotide pyrophosphatase/phosphodiesterase family member 7 precursor
18. Sphingomyelin phosphodiesterase 2
19. Goodpasture antigen-binding protein
20. Proactivator polypeptide precursor [Contains: Saposin A
21. Ganglioside GM2 activator precursor
22. Myelin basic protein
23. Glucosylceramidase precursor
24. P-selectin precursor
25. L-selectin precursor
26. T-cell surface glycoprotein CD1e precursor
27. Epididymal secretory protein E1 precursor
28. LAG1 longevity assurance homolog 1
29. T-cell surface glycoprotein CD1d precursor
30. ADAMTS-like protein 1 precursor
31. GPI mannosyltransferase 1
32. Phosphatidylinositol-glycan biosynthesis class W protein
33. Phosphatidylinositol-glycan biosynthesis class X protein precursor
34. GPI mannosyltransferase 4
35. UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 5
36. Sphingomyelin phosphodiesterase 3
37. Beta-1,3-galactosyltransferase 5
38. Beta-1,4-galactosyltransferase 6
39. GPI mannosyltransferase 3
40. Phosphatidylinositol-glycan biosynthesis class F protein
41. GPI ethanolamine phosphate transferase 2
42. GPI ethanolamine phosphate transferase 1
43. GPI ethanolamine phosphate transferase 3
44. GPI transamidase component PIG-S
45. GPI transamidase component PIG-T precursor
46. Phosphatidylinositol glycan anchor biosynthesis class U protein
47. GPI mannosyltransferase 2
48. Phosphatidylinositol N-acetylglucosaminyltransferase subunit Y
49. Pleckstrin homology domain-containing family A member 8
50. Sphingomyelin phosphodiesterase 4
51. Laminin subunit alpha-1 precursor
52. Putative neutral ceramidase C
53. Alkaline ceramidase 2
54. Alkaline ceramidase 2
55. Neutral ceramidase
56. Non-lysosomal glucosylceramidase
57. Alkaline ceramidase 1
58. Killer cell lectin-like receptor subfamily B member 1
59. Accessory protein p30II
60. LAG1 longevity assurance homolog 5
61. ATP-binding cassette sub-family A member 7
62. GPI-anchor transamidase
63. Glycosylphosphatidylinositol anchor attachment 1 protein
64. Protein PLEKHA9
65. Glycolipid transfer protein domain-containing protein 2
66. Putative uncharacterized protein PLEKHA8
67. cDNA FLJ61247, highly similar to Mus musculus pleckstrin homology domain containing, family A member 8, mRNA
68. T-cell surface glycoprotein CD1a
69. Glycolipid transfer protein domain-containing protein 1
70. T-cell surface glycoprotein CD1c
71. Lipopolysaccharide-binding protein
72. Putative uncharacterized protein DKFZp434L0435
73. T-cell surface glycoprotein CD1b
74. Glycolipid transfer protein

1. GALCERase
2. Galactosylceramidase
3. Galactosylceramide beta-galactosidase
4. Galactocerebroside beta-galactosidase

MTAAAGSAGRAAVPLLLCALLAPGGAYVLDDSDGLGREFDGIGAVSGGGATSRLLVNYPE
PYRSQILDYLFKPNFGASLHILKVEIGGDGQTTDGTEPSHMHYALDENYFRGYEWWLMKE
AKKRNPNITLIGLPWSFPGWLGKGFDWPYVNLQLTAYYVVTWIVGAKRYHDLDIDYIGIW
NERSYNANYIKILRKMLNYQGLQRVKIIASDNLWESISASMLLDAELFKVVDVIGAHYPG
THSAKDAKLTGKKLWSSEDFSTLNSDMGAGCWGRILNQNYINGYMTSTIAWNLVASYYEQ
LPYGRCGLMTAQEPWSGHYVVESPVWVSAHTTQFTQPGWYYLKTVGHLEKGGSYVALTDG
LGNLTIIIETMSHKHSKCIRPFLPYFNVSQQFATFVLKGSFSEIPELQVWYTKLGKTSER
FLFKQLDSLWLLDSDGSFTLSLHEDELFTLTTLTTGRKGSYPLPPKSQPFPSTYKDDFNV
DYPFFSEAPNFADQTGVFEYFTNIEDPGEHHFTLRQVLNQRPITWAADASNTISIIGDYN
WTNLTIKCDVYIETPDTGGVFIAGRVNKGGILIRSARGIFFWIFANGSYRVTGDLAGWII
YALGRVEVTAKKWYTLTLTIKGHFASGMLNDKSLWTDIPVNFPKNGWAAIGTHSFEFAQF
DNFLVEATR

• Sphingolipid Metabolism (map00600 )

• D-galactosyl-N-acylsphingosine + H2O = D-galactose + N-acylsphingosine

• Glyco_hydro_59 (PF02057 )

• 1-26

ATGACTGCGGCCGCGGGTTCGGCGGGCCGCGCCGCGGTGCCCTTGCTGCTGTGTGCGCTG
CTGGCGCCCGGCGGCGCGTACGTGCTCGACGACTCCGACGGGCTGGGCCGGGAGTTCGAC
GGCATCGGCGCGGTCAGCGGCGGCGGGGCAACCTCCCGACTTCTAGTAAATTACCCAGAG
CCCTATCGTTCTCAGATATTGGATTATCTCTTTAAGCCGAATTTTGGTGCCTCTTTGCAT
ATTTTAAAAGTGGAAATAGGTGGTGATGGGCAGACAACAGACGGCACTGAGCCCTCCCAC
ATGCATTATGCACTAGATGAGAATTATTTCCGAGGATACGAGTGGTGGTTGATGAAAGAA
GCTAAGAAGAGGAATCCCAATATTACACTCATTGGGTTGCCATGGTCATTCCCTGGATGG
CTGGGAAAAGGTTTCGACTGGCCTTATGTCAATCTTCAGCTGACTGCCTATTATGTCGTG
ACCTGGATTGTGGGCGCCAAGCGTTACCATGATTTGGACATTGATTATATTGGAATTTGG
AATGAGAGGTCATATAATGCCAATTATATTAAGATATTAAGAAAAATGCTGAATTATCAA
GGTCTCCAGCGAGTGAAAATCATAGCAAGTGATAATCTCTGGGAGTCCATCTCTGCATCC
ATGCTCCTTGATGCCGAACTCTTCAAGGTGGTTGATGTTATAGGGGCTCATTATCCTGGA
ACCCATTCAGCAAAAGATGCAAAGTTGACTGGGAAGAAGCTTTGGTCTTCTGAAGACTTT
AGCACTTTAAATAGTGACATGGGTGCAGGCTGCTGGGGTCGCATTTTAAATCAGAATTAT
ATCAATGGCTATATGACTTCCACAATCGCATGGAATTTAGTGGCTAGTTACTATGAACAG
TTGCCTTATGGGAGATGCGGGTTGATGACGGCCCAAGAGCCATGGAGTGGGCACTACGTG
GTAGAATCTCCTGTCTGGGTATCAGCTCATACCACTCAGTTTACTCAACCTGGCTGGTAT
TACCTGAAGACAGTTGGCCATTTAGAGAAAGGAGGAAGCTACGTAGCTCTGACTGATGGC
TTAGGGAACCTCACCATCATCATTGAAACCATGAGTCATAAACATTCTAAGTGCATACGG
CCATTTCTTCCTTATTTCAATGTGTCACAACAATTTGCCACCTTTGTTCTTAAGGGATCT
TTTAGTGAAATACCAGAGCTACAGGTATGGTATACCAAACTTGGAAAAACATCCGAAAGA
TTTCTTTTTAAGCAGCTGGATTCTCTATGGCTCCTTGACAGCGATGGCAGTTTCACACTG
AGCCTGCATGAAGATGAGCTGTTCACACTCACCACTCTCACCACTGGTCGCAAAGGCAGC
TACCCGCTTCCTCCAAAATCCCAGCCCTTCCCAAGTACCTATAAGGATGATTTCAATGTT
GATTACCCATTTTTTAGTGAAGCTCCAAACTTTGCTGATCAAACTGGTGTATTTGAATAT
TTTACAAATATTGAAGACCCTGGCGAGCATCACTTCACGCTACGCCAAGTTCTCAACCAG
AGACCCATTACGTGGGCTGCCGATGCATCCAACACAATCAGTATTATAGGAGACTACAAC
TGGACCAATCTGACTATAAAGTGTGATGTTTACATAGAGACCCCTGACACAGGAGGTGTG
TTCATTGCAGGAAGAGTAAATAAAGGTGGTATTTTGATTAGAAGTGCCAGAGGAATTTTC
TTCTGGATTTTTGCAAATGGATCTTACAGGGTTACAGGTGATTTAGCTGGATGGATTATA
TATGCTTTAGGACGTGTTGAAGTTACAGCAAAAAAATGGTATACACTCACGTTAACTATT
AAGGGTCATTTCGCCTCTGGCATGCTGAATGACAAGTCTCTGTGGACAGACATCCCTGTG
AATTTTCCAAAGAATGGCTGGGCTGCAATTGGAACTCACTCCTTTGAATTTGCACAGTTT
GACAACTTTCTTGTGGAAGCCACACGCTAA

1. Sakai N, Inui K, Fujii N, Fukushima H, Nishimoto J, Yanagihara I, Isegawa Y, Iwamatsu A, Okada S: Krabbe disease: isolation and characterization of a full-length cDNA for human galactocerebrosidase. Biochem Biophys Res Commun. 1994 Jan 28;198(2):485-91. [PubMed ]
2. Chen YQ, Rafi MA, de Gala G, Wenger DA: Cloning and expression of cDNA encoding human galactocerebrosidase, the enzyme deficient in globoid cell leukodystrophy. Hum Mol Genet. 1993 Nov;2(11):1841-5. [PubMed ]
3. Luzi P, Rafi MA, Wenger DA: Structure and organization of the human galactocerebrosidase (GALC) gene. Genomics. 1995 Mar 20;26(2):407-9. [PubMed ]
4. Sakai N, Fukushima H, Inui K, Fu L, Nishigaki T, Yanagihara I, Tatsumi N, Ozono K, Okada S: Human galactocerebrosidase gene: promoter analysis of the 5'-flanking region and structural organization. Biochim Biophys Acta. 1998 Jan 7;1395(1):62-7. [PubMed ]
5. Chen YQ, Wenger DA: Galactocerebrosidase from human urine: purification and partial characterization. Biochim Biophys Acta. 1993 Sep 29;1170(1):53-61. [PubMed ]
6. Wenger DA, Rafi MA, Luzi P: Molecular genetics of Krabbe disease (globoid cell leukodystrophy): diagnostic and clinical implications. Hum Mutat. 1997;10(4):268-79. [PubMed ]
7. Wenger DA, Rafi MA, Luzi P, Datto J, Costantino-Ceccarini E: Krabbe disease: genetic aspects and progress toward therapy. Mol Genet Metab. 2000 May;70(1):1-9. [PubMed ]
8. Rafi MA, Luzi P, Chen YQ, Wenger DA: A large deletion together with a point mutation in the GALC gene is a common mutant allele in patients with infantile Krabbe disease. Hum Mol Genet. 1995 Aug;4(8):1285-9. [PubMed ]
9. Tatsumi N, Inui K, Sakai N, Fukushima H, Nishimoto J, Yanagihara I, Nishigaki T, Tsukamoto H, Fu L, Taniike M, et al.: Molecular defects in Krabbe disease. Hum Mol Genet. 1995 Oct;4(10):1865-8. [PubMed ]
10. De Gasperi R, Gama Sosa MA, Sartorato EL, Battistini S, MacFarlane H, Gusella JF, Krivit W, Kolodny EH: Molecular heterogeneity of late-onset forms of globoid-cell leukodystrophy. Am J Hum Genet. 1996 Dec;59(6):1233-42. [PubMed ]
11. Rafi MA, Luzi P, Zlotogora J, Wenger DA: Two different mutations are responsible for Krabbe disease in the Druze and Moslem Arab populations in Israel. Hum Genet. 1996 Mar;97(3):304-8. [PubMed ]
12. Furuya H, Kukita Y, Nagano S, Sakai Y, Yamashita Y, Fukuyama H, Inatomi Y, Saito Y, Koike R, Tsuji S, Fukumaki Y, Hayashi K, Kobayashi T: Adult onset globoid cell leukodystrophy (Krabbe disease): analysis of galactosylceramidase cDNA from four Japanese patients. Hum Genet. 1997 Sep;100(3-4):450-6. [PubMed ]
13. De Gasperi R, Gama Sosa MA, Sartorato E, Battistini S, Raghavan S, Kolodny EH: Molecular basis of late-life globoid cell leukodystrophy. Hum Mutat. 1999;14(3):256-62. [PubMed ]
14. Fu L, Inui K, Nishigaki T, Tatsumi N, Tsukamoto H, Kokubu C, Muramatsu T, Okada S: Molecular heterogeneity of Krabbe disease. J Inherit Metab Dis. 1999 Apr;22(2):155-62. [PubMed ]

1. ASD

MRSAARRGRAAPAARDSLPVLLFLCLLLKTCEPKTANAFKPNILLIMADDLGTGDLGCYG
NNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMDASNGYRALQWNA
GSGGLPENETTFARILQQHGYATGLIGKWHQGVNCASRGDHCHHPLNHGFDYFYGMPFTL
TNDCDPGRPPEVDAALRAQLWGYTQFLALGILTLAAGQTCGFFSVSARAVTGMAGVGCLF
FISWYSSFGFVRRWNCILMRNHDVTEQPMVLEKTASLMLKEAVSYIERHKHGPFLLFLSL
LHVHIPLVTTSAFLGKSQHGLYGDNVEEMDWLIGKVLNAIEDNGLKNSTFTYFTSDHGGH
LEARDGHSQLGGWNGIYKGGKGMGGWEGGIRVPGIFHWPGVLPAGRVIGEPTSLMDVFPT
VVQLVGGEVPQDRVIDGHSLVPLLQGAEARSAHEFLFHYCGQHLHAARWHQKDSGSVWKV
HYTTPQFHPEERGLLTAEASAHAEWGGVTHHRPPLLFDLSRDPSEARPLTPDSEPLYHAV
IARVGAAVSEHRQTLSPVPQQFSMSNILWKPWLQPCCGHFPFCSCHEDGDGTP

• Sulfatase (PF00884 )

• 1-33

• 206-225
• 229-251
• 292-314

ATGCGATCCGCCGCGCGGAGGGGACGCGCCGCGCCCGCCGCCAGGGACTCTTTGCCGGTG
CTACTGTTTTTATGCTTGCTTCTGAAGACGTGTGAACCTAAAACTGCAAATGCCTTTAAA
CCAAATATCCTACTGATCATGGCGGATGATCTAGGCACTGGGGATCTCGGTTGCTACGGG
AACAATACACTGAGAACGCCGAATATTGACCAGCTTGCAGAGGAAGGTGTGAGGCTCACT
CAGCACCTGGCGGCCGCCCCGCTCTGCACCCCAAGCCGAGCTGCATTCCTCACAGGGAGA
CATTCCTTCAGATCAGGCATGGACGCCAGCAATGGATACCGGGCCCTTCAGTGGAACGCA
GGCTCAGGTGGACTCCCTGAGAACGAAACCACTTTTGCAAGAATCTTGCAGCAGCATGGC
TATGCAACCGGCCTCATAGGAAAATGGCACCAGGGTGTGAATTGTGCATCCCGCGGGGAT
CACTGCCACCACCCCCTGAACCACGGATTTGACTATTTCTACGGCATGCCCTTCACGCTC
ACAAACGACTGTGACCCAGGCAGGCCCCCCGAAGTGGACGCCGCCCTGAGGGCGCAGCTC
TGGGGTTACACCCAGTTCCTGGCGCTGGGGATTCTCACCCTGGCTGCCGGCCAGACCTGC
GGTTTCTTCTCTGTCTCCGCGAGAGCAGTCACCGGCATGGCCGGCGTGGGCTGCCTGTTT
TTCATCTCTTGGTACTCCTCCTTCGGGTTTGTGCGACGCTGGAACTGTATCCTGATGAGA
AACCATGACGTCACGGAGCAACCCATGGTTCTGGAGAAAACAGCGAGTCTTATGCTAAAG
GAAGCTGTTTCCTATATTGAAAGACACAAGCATGGGCCATTTCTCCTCTTCCTTTCTTTG
CTGCATGTGCACATTCCCCTTGTGACCACGAGTGCATTCCTGGGGAAAAGTCAGCATGGC
TTATATGGTGATAATGTGGAGGAGATGGACTGGCTCATAGGTAAGGTTCTTAATGCCATC
GAAGACAATGGTTTAAAGAACTCAACATTCACGTATTTCACCTCTGACCATGGAGGACAT
TTAGAGGCAAGAGATGGACACAGCCAGTTAGGGGGATGGAACGGAATTTACAAAGGTGGG
AAGGGCATGGGAGGATGGGAAGGTGGGATCCGAGTGCCCGGGATCTTCCACTGGCCGGGG
GTGCTCCCGGCCGGCCGAGTGATTGGAGAGCCCACGAGCCTGATGGACGTGTTCCCTACT
GTGGTCCAGCTGGTGGGTGGCGAGGTGCCCCAGGACAGGGTGATTGATGGCCACAGCCTG
GTACCCTTGCTGCAGGGAGCTGAGGCACGCTCGGCACATGAGTTCCTGTTTCATTACTGT
GGGCAGCATCTTCACGCAGCACGCTGGCACCAGAAGGACAGTGGAAGCGTCTGGAAGGTT
CATTACACGACCCCGCAGTTCCACCCCGAGGAGCGGGGCCTGCTAACGGCCGAGGCGTCT
GCCCATGCTGAATGGGGAGGCGTGACCCATCACAGACCCCCTTTGCTCTTTGACCTCTCC
AGGGACCCCTCCGAGGCACGGCCCCTGACCCCCGACTCCGAGCCCCTGTACCACGCCGTG
ATAGCAAGGGTAGGTGCCGCGGTGTCGGAGCATCGGCAGACCCTGAGTCCTGTGCCCCAG
CAGTTTTCCATGAGCAACATCCTGTGGAAGCCGTGGCTGCAGCCGTGCTGCGGACATTTC
CCGTTCTGTTCATGCCACGAGGATGGGGATGGCACCCCCTGA

1. Franco B, Meroni G, Parenti G, Levilliers J, Bernard L, Gebbia M, Cox L, Maroteaux P, Sheffield L, Rappold GA, et al.: A cluster of sulfatase genes on Xp22.3: mutations in chondrodysplasia punctata (CDPX) and implications for warfarin embryopathy. Cell. 1995 Apr 7;81(1):15-25. [PubMed ]
2. Urbitsch P, Salzer MJ, Hirschmann P, Vogt PH: Arylsulfatase D gene in Xp22.3 encodes two protein isoforms. DNA Cell Biol. 2000 Dec;19(12):765-73. [PubMed ]

1. GalCer sulfotransferase
2. Cerebroside sulfotransferase
3. 3'- phosphoadenylylsulfate:galactosylceramide 3'-sulfotransferase
4. 3'- phosphoadenosine-5'-phosphosulfate:GalCer sulfotransferase

MLPPQKKPWESMAKGLVLGALFTSFLLLVYSYAVPPLHAGLASTTPEAAASCSPPALEPE
AVIRANGSAGECQPRRNIVFLKTHKTASSTLLNILFRFGQKHRLKFAFPNGRNDFDYPTF
FARSLVQDYRPGACFNIICNHMRFHYDEVRGLVPTNAIFITVLRDPARLFESSFHYFGPV
VPLTWKLSAGDKLTEFLQDPDRYYDPNGFNAHYLRNLLFFDLGYDNSLDPSSPQVQEHIL
EVERRFHLVLLQEYFDESLVLLKDLLCWELEDVLYFKLNARRDSPVPRLSGELYGRATAW
NMLDSHLYRHFNASFWRKVEAFGRERMAREVAALRHANERMRTICIDGGHAVDAAAIQDE
AMQPWQPLGTKSILGYNLKKSIGQRHAQLCRRMLTPEIQYLMDLGANLWVTKLWKFIRDF
LRW

• Sphingolipid Metabolism (map00600 )

• 3'-phosphoadenylyl sulfate + a galactosylceramide = adenosine 3',5'-bisphosphate + galactosylceramidesulfate

• Gal-3-0_sulfotr (PF06990 )

• 1-33

ATGCTGCCACCGCAGAAGAAGCCCTGGGAGTCCATGGCTAAGGGGCTGGTGCTGGGCGCG
CTCTTCACTAGTTTCCTGCTGCTGGTGTACTCCTATGCCGTGCCCCCGCTGCATGCCGGC
CTGGCCTCCACGACCCCGGAGGCCGCAGCGTCCTGCTCTCCACCTGCACTCGAGCCAGAG
GCAGTGATCCGGGCCAACGGCTCGGCGGGGGAGTGCCAGCCGCGGCGCAACATCGTGTTC
TTGAAGACGCACAAGACGGCCAGCAGCACCCTGCTCAACATCCTGTTCCGCTTCGGCCAG
AAGCACCGGCTCAAGTTCGCCTTCCCTAACGGCCGCAATGACTTCGACTACCCGACCTTC
TTCGCCCGCAGCCTGGTGCAGGACTATCGGCCCGGGGCCTGCTTCAACATCATCTGCAAC
CACATGCGCTTCCACTACGACGAGGTGCGCGGCCTGGTGCCGACCAACGCCATCTTCATC
ACGGTGCTCCGCGACCCCGCCCGCTTGTTCGAGTCCTCCTTCCACTACTTCGGGCCGGTG
GTGCCCCTCACGTGGAAGCTCTCGGCCGGCGACAAGCTGACCGAGTTCCTGCAAGACCCG
GATCGCTACTACGACCCCAACGGCTTCAATGCCCACTACCTCCGAAACCTGCTCTTCTTC
GACCTGGGCTATGACAACAGCCTGGACCCCAGCAGCCCGCAGGTGCAGGAGCACATCCTG
GAGGTGGAGCGTCGCTTCCACCTGGTGCTCCTTCAAGAGTACTTCGACGAGTCGCTGGTG
CTGCTGAAGGACCTGCTGTGCTGGGAGCTGGAGGACGTGCTCTACTTCAAGCTCAACGCC
CGCCGCGACTCGCCCGTGCCGCGGCTCTCGGGGGAGCTGTATGGGCGCGCCACCGCCTGG
AACATGCTGGACTCCCACCTCTACCGCCACTTCAACGCCAGCTTCTGGCGCAAGGTGGAG
GCCTTCGGGCGGGAGCGCATGGCCCGCGAGGTGGCCGCCCTGCGCCATGCCAACGAGCGC
ATGCGGACCATCTGCATCGACGGGGGCCACGCCGTGGACGCCGCCGCCATCCAGGACGAG
GCCATGCAGCCCTGGCAGCCGCTGGGCACCAAGTCCATCCTGGGCTACAACCTCAAGAAG
AGCATCGGGCAGCGGCACGCGCAGCTCTGCCGGCGCATGCTCACGCCCGAGATCCAGTAC
CTGATGGACCTCGGCGCCAACCTGTGGGTCACCAAGCTCTGGAAGTTCATTCGCGATTTC
CTGCGGTGGTGA

1. Honke K, Tsuda M, Hirahara Y, Ishii A, Makita A, Wada Y: Molecular cloning and expression of cDNA encoding human 3'-phosphoadenylylsulfate:galactosylceramide 3'-sulfotransferase. J Biol Chem. 1997 Feb 21;272(8):4864-8. [PubMed ]
2. Tsuda M, Egashira M, Niikawa N, Wada Y, Honke K: Cancer-associated alternative usage of multiple promoters of human GalCer sulfotransferase gene. Eur J Biochem. 2000 May;267(9):2672-9. [PubMed ]
3. Honke K, Yamane M, Ishii A, Kobayashi T, Makita A: Purification and characterization of 3'-phosphoadenosine-5'-phosphosulfate:GalCer sulfotransferase from human renal cancer cells. J Biochem (Tokyo). 1996 Mar;119(3):421-7. [PubMed ]

1. ASA
2. Cerebroside-sulfatase[Contains: Arylsulfatase A component B
3. Arylsulfatase A component C]

MGAPRSLLLALAAGLAVARPPNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFT
DFYVPVSLCTPSRAALLTGRLPVRMGMYPGVLVPSSRGGLPLEEVTVAEVLAARGYLTGM
AGKWHLGVGPEGAFLPPHQGFHRFLGIPYSHDQGPCQNLTCFPPATPCDGGCDQGLVPIP
LLANLSVEAQPPWLPGLEARYMAFAHDLMADAQRQDRPFFLYYASHHTHYPQFSGQSFAE
RSGRGPFGDSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPETMRMSRGGCSGLLRC
GKGTTYEGGVREPALAFWPGHIAPGVTHELASSLDLLPTLAALAGAPLPNVTLDGFDLSP
LLLGTGKSPRQSLFFYPSYPDEVRGVFAVRTGKYKAHFFTQGSAHSDTTADPACHASSSL
TAHEPPLLYDLSKDPGENYNLLGGVAGATPEVLQALKQLQLLKAQLDAAVTFGPSQVARG
EDPALQICCHPGCTPRPACCHCPDPHA

• Sphingolipid Metabolism (map00600 )

• A cerebroside 3-sulfate + H2O = a cerebroside + sulfate

• Sulfatase (PF00884 )

• 1-18

ATGGGGGCACCGCGGTCCCTCCTCCTGGCCCTGGCTGCTGGCCTGGCCGTTGCCCGTCCG
CCCAACATCGTGCTGATCTTTGCCGACGACCTCGGCTATGGGGACCTGGGCTGCTATGGG
CACCCCAGCTCTACCACTCCCAACCTGGACCAGCTGGCGGCGGGAGGGCTGCGGTTCACA
GACTTCTACGTGCCTGTGTCTCTGTGCACACCCTCTAGGGCCGCCCTCCTGACCGGCCGG
CTCCCGGTTCGGATGGGCATGTACCCTGGCGTCCTGGTGCCCAGCTCCCGGGGGGGCCTG
CCCCTGGAGGAGGTGACCGTGGCCGAAGTCCTGGCTGCCCGAGGCTACCTCACAGGAATG
GCCGGCAAGTGGCACCTTGGGGTGGGGCCTGAGGGGGCCTTCCTGCCCCCCCATCAGGGC
TTCCATCGATTTCTAGGCATCCCGTACTCCCACGACCAGGGCCCCTGCCAGAACCTGACC
TGCTTCCCGCCGGCCACTCCTTGCGACGGTGGCTGTGACCAGGGCCTGGTCCCCATCCCA
CTGTTGGCCAACCTGTCCGTGGAGGCGCAGCCCCCCTGGCTGCCCGGACTAGAGGCCCGC
TACATGGCTTTCGCCCATGACCTCATGGCCGACGCCCAGCGCCAGGATCGCCCCTTCTTC
CTGTACTATGCCTCTCACCACACCCACTACCCTCAGTTCAGTGGGCAGAGCTTTGCAGAG
CGTTCAGGCCGCGGGCCATTTGGGGACTCCCTGATGGAGCTGGATGCAGCTGTGGGGACC
CTGATGACAGCCATAGGGGACCTGGGGCTGCTTGAAGAGACGCTGGTCATCTTCACTGCA
GACAATGGACCTGAGACCATGCGTATGTCCCGAGGCGGCTGCTCCGGTCTCTTGCGGTGT
GGAAAGGGAACGACCTACGAGGGCGGTGTCCGAGAGCCTGCCTTGGCCTTCTGGCCAGGT
CATATCGCTCCCGGCGTGACCCACGAGCTGGCCAGCTCCCTGGACCTGCTGCCTACCCTG
GCAGCCCTGGCTGGGGCCCCACTGCCCAATGTCACCTTGGATGGCTTTGACCTCAGCCCC
CTGCTGCTGGGCACAGGCAAGAGCCCTCGGCAGTCTCTCTTCTTCTACCCGTCCTACCCA
GACGAGGTCCGTGGGGTTTTTGCTGTGCGGACTGGAAAGTACAAGGCTCACTTCTTCACC
CAGGGCTCTGCCCACAGTGATACCACTGCAGACCCTGCCTGCCACGCCTCCAGCTCTCTG
ACTGCTCATGAGCCCCCGCTGCTCTATGACCTGTCCAAGGACCCTGGTGAGAACTACAAC
CTGCTGGGGGGTGTGGCCGGGGCCACCCCAGAGGTGCTGCAAGCCCTGAAACAGCTTCAG
CTGCTCAAGGCCCAGTTAGACGCAGCTGTGACCTTCGGCCCCAGCCAGGTGGCCCGGGGC
GAGGACCCCGCCCTGCAGATCTGCTGTCATCCTGGCTGCACCCCCCGCCCAGCTTGCTGC
CATTGCCCAGATCCCCATGCCTGA

1. Stein C, Gieselmann V, Kreysing J, Schmidt B, Pohlmann R, Waheed A, Meyer HE, O'Brien JS, von Figura K: Cloning and expression of human arylsulfatase A. J Biol Chem. 1989 Jan 15;264(2):1252-9. [PubMed ]
2. Kreysing J, von Figura K, Gieselmann V: Structure of the arylsulfatase A gene. Eur J Biochem. 1990 Aug 17;191(3):627-31. [PubMed ]
3. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed ]
4. Fujii T, Kobayashi T, Honke K, Gasa S, Ishikawa M, Shimizu T, Makita A: Proteolytic processing of human lysosomal arylsulfatase A. Biochim Biophys Acta. 1992 Jul 13;1122(1):93-8. [PubMed ]
5. Schmidt B, Selmer T, Ingendoh A, von Figura K: A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency. Cell. 1995 Jul 28;82(2):271-8. [PubMed ]
6. Lukatela G, Krauss N, Theis K, Selmer T, Gieselmann V, von Figura K, Saenger W: Crystal structure of human arylsulfatase A: the aldehyde function and the metal ion at the active site suggest a novel mechanism for sulfate ester hydrolysis. Biochemistry. 1998 Mar 17;37(11):3654-64. [PubMed ]
7. von Bulow R, Schmidt B, Dierks T, von Figura K, Uson I: Crystal structure of an enzyme-substrate complex provides insight into the interaction between human arylsulfatase A and its substrates during catalysis. J Mol Biol. 2001 Jan 12;305(2):269-77. [PubMed ]
8. Gieselmann V, Zlotogora J, Harris A, Wenger DA, Morris CP: Molecular genetics of metachromatic leukodystrophy. Hum Mutat. 1994;4(4):233-42. [PubMed ]
9. Kappler J, von Figura K, Gieselmann V: Late-onset metachromatic leukodystrophy: molecular pathology in two siblings. Ann Neurol. 1992 Mar;31(3):256-61. [PubMed ]
10. Gieselmann V, Fluharty AL, Tonnesen T, Von Figura K: Mutations in the arylsulfatase A pseudodeficiency allele causing metachromatic leukodystrophy. Am J Hum Genet. 1991 Aug;49(2):407-13. [PubMed ]
11. Kondo R, Wakamatsu N, Yoshino H, Fukuhara N, Miyatake T, Tsuji S: Identification of a mutation in the arylsulfatase A gene of a patient with adult-type metachromatic leukodystrophy. Am J Hum Genet. 1991 May;48(5):971-8. [PubMed ]
12. Polten A, Fluharty AL, Fluharty CB, Kappler J, von Figura K, Gieselmann V: Molecular basis of different forms of metachromatic leukodystrophy. N Engl J Med. 1991 Jan 3;324(1):18-22. [PubMed ]
13. Honke K, Kobayashi T, Fujii T, Gasa S, Xu M, Takamaru Y, Kondo R, Tsuji S, Makita A: An adult-type metachromatic leukodystrophy caused by substitution of serine for glycine-122 in arylsulfatase A. Hum Genet. 1993 Nov;92(5):451-6. [PubMed ]
14. Kafert S, Heinisch U, Zlotogora J, Gieselmann V: A missense mutation P136L in the arylsulfatase A gene causes instability and loss of activity of the mutant enzyme. Hum Genet. 1995 Feb;95(2):201-4. [PubMed ]
15. Hasegawa Y, Kawame H, Eto Y: Mutations in the arylsulfatase A gene of Japanese patients with metachromatic leukodystrophy. DNA Cell Biol. 1993 Jul-Aug;12(6):493-8. [PubMed ]
16. Harvey JS, Nelson PV, Carey WF, Robertson EF, Morris CP: An arylsulfatase A (ARSA) missense mutation (T274M) causing late-infantile metachromatic leukodystrophy. Hum Mutat. 1993;2(4):261-7. [PubMed ]
17. Kreysing J, Bohne W, Bosenberg C, Marchesini S, Turpin JC, Baumann N, von Figura K, Gieselmann V: High residual arylsulfatase A (ARSA) activity in a patient with late-infantile metachromatic leukodystrophy. Am J Hum Genet. 1993 Aug;53(2):339-46. [PubMed ]
18. Gieselmann V, Polten A, Kreysing J, von Figura K: Arylsulfatase A pseudodeficiency: loss of a polyadenylylation signal and N-glycosylation site. Proc Natl Acad Sci U S A. 1989 Dec;86(23):9436-40. [PubMed ]
19. Barth ML, Fensom A, Harris A: Prevalence of common mutations in the arylsulphatase A gene in metachromatic leukodystrophy patients diagnosed in Britain. Hum Genet. 1993 Mar;91(1):73-7. [PubMed ]
20. Barth ML, Fensom A, Harris A: Missense mutations in the arylsulphatase A genes of metachromatic leukodystrophy patients. Hum Mol Genet. 1993 Dec;2(12):2117-21. [PubMed ]
21. Barth ML, Fensom A, Harris A: Identification of seven novel mutations associated with metachromatic leukodystrophy. Hum Mutat. 1995;6(2):170-6. [PubMed ]
22. Hess B, Kafert S, Heinisch U, Wenger DA, Zlotogora J, Gieselmann V: Characterization of two arylsulfatase A missense mutations D335V and T274M causing late infantile metachromatic leukodystrophy. Hum Mutat. 1996;7(4):311-7. [PubMed ]
23. Draghia R, Letourneur F, Drugan C, Manicom J, Blanchot C, Kahn A, Poenaru L, Caillaud C: Metachromatic leukodystrophy: identification of the first deletion in exon 1 and of nine novel point mutations in the arylsulfatase A gene. Hum Mutat. 1997;9(3):234-42. [PubMed ]
24. Regis S, Filocamo M, Stroppiano M, Corsolini F, Caroli F, Gatti R: A 9-bp deletion (2320del9) on the background of the arylsulfatase A pseudodeficiency allele in a metachromatic leukodystrophy patient and in a patient with nonprogressive neurological symptoms. Hum Genet. 1998 Jan;102(1):50-3. [PubMed ]
25. Gomez-Lira M, Perusi C, Mottes M, Pignatti PF, Manfredi M, Rizzuto N, Salviati A: Molecular genetic characterization of two metachromatic leukodystrophy patients who carry the T799G mutation and show different phenotypes; description of a novel null-type mutation. Hum Genet. 1998 Apr;102(4):459-63. [PubMed ]
26. Coulter-Mackie MB, Gagnier L: Two novel mutations in the arylsulfatase A gene associated with juvenile (R390Q) and adult onset (H397Y) metachromatic leukodystrophy. Hum Mutat. 1998;Suppl 1:S254-6. [PubMed ]
27. Ricketts MH, Poretz RD, Manowitz P: The R496H mutation of arylsulfatase A does not cause metachromatic leukodystrophy. Hum Mutat. 1998;12(4):238-9. [PubMed ]
28. Berger J, Gmach M, Mayr U, Molzer B, Bernheimer H: Coincidence of two novel arylsulfatase A alleles and mutation 459+1G>A within a family with metachromatic leukodystrophy: molecular basis of phenotypic heterogeneity. Hum Mutat. 1999;13(1):61-8. [PubMed ]
29. Marcao A, Amaral O, Pinto E, Pinto R, Sa Miranda MC: Metachromatic leucodystrophy in Portugal-finding of four new molecular lesions: C300F, P425T, g.1190-1191insC, and g.2408delC. Mutations in brief no. 232. Online. Hum Mutat. 1999;13(4):337-8. [PubMed ]

1. ASE

MLHLHHSCLCFRSWLPAMLAVLLSLAPSASSDISASRPNILLLMADDLGIGDIGCYGNNT
MRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQWTGASG
GLPTNETTFAKILKEKGYATGLIGKWHLGLNCESASDHCHHPLHHGFDHFYGMPFSLMGD
CARWELSEKRVNLEQKLNFLFQVLALVALTLVAGKLTHLIPVSWMPVIWSALSAVLLLAS
SYFVGALIVHADCFLMRNHTITEQPMCFQRTTPLILQEVASFLKRNKHGPFLLFVSFLHV
HIPLITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGSLEN
QLGNTQYGGWNGIYKGGKGMGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVR
LAGGEVPQDRVIDGQDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQRDRGTMWKVHFV
TPVFQPEGAGACYGRKVCPCFGEKVVHHDPPLLFDLSRDPSETHILTPASEPVFYQVMER
VQQAVWEHQRTLSPVPLQLDRLGNIWRPWLQPCCGPFPLCWCLREDDPQ

• Sulfatase (PF00884 )

• 1-31

• 200-222
• 227-249
• 289-311

ATGTTACATCTGCACCATTCTTGTTTGTGTTTCAGGAGCTGGCTGCCAGCGATGCTCGCT
GTACTGCTAAGTTTGGCACCATCAGCTTCCAGCGACATTTCCGCCTCCCGACCGAACATC
CTTCTTCTGATGGCGGACGACCTTGGCATTGGGGACATTGGCTGCTATGGCAACAACACC
ATGAGGACTCCGAATATTGACCGCCTTGCAGAGGACGGCGTGAAGCTGACCCAACACATC
TCTGCCGCATCTTTGTGCACCCCAAGCAGAGCCGCCTTCCTCACGGGCAGATACCCTGTG
CGATCAGGGATGGTTTCCAGCATTGGTTACCGTGTTCTTCAGTGGACCGGAGCATCTGGA
GGTCTTCCAACAAATGAGACAACTTTTGCAAAAATACTGAAAGAGAAAGGCTATGCCACT
GGACTCATTGGAAAATGGCATCTGGGTCTCAACTGTGAGTCAGCCAGTGATCATTGCCAC
CACCCTCTCCATCATGGCTTTGAGCATTTCTACGGAATGCCTTTCTCCTTGATGGGTGAT
TGCGCCCGCTGGGAACTCTCAGAGAAGCGTGTCAACCTGGAACAAAAACTCAACTTCCTC
TTCCAAGTCCTGGCCTTGGTTGCCCTCACACTGGTAGCAGGGAAGCTCACACACCTGATA
CCCGTCTCGTGGATGCCGGTCATCTGGTCAGCCCTTTCGGCCGTCCTCCTCCTCGCAAGC
TCCTATTTTGTGGGTGCTCTGATTGTCCATGCCGATTGCTTTCTGATGAGAAACCACACC
ATCACGGAGCAGCCCATGTGCTTCCAAAGAACGACACCCCTTATTCTGCAGGAGGTTGCG
TCCTTTCTCAAAAGGAATAAGCATGGGCCTTTCCTCCTCTTTGTTTCCTTTCTACACGTT
CACATCCCTCTTATCACTATGGAGAACTTCCTCGGGAAGAGTCTCCACGGGCTGTATGGG
GACAACGTAGAGGAGATGGACTGGATGGTAGGACGGATCCTTGACACTTTGGACGTGGAG
GGTTTGAGCAACAGCACCCTCATTTATTTTACGTCGGATCACGGCGGTTCCCTAGAGAAT
CAACTTGGAAACACCCAGTATGGTGGCTGGAATGGAATTTATAAAGGTGGGAAGGGCATG
GGAGGATGGGAAGGTGGGATCCGCGTGCCCGGGATCTTCCGCTGGCCCGGGGTGCTCCCG
GCCGGCCGAGTGATTGGCGAGCCCACGAGTCTGATGGACGTGTTCCCCACCGTGGTCCGG
CTGGCGGGCGGCGAGGTGCCCCAGGACAGAGTGATTGACGGCCAAGACCTTCTGCCCTTG
CTCCTGGGGACAGCCCAACACTCAGACCACGAGTTCCTGATGCATTATTGTGAGAGGTTT
CTGCACGCAGCCAGGTGGCATCAACGGGACAGAGGAACAATGTGGAAAGTCCACTTTGTG
ACGCCTGTGTTCCAGCCAGAGGGAGCCGGTGCCTGCTATGGAAGAAAGGTCTGCCCGTGC
TTTGGGGAAAAAGTAGTCCACCACGATCCACCTTTGCTCTTTGACCTCTCAAGAGACCCT
TCTGAGACCCACATCCTCACACCAGCCTCAGAGCCCGTGTTCTATCAGGTGATGGAACGA
GTCCAGCAGGCGGTGTGGGAACACCAGCGGACACTCAGCCCAGTTCCTCTGCAGCTGGAC
AGGCTGGGCAACATCTGGAGACCGTGGCTGCAGCCCTGCTGTGGCCCGTTCCCCCTCTGC
TGGTGCCTTAGGGAAGATGACCCACAATAA

1. Franco B, Meroni G, Parenti G, Levilliers J, Bernard L, Gebbia M, Cox L, Maroteaux P, Sheffield L, Rappold GA, et al.: A cluster of sulfatase genes on Xp22.3: mutations in chondrodysplasia punctata (CDPX) and implications for warfarin embryopathy. Cell. 1995 Apr 7;81(1):15-25. [PubMed ]
2. Daniele A, Parenti G, d'Addio M, Andria G, Ballabio A, Meroni G: Biochemical characterization of arylsulfatase E and functional analysis of mutations found in patients with X-linked chondrodysplasia punctata. Am J Hum Genet. 1998 Mar;62(3):562-72. [PubMed ]
3. Parenti G, Buttitta P, Meroni G, Franco B, Bernard L, Rizzolo MG, Brunetti-Pierri N, Ballabio A, Andria G: X-linked recessive chondrodysplasia punctata due to a new point mutation of the ARSE gene. Am J Med Genet. 1997 Dec 12;73(2):139-43. [PubMed ]

1. Forssman glycolipid synthetase-like protein

MHRRRLALGLGFCLLAGTSLSVLWVYLENWLPVSYVPYYLPCPEIFNMKLHYKREKPLQP
VVWSQYPQPKLLEHRPTQLLTLTPWLAPIVSEGTFNPELLQHIYQPLNLTIGVTVFAVGK
YTHFIQSFLESAEEFFMRGYRVHYYIFTDNPAAVPGVPLGPHRLLSSIPIQGHSHWEETS
MRRMETISQHIAKRAHREVDYLFCLDVDMVFRNPWGPETLGDLVAAIHPSYYAVPRQQFP
YERRRVSTAFVADSEGDFYYGGAVFGGQVARVYEFTRGCHMAILADKANGIMAAWREESH
LNRHFISNKPSKVLSPEYLWDDRKPQPPSLKLIRFSTLDKDISCLRS

• Glyco_transf_6 (PF03414 )

• 1-21

ATGCATCGCCGGAGACTGGCCCTGGGTCTGGGGTTCTGCCTGTTGGCGGGCACAAGCCTC
AGTGTCCTGTGGGTGTATCTTGAGAACTGGCTGCCAGTCTCCTATGTCCCCTATTATCTC
CCCTGCCCAGAGATCTTCAACATGAAGCTGCACTACAAGAGGGAGAAGCCACTCCAGCCC
GTGGTATGGTCACAGTACCCTCAGCCCAAGCTGCTGGAGCACAGGCCCACACAGCTGCTG
ACACTCACACCCTGGTTGGCGCCCATCGTCTCCGAGGGAACCTTCAACCCAGAGCTTCTG
CAGCACATCTACCAGCCACTGAACCTGACCATTGGGGTCACGGTGTTTGCCGTGGGGAAG
TACACTCATTTCATCCAGTCCTTCCTGGAGTCAGCCGAGGAGTTCTTCATGCGTGGGTAC
CGGGTGCACTACTACATCTTCACTGACAACCCTGCAGCCGTTCCCGGGGTCCCGCTGGGT
CCCCACCAGCTTCTCAGCTCCATCCCCATCCAGGGTCACTCCCACTGGGAGGAGACATCC
ATGCGCCGGATGGAGACCATCAGCCAGCACATTGCTAAGAGGGCTCACCGGGAGGTGGAC
TACTTTTTCTGCCTTGATGTGGACATGGTGTTTCGGAACCCGTGGGGCCCTGAGACCTTG
GGAGACCTGGTGGCTGCCATTCACCCAAGCTACTACGCCGTTCCCCGCCAGCAGTTCCCC
TATGAGCGCAGGCGTGTTTCCACTGCCTTTGTGGCAGACAGGGAAGGGGACTTCTATTAT
GGTGGGGCAGTCTTCGGGGGGCAGGTGGCCAGGGTATATGAGTTTACTAGGGGCTGCCAC
ATGGCCATCCTGGCGGACAAGGCCAATGGCATCATGGCTGCCTGGCGGGAGGAAAGCCAC
CTGAACCGTCACTTCATCTCAAACAAGCCGTCCAAGGTGCTGTCCCCCGAGTACCTCTGG
GACGACAGGAAGCCCCAGCCACCCAGCCTGAAGCTGATCCGCTTTTCTACACTGGACAAG
GATATCAGCTGCCTGAGGAGCTGA

1. Xu H, Storch T, Yu M, Elliott SP, Haslam DB: Characterization of the human Forssman synthetase gene. An evolving association between glycolipid synthesis and host-microbial interactions. J Biol Chem. 1999 Oct 8;274(41):29390-8. [PubMed ]
2. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed ]

1. Phosphatidylinositol-glycan biosynthesis class L protein
2. PIG-L

MEAMWLLCVALAVLAWGFLWVWDSSERMKSREQGGRLGAESRTLLVIAHPDDEAMFFAPT
VLGLARLRHWVYLLCFSAGNYYNQGETRKKELLQSCDVLGIPLSSVMIIDNRDFPDDPGM
QWDTEHVARVLLQHIEVNGINLVVTFDAGGVSGHSNHIALYAAVRALHSEGKLPKGCSVL
TLQSVNVLRKYISLLDLPLSLLHTQDVLFVLNSKEVAQAKKAMSCHRSQLLWFRRLYIIF
SRYMRINSLSFL

• 6-(N-acetyl-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O = 6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + acetate

• PIG-L (PF02585 )

• 1-17

ATGGAAGCAATGTGGCTCCTGTGTGTGGCGTTGGCGGTCTTGGCATGGGGCTTCCTCTGG
GTTTGGGACTCCTCAGAACGAATGAAGAGTCGGGAGCAGGGAGGACGGCTGGGAGCCGAA
AGCCGGACCCTGCTGGTCATAGCGCACCCTGACGATGAAGCCATGTTTTTTGCTCCCACA
GTGCTAGGCTTGGCCCGCCTAAGGCACTGGGTGTACCTGCTTTGCTTCTCTGCAGGAAAT
TACTACAATCAAGGAGAGACTCGTAAGAAAGAACTTTTGCAGAGCTGTGATGTTTTGGGG
ATTCCACTCTCCAGTGTAATGATTATTGACAACAGGGATTTCCCAGATGACCCAGGCATG
CAGTGGGACACAGAGCACGTGGCCAGAGTCCTCCTTCAGCACATAGAAGTGAATGGCATC
AATCTGGTGGTGACTTTCGATGCAGGGGGAGTAAGTGGCCACAGCAATCACATTGCTCTG
TATGCAGCTGTGAGGGCCCTGCACTCAGAAGGGAAGTTACCTAAAGGGTGCTCTGTGCTC
ACGCTTCAGTCTGTGAATGTGCTGCGCAAGTACATCTCCCTTCTGGATCTGCCCTTGTCT
CTGCTTCATACGCAGGATGTCCTCTTCGTGCTCAACAGCAAAGAAGTGGCACAGGCCAAG
AAAGCCATGTCCTGCCACCGCAGCCAGCTCCTCTGGTTCCGCCGCCTCTACATTATCTTC
TCCCGGTACATGAGAATCAACTCACTGAGCTTCCTCTGA

1. Watanabe R, Ohishi K, Maeda Y, Nakamura N, Kinoshita T: Mammalian PIG-L and its yeast homologue Gpi12p are N-acetylglucosaminylphosphatidylinositol de-N-acetylases essential in glycosylphosphatidylinositol biosynthesis. Biochem J. 1999 Apr 1;339 ( Pt 1):185-92. [PubMed ]

1. Acid sphingomyelinase
2. aSMase

MPRYGASLRQSCPRSGREQGQDGTAGAPGLLWMGLVLALALALALALSDSRVLWAPAEAH
PLSPQGHPARLHRIVPRLRDVFGWGNLTCPICKGLFTAINLGLKKEPNVARVGSVAIKLC
NLLKIAPPAVCQSIVHLFEDDMVEVWRRSVLSPSEACGLLLGSTCGHWDIFSSWNISLPT
VPKPPPKPPSPPAPGAPVSRILFLTDLHWDHDYLEGTDPDCADPLCCRRGSGLPPASRPG
AGYWGEYSKCDLPLRTLESLLSGLGPAGPFDMVYWTGDIPAHDVWHQTRQDQLRALTTVT
ALVRKFLGPVPVYPAVGNHESTPVNSFPPPFIEGNHSSRWLYEAMAKAWEPWLPAEALRT
LRIGGFYALSPYPGLRLISLNMNFCSRENFWLLINSTDPAGQLQWLVGELQAAEDRGDKV
HIIGHIPPGHCLKSWSWNYYRIVARYENTLAAQFFGHTHVDEFEVFYDEETLSRPLAVAF
LAPSATTYIGLNPGYRVYQIDGNYSRSSHVVLDHETYILNLTQANIPGAIPHWQLLYRAR
ETYGLPNTLPTAWHNLVYRMRGDMQLFQTFWFLYHKGHPPSEPCGTPCRLATLCAQLSAR
ADSPALCRHLMPDGSLPEAQSLWPRPLFC

• Sphingolipid Metabolism (map00600 )

• sphingomyelin + H2O = N-acylsphingosine + choline phosphate

• Metallophos (PF00149 )

• None

• 25-47

ATGCCCCGCTACGGAGCGTCACTCCGCCAGAGCTGCCCCAGGTCCGGCCGGGAGCAGGGA
CAAGACGGGACCGCCGGAGCCCCCGGACTCCTTTGGATGGGCCTGGTGCTGGCGCTGGCG
CTGGCGCTGGCGCTGGCTCTGTCTGACTCTCGGGTTCTCTGGGCTCCGGCAGAGGCTCAC
CCTCTTTCTCCCCAAGGCCATCCTGCCAGGTTACATCGCATAGTGCCCCGGCTCCGAGAT
GTCTTTGGGTGGGGGAACCTCACCTGCCCAATCTGCAAAGGTCTATTCACCGCCATCAAC
CTCGGGCTGAAGAAGGAACCCAATGTGGCTCGCGTGGGCTCCGTGGCCATCAAGCTGTGC
AATCTGCTGAAGATAGCACCACCTGCCGTGTGCCAATCCATTGTCCACCTCTTTGAGGAT
GACATGGTGGAGGTGTGGAGACGCTCAGTGCTGAGCCCATCTGAGGCCTGTGGCCTGCTC
CTGGGCTCCACCTGTGGGCACTGGGACATTTTCTCATCTTGGAACATCTCTTTGCCTACT
GTGCCGAAGCCGCCCCCCAAACCCCCTAGCCCCCCAGCCCCAGGTGCCCCTGTCAGCCGC
ATCCTCTTCCTCACTGACCTGCACTGGGATCATGACTACCTGGAGGGCACGGACCCTGAC
TGTGCAGACCCACTGTGCTGCCGCCGGGGTTCTGGCCTGCCGCCCGCATCCCGGCCAGGT
GCCGGATACTGGGGCGAATACAGCAAGTGTGACCTGCCCCTGAGGACCCTGGAGAGCCTG
TTGAGTGGGCTGGGCCCAGCCGGCCCTTTTGATATGGTGTACTGGACAGGAGACATCCCC
GCACATGATGTCTGGCACCAGACTCGTCAGGACCAACTGCGGGCCCTGACCACCGTCACA
GCACTTGTGAGGAAGTTCCTGGGGCCAGTGCCAGTGTACCCTGCTGTGGGTAACCATGAA
AGCATACCTGTCAATAGCTTCCCTCCCCCCTTCATTGAGGGCAACCACTCCTCCCGCTGG
CTCTATGAAGCGATGGCCAAGGCTTGGGAGCCCTGGCTGCCTGCCGAAGCCCTGCGCACC
CTCAGAATTGGGGGGTTCTATGCTCTTTCCCCATACCCCGGTCTCCGCCTCATCTCTCTC
AATATGAATTTTTGTTCCCGTGAGAACTTCTGGCTCTTGATCAACTCCACGGATCCCGCA
GGACAGCTCCAGTGGCTGGTGGGGGAGCTTCAGGCTGCTGAGGATCGAGGAGACAAAGTG
CATATAATTGGCCACATTCCCCCAGGGCACTGTCTGAAGAGCTGGAGCTGGAATTATTAC
CGAATTGTAGCCAGGTATGAGAACACCCTGGCTGCTCAGTTCTTTGGCCACACTCATGTG
GATGAATTTGAGGTCTTCTATGATGAAGAGACTCTGAGCCGGCCGCTGGCTGTAGCCTTC
CTGGCACCCAGTGCAACTACCTACATCGGCCTTAATCCTGGTTACCGTGTGTACCAAATA
GATGGAAACTACTCCAGGAGCTCTCACGTGGTCCTGGACCATGAGACCTACATCCTGAAT
CTGACCCAGGCAAACATACCGGGAGCCATACCGCACTGGCAGCTTCTCTACAGGGCTCGA
GAAACCTATGGGCTGCCCAACACACTGCCTACCGCCTGGCACAACCTGGTATATCGCATG
CGGGGCGACATGCAACTTTTCCAGACCTTCTGGTTTCTCTACCATAAGGGCCACCCACCC
TCGGAGCCCTGTGGCACGCCCTGCCGTCTGGCTACTCTTTGTGCCCAGCTCTCTGCCCGT
GCTGACAGCCCTGCTCTGTGCCGCCACCTGATGCCAGATGGGAGCCTCCCAGAGGCCCAG
AGCCTGTGGCCAAGGCCACTGTTTTGCTAG

1. Schuchman EH, Suchi M, Takahashi T, Sandhoff K, Desnick RJ: Human acid sphingomyelinase. Isolation, nucleotide sequence and expression of the full-length and alternatively spliced cDNAs. J Biol Chem. 1991 May 5;266(13):8531-9. [PubMed ]
2. Newrzella D, Stoffel W: Molecular cloning of the acid sphingomyelinase of the mouse and the organization and complete nucleotide sequence of the gene. Biol Chem Hoppe Seyler. 1992 Dec;373(12):1233-8. [PubMed ]
3. Schuchman EH, Levran O, Pereira LV, Desnick RJ: Structural organization and complete nucleotide sequence of the gene encoding human acid sphingomyelinase (SMPD1). Genomics. 1992 Feb;12(2):197-205. [PubMed ]
4. Ida H, Rennert OM, Eto Y, Chan WY: Cloning of a human acid sphingomyelinase cDNA with a new mutation that renders the enzyme inactive. J Biochem (Tokyo). 1993 Jul;114(1):15-20. [PubMed ]
5. Quintern LE, Schuchman EH, Levran O, Suchi M, Ferlinz K, Reinke H, Sandhoff K, Desnick RJ: Isolation of cDNA clones encoding human acid sphingomyelinase: occurrence of alternatively processed transcripts. EMBO J. 1989 Sep;8(9):2469-73. [PubMed ]
6. Ferlinz K, Hurwitz R, Moczall H, Lansmann S, Schuchman EH, Sandhoff K: Functional characterization of the N-glycosylation sites of human acid sphingomyelinase by site-directed mutagenesis. Eur J Biochem. 1997 Jan 15;243(1-2):511-7. [PubMed ]
7. Lansmann S, Schuette CG, Bartelsen O, Hoernschemeyer J, Linke T, Weisgerber J, Sandhoff K: Human acid sphingomyelinase. Eur J Biochem. 2003 Mar;270(6):1076-88. [PubMed ]
8. Ferlinz K, Hurwitz R, Sandhoff K: Molecular basis of acid sphingomyelinase deficiency in a patient with Niemann-Pick disease type A. Biochem Biophys Res Commun. 1991 Sep 30;179(3):1187-91. [PubMed ]
9. Levran O, Desnick RJ, Schuchman EH: Niemann-Pick disease: a frequent missense mutation in the acid sphingomyelinase gene of Ashkenazi Jewish type A and B patients. Proc Natl Acad Sci U S A. 1991 May 1;88(9):3748-52. [PubMed ]
10. Levran O, Desnick RJ, Schuchman EH: Niemann-Pick type B disease. Identification of a single codon deletion in the acid sphingomyelinase gene and genotype/phenotype correlations in type A and B patients. J Clin Invest. 1991 Sep;88(3):806-10. [PubMed ]
11. Levran O, Desnick RJ, Schuchman EH: Identification and expression of a common missense mutation (L302P) in the acid sphingomyelinase gene of Ashkenazi Jewish type A Niemann-Pick disease patients. Blood. 1992 Oct 15;80(8):2081-7. [PubMed ]
12. Takahashi T, Desnick RJ, Takada G, Schuchman EH: Identification of a missense mutation (S436R) in the acid sphingomyelinase gene from a Japanese patient with type B Niemann-Pick disease. Hum Mutat. 1992;1(1):70-1. [PubMed ]
13. Takahashi T, Suchi M, Desnick RJ, Takada G, Schuchman EH: Identification and expression of five mutations in the human acid sphingomyelinase gene causing types A and B Niemann-Pick disease. Molecular evidence for genetic heterogeneity in the neuronopathic and non-neuronopathic forms. J Biol Chem. 1992 Jun 25;267(18):12552-8. [PubMed ]
14. Sperl W, Bart G, Vanier MT, Christomanou H, Baldissera I, Steichen-Gersdorf E, Paschke E: A family with visceral course of Niemann-Pick disease, macular halo syndrome and low sphingomyelin degradation rate. J Inherit Metab Dis. 1994;17(1):93-103. [PubMed ]
15. Schuchman EH: Two new mutations in the acid sphingomyelinase gene causing type a Niemann-pick disease: N389T and R441X. Hum Mutat. 1995;6(4):352-4. [PubMed ]
16. Takahashi T, Suchi M, Sato W, Ten SB, Sakuragawa N, Desnick RJ, Schuchman EH, Takada G: Identification and expression of a missense mutation (Y446C) in the acid sphingomyelinase gene from a Japanese patient with type A Niemann-Pick disease. Tohoku J Exp Med. 1995 Oct;177(2):117-23. [PubMed ]
17. Ida H, Rennert OM, Maekawa K, Eto Y: Identification of three novel mutations in the acid sphinogomyelinase gene of Japanese patients with Niemann-Pick disease type A and B. Hum Mutat. 1996;7(1):65-7. [PubMed ]
18. Simonaro CM, Desnick RJ, McGovern MM, Wasserstein MP, Schuchman EH: The demographics and distribution of type B Niemann-Pick disease: novel mutations lead to new genotype/phenotype correlations. Am J Hum Genet. 2002 Dec;71(6):1413-9. Epub 2002 Oct 4. [PubMed ]
19. Sikora J, Pavlu-Pereira H, Elleder M, Roelofs H, Wevers RA: Seven novel acid sphingomyelinase gene mutations in Niemann-Pick type A and B patients. Ann Hum Genet. 2003 Jan;67(Pt 1):63-70. [PubMed ]

1. Glucosylceramide synthase
2. GCS
3. UDP-glucose:N-acylsphingosine D-glucosyltransferase
4. UDP- glucose ceramide glucosyltransferase
5. GLCT-1

MALLDLALEGMAVFGFVLFLVLWLMHFMAIIYTRLHLNKKATDKQPYSKLPGVSLLKPLK
GVDPNLINNLETFFELDYPKYEVLLCVQDHDDPAIDVCKKLLGKYPNVDARLFIGGKKVG
INPKINNLMPGYEVAKYDLIWICDSGIRVIPDTLTDMVNQMTEKVGLVHGLPYVADRQGF
AATLEQVYFGTSHPRYYISANVTGFKCVTGMSCLMRKDVLDQAGGLIAFAQYIAEDYFMA
KAIADRGWRFAMSTQVAMQNSGSYSISQFQSRMIRWTKLRINMLPATIICEPISECFVAS
LIIGWAAHHVFRWDIMVFFMCHCLAWFIFDYIQLRGVQGGTLCFSKLDYAVAWFIRESMT
IYIFLSALWDPTISWRTGRYRLRCGGTAEEILDV

• Sphingolipid Metabolism (map00600 )

• UDP-glucose + N-acylsphingosine = UDP + D-glucosyl-N-acylsphingosine

• Glycos_transf_2 (PF00535 )

• 1-29

ATGGCGCTGCTGGACCTGGCCTTGGAGGGAATGGCCGTCTTCGGGTTCGTCCTCTTCTTG
GTGCTGTGGCTGATGCATTTCATGGCTATCATCTACACCCGATTACACCTCAACAAGAAG
GCAACTGACAAACAGCCTTATAGCAAGCTCCCAGGTGTCTCTCTTCTGAAACCACTGAAA
GGGGTAGATCCTAACTTAATCAACAACCTGGAAACATTCTTTGAATTGGATTATCCCAAA
TATGAAGTGCTCCTTTGTGTACAAGATCATGATGATCCAGCCATTGATGTATGTAAGAAG
CTTCTTGGAAAATATCCAAATGTTGATGCTAGATTGTTTATAGGTGGTAAAAAAGTTGGC
ATTAATCCTAAAATTAATAATTTAATGCCAGGATATGAAGTTGCAAAGTATGATCTTATA
TGGATTTGTGATAGTGGAATAAGAGTAATTCCAGATACGCTTACTGACATGGTGAATCAA
ATGACAGAAAAAGTAGGCTTGGTTCACGGGCTGCCTTACGTAGCAGACAGACAGGGCTTT
GCTGCCACCTTAGAGCAGGTATATTTTGGAACTTCACATCCAAGATACTATATCTCTGCC
AATGTAACTGGTTTCAAATGTGTGACAGGAATGTCTTGTTTAATGAGAAAAGATGTGTTG
GATCAAGCAGGAGGACTTATAGCTTTTGCTCAGTACATTGCCGAAGATTACTTTATGGCC
AAAGCGATAGCTGACCGAGGTTGGAGGTTTGCAATGTCCACTCAAGTTGCAATGCAAAAC
TCTGGCTCATATTCAATTTCTCAGTTTCAATCCAGAATGATCAGGTGGACCAAACTACGA
ATTAACATGCTTCCTGCTACAATAATTTGTGAGCCAATTTCAGAATGCTTTGTTGCCAGT
TTAATTATTGGATGGGCAGCCCACCATGTGTTCAGATGGGATATTATGGTATTTTTCATG
TGTCATTGCCTGGCATGGTTTATATTTGACTACATTCAACTCAGGGGTGTCCAGGGTGGC
ACACTGTGTTTTTCAAAACTTGATTATGCAGTCGCCTGGTTCATCCGCGAATCCATGACA
ATATACATTTTTTTGTCTGCATTATGGGACCCAACTATAAGCTGGAGAACTGGTCGCTAC
AGATTACGCTGTGGGGGTACAGCAGAGGAAATCCTAGATGTATAA

1. Ichikawa S, Sakiyama H, Suzuki G, Hidari KI, Hirabayashi Y: Expression cloning of a cDNA for human ceramide glucosyltransferase that catalyzes the first glycosylation step of glycosphingolipid synthesis. Proc Natl Acad Sci U S A. 1996 May 14;93(10):4638-43. [PubMed ]
2. Ichikawa S, Sakiyama H, Suzuki G, Hidari KI, Hirabayashi Y: Expression cloning of a cDNA for human ceramide glucosyltransferase that catalyzes the first glycosylation step of glycosphingolipid synthesis. Proc Natl Acad Sci U S A. 1996 Oct 29;93(22):12654. [PubMed ]

1. Alpha- 1,4-galactosyltransferase
2. UDP-galactose:beta-D-galactosyl-beta1-R 4- alpha-D-galactosyltransferase
3. Alpha-1,4-N- acetylglucosaminyltransferase
4. Alpha4Gal-T1
5. Globotriaosylceramide synthase
6. Gb3 synthase
7. CD77 synthase
8. P1/Pk synthase

MSKPPDLLLRLLRGAPRQRVCTLFIIGFKFTFFVSIMIYWHVVGEPKEKGQLYNLPAEIP
CPTLTPPTPPSHGPTPGNIFFLETSDRTNPNFLFMCSVESAARTHPESHVLVLMKGLPGG
NASLPRHLGISLLSCFPNVQMLPLDLRELFRDTPLADWYAAVQGRWEPYLLPVLSDASRI
ALMWKFGGIYLDTDFIVLKNLRNLTNVLGTQSRYVLNGAFLAFERRHEFMALCMRDFVDH
YNGWIWGHQGPQLLTRVFKKWCSIRSLAESRACRGVTTLPPEAFYPIPWQDWKKYFEDIN
PEELPRLLSATYAVHVWNKKSQGTRFEATSRALLAQLHARYCPTTHEAMKMYL

• Globoside metabolism (map00603 )

• UDP-galactose + beta-D-galactosyl-(1->4)-D-glucosylceramide = UDP + alpha-D-galactosyl-(1->4)-beta-D-galactosyl-(1->4)-D-glucosylceramide

• Gb3_synth (PF04572 )
• Gly_transf_sug (PF04488 )

• None

• 23-43

ATGTCCAAGCCCCCCGACCTCCTGCTGCGGCTGCTCCGGGGCGCCCCAAGGCAGCGGGTC
TGCACCCTGTTCATCATCGGCTTCAAGTTCACGTTTTTCGTCTCCATCATGATCTACTGG
CACGTTGTGGGAGAGCCCAAGGAGAAAGGGCAGCTCTATAACCTGCCAGCAGAGATCCCC
TGCCCCACCTTGACACCCCCCACCCCACCCTCCCACGGCCCCACTCCAGGCAACATCTTC
TTCCTGGAGACTTCAGACCGGACCAACCCCAACTTCCTGTTCATGTGCTCGGTGGAGTCG
GCCGCCAGAACTCACCCCGAATCCCACGTGCTGGTCCTGATGAAAGGGCTTCCGGGTGGC
AACGCCTCTCTGCCCCGGCACCTGGGCATCTCACTTCTGAGCTGCTTCCCGAATGTCCAG
ATGCTCCCGCTGGACCTGCGGGAGCTGTTCCGGGACACACCCCTGGCCGACTGGTACGCG
GCCGTGCAGGGGCGCTGGGAGCCCTACCTGCTGCCCGTGCTCTCCGACGCCTCCAGGATC
GCACTCATGTGGAAGTTCGGCGGCATCTACCTGGACACGGACTTCATTGTTCTCAAGAAC
CTGCGGAACCTGACCAACGTGCTGGGCACCCAGTCCCGCTACGTCCTCAACGGCGCGTTC
CTGGCCTTCGAGCGCCGGCACGAGTTCATGGCGCTGTGCATGCGGGACTTCGTGGACCAC
TACAACGGCTGGATCTGGGGTCACCAGGGCCCGCAGCTGCTCACGCGGGTCTTCAAGAAG
TGGTGTTCCATCCGCAGCCTGGCCGAGAGCCGCGCCTGCCGCGGCGTCACCACCCTGCCC
CCTGAGGCCTTCTACCCCATCCCCTGGCAGGACTGGAAGAAGTACTTTGAGGACATCAAC
CCGGAGGAGCTGCCGCGGCTGCTCAGTGCCACCTATGCTGTCCACGTGTGGAACAAGAAG
AGCCAGGGCACGCGGTTCGAGGCCACGTCCAGGGCACTGCTGGCCCAGCTGCATGCCCGC
TACTGCCCCACGACGCACGAGGCCATGAAAATGTACTTGTGA

1. Kojima Y, Fukumoto S, Furukawa K, Okajima T, Wiels J, Yokoyama K, Suzuki Y, Urano T, Ohta M, Furukawa K: Molecular cloning of globotriaosylceramide/CD77 synthase, a glycosyltransferase that initiates the synthesis of globo series glycosphingolipids. J Biol Chem. 2000 May 19;275(20):15152-6. [PubMed ]
2. Steffensen R, Carlier K, Wiels J, Levery SB, Stroud M, Cedergren B, Nilsson Sojka B, Bennett EP, Jersild C, Clausen H: Cloning and expression of the histo-blood group Pk UDP-galactose: Ga1beta-4G1cbeta1-cer alpha1, 4-galactosyltransferase. Molecular genetic basis of the p phenotype. J Biol Chem. 2000 Jun 2;275(22):16723-9. [PubMed ]
3. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed ]

1. Phosphatidylinositol-glycan biosynthesis class Q protein
2. PIG-Q
3. N-acetylglucosamyl transferase component GPI1

MVLKAFFPTCCVSTDSGLLVGRWVPEQSSAVVLAVLHFPFIPIQVKQLLAQVRQASQVGV
AVLGTWCHCRQEPEESLGRFLESLGAVFPHEPWLRLCRERGGTFWSCEATHRQAPTAPGA
PGEDQVMLIFYDQRQVLLSQLHLPTVLPDRQAGATTASTGGLAAVFDTVARSEVLFRSDR
FDEGPVRLSHWQSEGVEASILAELARRASGPICLLLASLLSLVSAVSACRVFKLWPLSFL
GSKLSTCEQLRHRLEHLTLIFSTRKAENPAQLMRKANTVASVLLDVALGLMLLSWLHGRS
RIGHLADALVPVADHVAEELQHLLQWLMGAPAGLKMNRALDQVLGRFFLYHIHLWISYIH
LMSPFVEHILWHVGLSACLGLTVALSLLSDIIALLTFHIYCFYVYGARLYCLKIHGLSSL
WRLFRGKKWNVLRQRVDSCSYDLDQLFIGTLLFTILLFLLPTTALYYLVFTLLRLLVVAV
QGLIHLLVDLINSLPLYSLGLRLCRPYRLADKPTALQPRGAHLPPPQLWLPPQALLGRPV
PQAVPWGAHLPLEAERGQAGLRELLARLAPPHGHSQPSALPGWHQLSWRMSCALWTLLCA
PEHGRPCYHTLGLEVIGSEQMWGWPARLAALHHWHCLPWDPLPTCCGHHGGEHSNPRCPE
HCPMPTLCTQVQRVRPPQQPQVEGWSPWGLPSGSALAVGVEGPCQDEPPSPRHPLAPSAE
QHPASGGLKQSLTPVPSGPGPSLPEPHGVYLRMFPGEVAL

• UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol

• Gpi1 (PF05024 )

• None

• 278-298 349-371 378-400 446-468 475-497

ATGGTGCTCAAGGCCTTCTTCCCCACGTGCTGCGTCTCGGCGGACAGCGGGCTGCTGGTG
GGACGGTGGGTGCCGGAGCAGAGCAGCGCCGTGGTCCTGGCGGTCCTGCACTTTCCCTTC
ATCCCCATCCAGGTCAAGCAGCTCCTGGCCCAGGTGCGGCAGGCCAGCCAGGTGGGCGTG
GCCGTGCTGGGCACCTGGTGCCACTGCCGGCAGGAGCCCGAGGAGAGCCTGGGCCGCTTC
CTGGAGAGCCTGGGTGCTGTCTTCCCCCATGAGCCCTGGCTGCGGCTGTGCCGGGAGAGA
GGCGGCACGTTCTGGAGCTGCGAGGCCACCCACCGGCAAGCGCCCACTGCCCCCGGTGCC
CCTGGTGAGGACCAGGTCATGCTCATCTTCTATGACCAGCGCCAGGTGTTGCTGTCACAG
CTACACCTGCCCACCGTCCTGCCCGACCGCCAGGCTGGAGCCACCACTGCCAGCACGGGG
GGCCTGGCTGCCGTCTTCGACACGGTAGCACGCAGTGAGGTGCTCTTCCGCAGTGACCGC
TTTGATGAGGGCCCCGTGCGGCTGAGCCACTGGCAGTCGGAGGGCGTGGAGGCCAGCATC
CTCGCGGAGCTGGCCAGGCGAGCCTCGGGACCCATTTGTCTGCTGTTGGCCAGCCTGCTG
TCGCTGGTCTCAGCTGTCAGTGCCTGCCGAGTGTTCAAGCTCTGGCCCCTGTCCTTCCTC
GGGAGCAAACTCTCCACGTGCGAACAGCTCCGGCACCGGCTGGAGCACCTCACGCTAATC
TTCAGTACACGGAAGGCGGAGAACCCTGCCCAGCTGATGAGGAAGGCCAACACGGTGGCC
TCTGTGCTGCTGGACGTGGCCCTGGGCCTCATGCTGCTGTCCTGGCTCCACGGGAGAAGC
CGCATCGGGCATCTGGCCGACGCCCTCGTTCCTGTGGCTGACCACGTGGCCGAGGAGCTC
CAGCATCTGCTGCAGTGGCTGATGGGTGCTCCCGCCGGGCTCAAGATGAACCGTGCACTG
GACCAGGTGCTGGGCCGCTTCTTCCTCTACCACATCCACCTGTGGATCAGCTACATCCAC
CTCATGTCCCCCTTCGTGGAGCACATCCTTTGGCACGTGGGCCTCTCGGCCTGCCTGGGC
CTGACGGTGGCCCTGTCCCTCCTCTCGGACATTATCGCCCTCCTCACCTTCCACATCTAC
TGCTTTTACGTCTATGGAGCCAGGCTGTACTGCCTGAAGATCCATGGCCTGTCCTCACTG
TGGCGTCTGTTCCGGGGGAAGAAGTGGAACGTTCTGCGCCAGCGCGTGGACTCCTGTTCC
TATGACCTGGACCAGCTGTTCATCGGGACTCTGCTCTTCACCATCCTGCTCTTCCTCCTG
CCTACCACAGCCCTGTACTACCTGGTGTTCACCCTGCTCCGGCTCCTGGTGGTCGCCGTG
CAGGGCCTGATCCATCTGCTGGTGGACCTCATCAACTCCCTGCCGCTGTACTCACTGGGT
CTTCGGCTCTGCCGGCCCTACAGGCTGGCGGCTGGCGTGAAGTTCCGTGTCCTCCGGCAC
GAGGCCAGCAGGCCCCTCCGCCTCCTGATGCAGATAAACCCACTGCCCTACAGCCGCGTG
GTGCACACCTACCGCCTCCCCAGCTGTGGCTGCCACCCCAAGCACTCCTGGGGCGCCCTG
TGCCGCAAGCTGTTCCTTGGGGAGCTCATCTACCCCTGGAGGCAGAGAGGGGACAAGCAG
GACTGA

1. Tiede A, Schubert J, Nischan C, Jensen I, Westfall B, Taron CH, Orlean P, Schmidt RE: Human and mouse Gpi1p homologues restore glycosylphosphatidylinositol membrane anchor biosynthesis in yeast mutants. Biochem J. 1998 Sep 15;334 ( Pt 3):609-16. [PubMed ]
2. Watanabe R, Inoue N, Westfall B, Taron CH, Orlean P, Takeda J, Kinoshita T: The first step of glycosylphosphatidylinositol biosynthesis is mediated by a complex of PIG-A, PIG-H, PIG-C and GPI1. EMBO J. 1998 Feb 16;17(4):877-85. [PubMed ]
3. Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [PubMed ]
4. Watanabe R, Murakami Y, Marmor MD, Inoue N, Maeda Y, Hino J, Kangawa K, Julius M, Kinoshita T: Initial enzyme for glycosylphosphatidylinositol biosynthesis requires PIG-P and is regulated by DPM2. EMBO J. 2000 Aug 15;19(16):4402-11. [PubMed ]

1. GlcNAc-PI synthesis protein
2. Phosphatidylinositol- glycan biosynthesis class A protein
3. PIG-A

MACRGGAGNGHRASATLSRVSPGSLYTCRTRTHNICMVSDFFYPNMGGVESHIYQLSQCL
IERGHKVIIVTHAYGNRKGIRYLTSGLKVYYLPLKVMYNQSTATTLFHSLPLLRYIFVRE
RVTIIHSHSSFSAMAHDALFHAKTMGLQTVFTDHSLFGFADVSSVLTNKLLTVSLCDTNH
IICVSYTSKENTVLRAALNPEIVSVIPNAVDPTDFTPDPFRRHDSITIVVVSRLVYRKGI
DLLSGIIPELCQKYPDLNFIIGGEGPKRIILEEVRERYQLHDRVRLLGALEHKDVRNVLV
QGHIFLNTSLTEAFCMAIVEAASCGLQVVSTRVGGIPEVLPENLIILCEPSVKSLCEGLE
KAIFQLKSGTLPAPENIHNIVKTFYTWRNVAERTEKVYDRVSVEAVLPMDKRLDRLISHC
GPVTGYIFALLAVFNFLFLIFLRWMTPDSIIDVAIDATGPRGAWTNNYSHSKRGGENNEI
SETR

• UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol

• Glycos_transf_1 (PF00534 )
• PIGA (PF08288 )

• None

• 422-442

ATGGCCTGTAGAGGAGGAGCTGGGAATGGCCACCGTGCCTCAGCTACACTCTCTCGGGTT
AGCCCTGGAAGTCTTTACACATGTAGAACCCGTACCCATAATATATGCATGGTATCTGAC
TTTTTCTACCCAAATATGGGAGGCGTGGAAAGCCACATTTACCAGCTCTCTCAGTGCCTG
ATTGAAAGAGGGCATAAGGTTATAATTGTCACCCATGCTTATGGAAATCGAAAAGGCATC
CGTTACCTCACCAGTGGCCTCAAAGTCTATTACTTGCCTCTGAAAGTCATGTACAACCAG
TCTACAGCCACGACCCTCTTTCACAGTCTGCCATTGCTCAGGTACATATTTGTTCGGGAG
AGAGTCACGATAATCCATTCACATAGTTCTTTTTCTGCTATGGCCCATGATGCTCTCTTC
CACGCCAAGACAATGGGGCTTCAGACAGTCTTCACGGACCATTCCCTTTTTGGATTTGCT
GATGTCAGCTCGGTGCTTACAAACAAGCTTCTAACCGTGTCTCTTTGTGATACAAACCAC
ATCATTTGTGTGTCTTATACTAGTAAGGAAAATACTGTACTAAGAGCAGCACTGAATCCT
GAAATAGTGTCCGTCATTCCTAATGCTGTAGATCCTACTGACTTCACTCCAGACCCATTT
AGAAGGCATGATAGTATAACTATTGTTGTTGTCAGCAGACTTGTTTACAGAAAAGGGATC
GATTTGCTTAGTGGTATAATACCTGAACTCTGTCAGAAATATCCAGATTTAAATTTCATA
ATTGGAGGAGAGGGACCAAAGAGAATCATTTTGGAAGAAGTTCGGGAAAGATACCAGCTG
CATGACAGGGTGCGTCTTTTGGGAGCTTTAGAACACAAGGATGTTAGAAATGTCTTAGTT
CAAGGACATATTTTTCTGAATACCTCCCTTACTGAAGCATTCTGCATGGCGATCGTGGAA
GCAGCCAGTTGTGGTTTACAGGTTGTAAGTACCAGAGTTGGTGGAATTCCTGAGGTGCTT
CCAGAAAACCTTATTATTTTATGTGAGCCTTCAGTAAAATCTTTGTGTGAAGGATTGGAA
AAGGCTATTTTCCAACTGAAGTCAGGGACATTGCCAGCTCCAGAAAACATCCATAACATA
GTAAAGACTTTCTACACCTGGAGGAATGTTGCAGAAAGAACTGAAAAGGTATATGACCGG
GTATCAGTGGAAGCTGTGTTGCCAATGGACAAACGACTGGACAGACTTATTTCTCACTGC
GGCCCAGTAACAGGCTACATCTTTGCTTTGTTGGCAGTTTTCAACTTCCTCTTCCTCATT
TTCTTGAGATGGATGACTCCAGATTCTATCATTGATGTTGCAATAGATGCCACTGGGCCA
CGGGGTGCCTGGACTAATAACTATTCTCACAGTAAAAGAGGGGGTGAGAATAATGAGATA
TCTGAAACCAGGTAG

1. Miyata T, Takeda J, Iida Y, Yamada N, Inoue N, Takahashi M, Maeda K, Kitani T, Kinoshita T: The cloning of PIG-A, a component in the early step of GPI-anchor biosynthesis. Science. 1993 Feb 26;259(5099):1318-20. [PubMed ]
2. Bessler M, Hillmen P, Longo L, Luzzatto L, Mason PJ: Genomic organization of the X-linked gene (PIG-A) that is mutated in paroxysmal nocturnal haemoglobinuria and of a related autosomal pseudogene mapped to 12q21. Hum Mol Genet. 1994 May;3(5):751-7. [PubMed ]
3. Iida Y, Takeda J, Miyata T, Inoue N, Nishimura J, Kitani T, Maeda K, Kinoshita T: Characterization of genomic PIG-A gene: a gene for glycosylphosphatidylinositol-anchor biosynthesis and paroxysmal nocturnal hemoglobinuria. Blood. 1994 Jun 1;83(11):3126-31. [PubMed ]
4. Yu J, Nagarajan S, Ueda E, Knez JJ, Petersen RB, Medof ME: Characterization of alternatively spliced PIG-A transcripts in normal and paroxysmal nocturnal hemoglobinuria cells. Braz J Med Biol Res. 1994 Feb;27(2):195-201. [PubMed ]
5. Takeda J, Miyata T, Kawagoe K, Iida Y, Endo Y, Fujita T, Takahashi M, Kitani T, Kinoshita T: Deficiency of the GPI anchor caused by a somatic mutation of the PIG-A gene in paroxysmal nocturnal hemoglobinuria. Cell. 1993 May 21;73(4):703-11. [PubMed ]
6. Bessler M, Mason PJ, Hillmen P, Miyata T, Yamada N, Takeda J, Luzzatto L, Kinoshita T: Paroxysmal nocturnal haemoglobinuria (PNH) is caused by somatic mutations in the PIG-A gene. EMBO J. 1994 Jan 1;13(1):110-7. [PubMed ]
7. Ware RE, Rosse WF, Howard TA: Mutations within the Piga gene in patients with paroxysmal nocturnal hemoglobinuria. Blood. 1994 May 1;83(9):2418-22. [PubMed ]
8. Nafa K, Bessler M, Castro-Malaspina H, Jhanwar S, Luzzatto L: The spectrum of somatic mutations in the PIG-A gene in paroxysmal nocturnal hemoglobinuria includes large deletions and small duplications. Blood Cells Mol Dis. 1998 Sep;24(3):370-84. [PubMed ]
9. Yoon JH, Cho HI, Park SS, Chang YH, Kim BK: Mutation analysis of the PIG-A gene in Korean patients with paroxysmal nocturnal haemoglobinuria. J Clin Pathol. 2002 Jun;55(6):410-3. [PubMed ]

1. Phosphatidylinositol-glycan biosynthesis class H protein
2. PIG-H

MEDERSFSDICGGRLALQRRYYSPSCREFCLSCPRLSLRSLTAVTCTVWLAAYGLFTLCE
NSMILSAAIFITLLGLLGYLHFVKIDQETLLIIDSLGIQMTSSYASGKESTTFIEMGKVK
DIVINEAIYMQKVIYYLCILLKDPVEPHGISQVVPVFQSAKPRLDCLIEVYRSCQEILAH
QKATSTSP

• UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol

• None

• 36-58
• 63-83

ATGGAGGATGAGCGGAGCTTTTCGGATATCTGCGGCGGCCGCCTGGCGCTGCAGCGCCGC
TACTACTCCCCGTCCTGCCGGGAATTCTGCCTCAGCTGCCCTCGGCTCTCGCTGCGTTCG
CTCACCGCTGTCACCTGCACGGTGTGGCTGGCGGCCTACGGACTCTTCACCCTCTGCGAG
AACAGCATGATCCTCTCTGCTGCCATCTTCATCACCCTCTTAGGTCTGCTTGGTTATCTC
CATTTTGTGAAGATTGATCAGGAGACTCTGTTAATCATTGATTCCCTTGGCATTCAGATG
ACTTCATCTTATGCTTCAGGCAAAGAAAGCACTACCTTCATAGAAATGGGCAAGGTCAAG
GATATTGTCATCAATGAGGCCATTTACATGCAGAAGGTGATTTACTACCTCTGCATCTTA
TTGAAAGATCCAGTGGAACCACATGGGATATCCCAAGTAGTACCCGTCTTCCAGAGTGCC
AAGCCCCGGCTGGACTGCTTGATTGAAGTATACAGGAGCTGCCAGGAGATCCTGGCACAC
CAGAAAGCCACATCAACAAGCCCATGA

1. Kamitani T, Chang HM, Rollins C, Waneck GL, Yeh ET: Correction of the class H defect in glycosylphosphatidylinositol anchor biosynthesis in Ltk- cells by a human cDNA clone. J Biol Chem. 1993 Oct 5;268(28):20733-6. [PubMed ]
2. Watanabe R, Inoue N, Westfall B, Taron CH, Orlean P, Takeda J, Kinoshita T: The first step of glycosylphosphatidylinositol biosynthesis is mediated by a complex of PIG-A, PIG-H, PIG-C and GPI1. EMBO J. 1998 Feb 16;17(4):877-85. [PubMed ]

1. Phosphatidylinositol-glycan biosynthesis class P protein
2. PIG-P
3. Down syndrome critical region protein 5
4. Down syndrome critical region protein C

MVPRSTSLTLIVFLFHRLSKAPGKMVENSPSPLPERAIYGFVLFLSSQFGFILYLVWAFI
PESWLNSLGLTYWPQKYWAVALPVYLLIAIVIGYVLLFGINMMSTSPLDSIHTITDNYAK
NQQQKKYQEEAIPALRDISISEVNQMFFLAAKELYTKN

• UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol

• PIG-P (PF08510 )

• 1-23

• 40-60 80-100

ATGGTGGAAAATTCACCGTCGCCATTGCCAGAAAGAGCGATTTATGGCTTTGTTCTTTTC
TTAAGCTCCCAATTTGGCTTCATACTTTACCTCGTGTGGGCCTTTATTCCTGAATCTTGG
CTAAACTCTTTAGGTTTAACCTATTGGCCTCAAAAATATTGGGCAGTTGCATTACCTGTC
TACCTCCTTATTGCTATAGTAATTGGCTACGTGCTCTTGTTTGGGATTAACATGATGAGT
ACCTCTCCACTCGACTCCATCCATACAATCACAGATAACTATGCAAAAAATCAACAGCAG
AAGAAATACCAAGAGGAGGCCATTCCAGCCTTAAGAGATATTTCTATTAGTGAAGTAAAC
CAAATGTTCTTTCTTGCAGCCAAAGAACTTTACACCAAAAACTGA

1. Shibuya K, Kudoh J, Minoshima S, Kawasaki K, Asakawa S, Shimizu N: Isolation of two novel genes, DSCR5 and DSCR6, from Down syndrome critical region on human chromosome 21q22.2. Biochem Biophys Res Commun. 2000 May 19;271(3):693-8. [PubMed ]
2. Togashi T, Choi DK, Taylor TD, Suzuki Y, Sugano S, Hattori M, Sakaki Y: A novel gene, DSCR5, from the distal Down syndrome critical region on chromosome 21q22.2. DNA Res. 2000 Jun 30;7(3):207-12. [PubMed ]
3. Watanabe R, Murakami Y, Marmor MD, Inoue N, Maeda Y, Hino J, Kangawa K, Julius M, Kinoshita T: Initial enzyme for glycosylphosphatidylinositol biosynthesis requires PIG-P and is regulated by DPM2. EMBO J. 2000 Aug 15;19(16):4402-11. [PubMed ]
4. Hattori M, Fujiyama A, Taylor TD, Watanabe H, Yada T, Park HS, Toyoda A, Ishii K, Totoki Y, Choi DK, Groner Y, Soeda E, Ohki M, Takagi T, Sakaki Y, Taudien S, Blechschmidt K, Polley A, Menzel U, Delabar J, Kumpf K, Lehmann R, Patterson D, Reichwald K, Rump A, Schillhabel M, Schudy A, Zimmermann W, Rosenthal A, Kudoh J, Schibuya K, Kawasaki K, Asakawa S, Shintani A, Sasaki T, Nagamine K, Mitsuyama S, Antonarakis SE, Minoshima S, Shimizu N, Nordsiek G, Hornischer K, Brant P, Scharfe M, Schon O, Desario A, Reichelt J, Kauer G, Blocker H, Ramser J, Beck A, Klages S, Hennig S, Riesselmann L, Dagand E, Haaf T, Wehrmeyer S, Borzym K, Gardiner K, Nizetic D, Francis F, Lehrach H, Reinhardt R, Yaspo ML: The DNA sequence of human chromosome 21. Nature. 2000 May 18;405(6784):311-9. [PubMed ]

1. Phosphatidylinositol-glycan biosynthesis class C protein
2. PIG-C

MYAQPVTNTKEVKWQKVLYERQPFPDNYVDRRFLEELRKNIHARKYQYWAVVFESSVVIQ
QLCSVCVFVVIWWYMDEGLLAPHWLLGTGLASSLIGYVLFDLIDGGEGRKKSGQTRWADL
KSALVFITFTYGFSPVLKTLTESVSTDTIYAMSVFMLLGHLIFFDYGANAAIVSSTLSLN
MAIFASVCLASRLPRSLHAFIMVTFAIQIFALWPMLQKKLKACTPRSYVGVTLLFAFSAV
GGLLSISAVGAVLFALLLMSISCLCPFYLIRLQLFKENIHGPWDEAEIKEDLSRFLS

• UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol

• GPI2 (PF06432 )

• None

• 51-71 80-100 154-174 239-259

ATGTATGCTCAACCTGTGACTAACACCAAGGAGGTCAAGTGGCAGAAGGTCTTGTATGAG
CGACAGCCCTTTCCTGATAACTATGTGGACCGGCGATTCCTGGAAGAGCTCCGGAAAAAC
ATCCATGCTCGGAAATACCAATATTGGGCTGTGGTATTTGAGTCCAGTGTGGTGATCCAG
CAGCTGTGCAGTGTTTGTGTTTTTGTGGTTATCTGGTGGTATATGGATGAGGGTCTTCTG
GCCCCCCATTGGCTTTTAGGGACTGGCCTGGCTTCTTCACTGATTGGGTATGTTTTGTTT
GATCTCATTGATGGAGGTGAAGGGCGGAAGAAGAGTGGGCAGACCCGGTGGGCTGACCTG
AAGAGTGCCCTAGTCTTCATTACTTTCACTTATGGGTTTTCACCAGTGCTGAAGACCCTT
ACAGAGTCTGTCAGCACTGACACCATCTATGCCATGTCAGTCTTCATGCTGTTAGGCCAT
CTCATCTTTTTTGACTATGGTGCCAATGCTGCCATTGTATCCAGCACACTATCCTTGAAC
ATGGCCATCTTTGCTTCTGTATGCTTGGCATCACGTCTTCCCCGGTCCCTGCATGCCTTC
ATCATGGTGACATTTGCCATTCAGATTTTTGCCCTGTGGCCCATGTTGCAGAAGAAACTA
AAGGCATGTACTCCCCGGAGCTATGTGGGGGTCACACTGCTTTTTGCATTTTCAGCCGTG
GGAGGCCTACTGTCCATTAGTGCTGTGGGAGCCGTACTCTTTGCCCTTCTGCTGATGTCT
ATCTCATGTCTGTGTCCATTCTACCTCATTCGCTTGCAGCTTTTTAAAGAAAACATTCAT
GGGCCTTGGGATGAAGCTGAAATCAAGGAAGACTTGTCCAGGTTCCTCAGTTAA

1. Inoue N, Watanabe R, Takeda J, Kinoshita T: PIG-C, one of the three human genes involved in the first step of glycosylphosphatidylinositol biosynthesis is a homologue of Saccharomyces cerevisiae GPI2. Biochem Biophys Res Commun. 1996 Sep 4;226(1):193-9. [PubMed ]
2. Hong Y, Ohishi K, Inoue N, Endo Y, Fujita T, Takeda J, Kinoshita T: Structures and chromosomal localizations of the glycosylphosphatidylinositol synthesis gene PIGC and its pseudogene PIGCP1. Genomics. 1997 Sep 15;44(3):347-9. [PubMed ]

1. Acylsphingosine deacylase
2. N-acylsphingosine amidohydrolase
3. AC
4. Putative 32 kDa heart protein
5. PHP32[Contains: Acid ceramidase subunit alpha
6. Acid ceramidase subunit beta]

MPGRSCVALVLLAAAVSCAVAQHAPPWTEDCRKSTYPPSGPTYRGAVPWYTINLDLPPYK
RWHELMLDKAPMLKVIVNSLKNMINTFVPSGKVMQVVDEKLPGLLGNFPGPFEEEMKGIA
AVTDIPLGEIISFNIFYELFTICTSIVAEDKKGHLIHGRNMDFGVFLGWNINNDTWVITE
QLKPLTVNLDFQRNNKTVFKASSFAGYVGMLTGFKPGLFSLTLNERFSINGGYLGILEWI
LGKKDAMWIGFLTRTVLENSTSYEEAKNLLTKTKILAPAYFILGGNQSGEGCVITRDRKE
SLDVYELDAKQGRWYVVQTNYDRWKHPFFLDDRRTPAKMCLNRTSQENISFETMYDVLST
KPVLNKLTVYTTLIDVTKGQFETYLRDCPDPCIGW

• Sphingolipid Metabolism (map00600 )

• N-acylsphingosine + H2O = a carboxylate + sphingosine

• CBAH (PF02275 )

• 1-21

ATGCCGGGCCGGAGTTGCGTCGCCTTAGTCCTCCTGGCTGCCGCCGTCAGCTGTGCCGTC
GCGCAGCACGCGCCGCCGTGGACAGAGGACTGCAGAAAATCAACCTATCCTCCTTCAGGA
CCAACGTACAGAGGTGCAGTTCCATGGTACACCATAAATCTTGACTTACCACCCTACAAA
AGATGGCATGAATTGATGCTTGACAAGGCACCAATGCTAAAGGTTATAGTGAATTCTCTG
AAGAATATGATAAATACATTCGTGCCAAGTGGAAAAGTTATGCAGGTGGTGGATGAAAAA
TTGCCTGGCCTACTTGGCAACTTTCCTGGCCCTTTTGAAGAGGAAATGAAGGGTATTGCC
GCTGTTACTGATATACCTTTAGGAGAGATTATTTCATTCAATATTTTTTATGAATTATTT
ACCATTTGTACTTCAATAGTAGCAGAAGACAAAAAAGGTCATCTAATACATGGGAGAAAC
ATGGATTTTGGAGTATTTCTTGGGTGGAACATAAATAATGATACCTGGGTCATAACTGAG
CAACTAAAACCTTTAACAGTGAATTTGGATTTCCAAAGAAACAACAAAACTGTCTTCAAG
GCTTCAAGCTTTGCTGGCTATGTGGGCATGTTAACAGGATTCAAACCAGGACTGTTCAGT
CTTACACTGAATGAACGTTTCAGTATAAATGGTGGTTATCTGGGTATTCTAGAATGGATT
CTGGGAAAGAAAGATGCCATGTGGATAGGGTTCCTCACTAGAACAGTTCTGGAAAATAGC
ACAAGTTATGAAGAAGCCAAGAATTTATTGACCAAGACCAAGATATTGGCCCCAGCCTAC
TTTATCCTGGGAGGCAACCAGTCTGGGGAAGGTTGTGTGATTACACGAGACAGAAAGGAA
TCATTGGATGTATATGAACTCGATGCTAAGCAGGGTAGATGGTATGTGGTACAAACAAAT
TATGACCGTTGGAAACATCCCTTCTTCCTTGATGATCGCAGAACGCCTGCAAAGATGTGT
CTGAACCGCACCAGCCAAGAGAATATCTCATTTGAAACCATGTATGATGTCCTGTCAACA
AAACCTGTCCTCAACAAGCTGACCGTATACACAACCTTGATAGATGTTACCAAAGGTCAA
TTCGAAACTTACCTGCGGGACTGCCCTGACCCTTGTATAGGTTGGTGA

1. Koch J, Gartner S, Li CM, Quintern LE, Bernardo K, Levran O, Schnabel D, Desnick RJ, Schuchman EH, Sandhoff K: Molecular cloning and characterization of a full-length complementary DNA encoding human acid ceramidase. Identification Of the first molecular lesion causing Farber disease. J Biol Chem. 1996 Dec 20;271(51):33110-5. [PubMed ]
2. Bernardo K, Hurwitz R, Zenk T, Desnick RJ, Ferlinz K, Schuchman EH, Sandhoff K: Purification, characterization, and biosynthesis of human acid ceramidase. J Biol Chem. 1995 May 12;270(19):11098-102. [PubMed ]
3. Zhang H, Li XJ, Martin DB, Aebersold R: Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat Biotechnol. 2003 Jun;21(6):660-6. Epub 2003 May 18. [PubMed ]

1. E-NPP7
2. NPP-7
3. Alkaline sphingomyelin phosphodiesterase
4. Intestinal alkaline sphingomyelinase
5. Alk-SMase

MRGLAVLLTVALATLLAPGAGAPVQSQGSQNKLLLVSFDGFRWNYDQDVDTPNLDAMARD
GVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMYYNTTSKVKLPYHATLGIQRWWD
NGSVPIWITAQRQGLRAGSFFYPGGNVTYQGVAVTRSRKEGIAHNYKNETEWRANIDTVM
AWFTEEDLDLVTLYFGEPDSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLTDRLN
LIITSDHGMTTVDKRAGDLVEFHKFPNFTFRDIEFELLDYGPNGMLLPKEGRLEKVYDAL
KDAHPKLHVYKKEAFPEAFHYANNPRVTPLLMYSDLGYVIHGRINVQFNNGEHGFDNKDM
DMKTIFRAVGPSFRAGLEVEPFESVHVYELMCRLLGIVPEANDGHLATLLPMLHTESALP
PDGRPTLLPKGRSALPPSSRPLLVMGLLGTVILLSEVA

• Sphingolipid Metabolism (map00600 )

• sphingomyelin + H2O = N-acylsphingosine + choline phosphate

• Phosphodiest (PF01663 )

• 1-21

• 434-454

ATGAGAGGCCCGGCCGTCCTCCTCACTGTGGCTCTGGCCACGCTCCTGGCTCCCGGGGCC
GGAGCACCGGTACAAAGTCAGGGCTCCCAGAACAAGCTGCTCCTGGTGTCCTTCGACGGC
TTCCGCTGGAACTACGACCAGGACGTGGACACCCCCAACCTGGACGCCATGGCCCGAGAC
GGGGTGAAGGCACGCTACATGACCCCCGCCTTTGTCACCATGACCAGCCCCTGCCACTTC
ACCCTGGTCACCGGCAAATATATCGAGAACCACGGGGTGGTTCACAACATGTACTACAAC
ACCACCAGCAAGGTGAAGCTGCCCTACCACGCCACGCTGGGCATCCAGAGGTGGTGGGAC
AACGGCAGCGTGCCCATCTGGATCACAGCCCAGAGGCAGGGCCTGAGGGCTGGCTCCTTC
TTCTACCCGGGCGGGAACGTCACCTACCAAGGGGTGGCTGTGACGCGGAGCCGGAAAGAA
GGCATCGCACACAACTACAAAAATGAGACGGAGTGGAGAGCGAACATCGACACAGTGATG
GCGTGGTTCACAGAGGAGGACCTGGATCTGGTCACACTCTACTTCGGGGAGCCGGACTCC
ACGGGCCACAGGTACGGCCCCGAGTCCCCGGAGAGGAGGGAGATGGTGCGGCAGGTGGAC
CGGACCGTGGGCTACCTCCGGGAGAGCATCGCGCGCAACCACCTCACAGACCGCCTCAAC
CTGATCATCACATCCGACCACGGCATGACGACCGTGGACAAACGGGCTGGCGACCTGGTT
GAATTCCACAAGTTCCCCAACTTCACCTTCCGGGACATCGAGTTTGAGCTCCTGGACTAC
GGACCAAACGGGATGCTGCTCCCTAAAGAAGGGAGGCTGGAGAAGGTGTACGATGCCCTC
AAGGACGCCCACCCCAAGCTCCACGTCTACAAGAAGGAGGCGTTCCCCGAGGCCTTCCAC
TACGCCAACAACCCCAGGGTCACACCCCTGCTGATGTACAGCGACCTTGGCTACGTCATC
CATGGGAGAATTAACGTCCAGTTCAACAATGGGGAGCACGGCTTTGACAACAAGGACATG
GACATGAAGACCATCTTCCGCGCTGTGGGCCCTAGCTTCAGGGCGGGCCTGGAGGTGGAG
CCCTTTGAGAGCGTCCACGTGTACGAGCTCATGTGCCGGCTGCTGGGCATCGTGCCCGAG
GCCAACGATGGGCACCTAGCTACTCTGCTGCCCATGCTGCACACAGAATCTGCTCTTCCG
CCTGATGGAAGGCCTACTCTCCTGCCCAAGGGAAGATCTGCTCTCCCGCCCAGCAGCAGG
CCCCTCCTCGTGATGGGACTGCTGGGGACCGTGATTCTTCTGTCTGAGGTCGCATAA

1. Duan RD, Bergman T, Xu N, Wu J, Cheng Y, Duan J, Nelander S, Palmberg C, Nilsson A: Identification of human intestinal alkaline sphingomyelinase as a novel ecto-enzyme related to the nucleotide phosphodiesterase family. J Biol Chem. 2003 Oct 3;278(40):38528-36. Epub 2003 Jul 28. [PubMed ]
2. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed ]

1. Neutral sphingomyelinase
2. nSMase
3. N-SMase
4. Lyso-platelet-activating factor- phospholipase C
5. Lyso-PAF-PLC

MKLNFSLRLRIFNLNCWGIPYLSKHRADRMRRLGDFLNQESFDLALLEEVWSEQDFQYLR
QKLSPTYPAAHHFRSGIIGSGLCVFSKHPIQELTQHIYTLNGYPYMIHHGDWFSGKAVGL
LVLHLSGMVLNAYVTHLHAEYNRQKDIYLAHRVAQAWELAQFIHHTSKKADVVLLCGDLN
MHPEDLGCCLLKEWTGLHDAYLETRDFKGSEEGNTMVPKNCYVSQQELKPFPFGVRIDYV
LYKAVSGFYISCKSFETTTGFDPHSGTPLSDHEALMATLFVRHSPPQQNPSSTHGPAERS
PLMCVLKEAWTELGLGMAQARWWATFASYVIGLGLLLLALLCVLAAGGGAGEAAILLWTP
SVGLVLWAGAFYLFHVQEVNGLYRAQAELQHVLGRAREAQDLGPEPQPALLLGQQEGDRT
KEQ

• Sphingolipid Metabolism (map00600 )

• sphingomyelin + H2O = N-acylsphingosine + choline phosphate

• Exo_endo_phos (PF03372 )

• 1-18

• 330-350 354-374

ATGAAGCTCAACTTCTCCCTGCGACTGCGGATCTTCAACCTCAACTGCTGGGGCATTCCG
TACTTGAGCAAGCACCGGGCCGACCGCATGAGGCGCCTGGGAGACTTTCTGAACCAGGAG
AGCTTCGACCTGGCTTTGCTGGAGGAGGTGTGGAGTGAGCAGGACTTCCAGTACCTGAGA
CAGAAGCTGTCACCTACCTACCCAGCTGCACACCACTTCCGGAGCGGAATCATTGGCAGT
GGCCTCTGTGTCTTCTCCAAACATCCAATCCAGGAGCTTACCCAGCACATCTACACTCTC
AATGGCTACCCCTACATGATCCATCATGGTGACTGGTTCAGTGGGAAGGCTGTGGGGCTG
CTGGTGCTCCATCTAAGTGGCATGGTGCTCAACGCCTATGTGACCCATCTCCATGCCGAA
TACAATCGACAGAAGGACATCTACCTAGCACATCGTGTGGCCCAAGCTTGGGAATTGGCC
CAGTTCATCCACCACACATCCAAGAAGGCAGACGTGGTTCTGTTGTGTGGAGACCTCAAC
ATGCACCCAGAAGACCTGGGCTGCTGCCTGCTGAAGGAGTGGACAGGGCTTCATGATGCC
TATCTTGAAACTCGGGACTTCAAGGGCTCTGAGGAAGGCAACACAATGGTACCCAAGAAC
TGCTACGTCAGCCAGCAGGAGCTGAAGCCATTTCCCTTTGGTGTCCGCATTGACTACGTG
CTTTACAAGGCAGTTTCTGGGTTTTACATCTCCTGTAAGAGTTTTGAAACCACTACAGGC
TTTGACCCTCACAGTGGCACCCCCCTCTCTGATCATGAAGCCCTGATGGCTACTCTGTTT
GTGAGGCACAGCCCCCCACAGCAGAACCCCAGCTCTACCCACGGACCAGCAGAGAGGTCG
CCGTTGATGTGTGTGCTAAAGGAGGCCTGGACGGAGCTGGGTCTGGGCATGGCTCAGGCT
CGCTGGTGGGCCACCTTCGCTAGCTATGTGATTGGCCTGGGGCTGCTTCTCCTGGCACTG
CTGTGTGTCCTGGCGGCTGGAGGAGGGGCCGGGGAAGCTGCCATACTGCTCTGGACCCCC
AGTGTAGGGCTGGTGCTGTGGGCAGGTGCATTCTACCTCTTCCACGTACAGGAGGTCAAT
GGCTTATATAGGGCCCAGGCTGAGCTCCAGCATGTGCTAGGAAGGGCAAGGGAGGCCCAG
GATCTGGGCCCAGAGCCTCAGCCAGCCCTACTCCTGGGGCAGCAGGAGGGGGACAGAACT
AAAGAACAATAA

1. Tomiuk S, Hofmann K, Nix M, Zumbansen M, Stoffel W: Cloned mammalian neutral sphingomyelinase: functions in sphingolipid signaling? Proc Natl Acad Sci U S A. 1998 Mar 31;95(7):3638-43. [PubMed ]
2. Sawai H, Domae N, Nagan N, Hannun YA: Function of the cloned putative neutral sphingomyelinase as lyso-platelet activating factor-phospholipase C. J Biol Chem. 1999 Dec 31;274(53):38131-9. [PubMed ]

1. GPBP
2. Collagen type IV alpha-3-binding protein
3. StAR-related lipid transfer protein 11
4. StARD11
5. START domain-containing protein 11

MSDNQSWNSSGSEEDPETESGPPVERCGVLSKWTNYIHGWQDRWVVLKNNALSYYKSEDE
TEYGCRGSICLSKAVITPHDFDECRFDISVNDSVWYLRAQDPDHRQQWIDAIEQHKTESG
YGSESSLRRHGSMVSLVSGASGYSATSTSSFKKGHSLREKLAEMETFRDILCRQVDTLQK
YFDACADAVSKDELQRDKVVEDDEDDFPTTRSDGDFLHSTNGNKEKLFPHVTPKGINGID
FKGEAITFKATTAGILATLSHCIELMVKREDSWQKRLDKETEKKRRTEEAYKNAMTELKK
KSHFGGPDYEEGPNSLINEEEFFDAVEAALDRQDKIEEQSQSEKVRLHWPTSLPSGDAFS
SVGTHRFVQKPYSRSSSMSSIDLVSASDDVHRFSSQVEEMVQNHMTYSLQDVGGDANWQL
VVEEGEMKVYRREVEENGIVLDPLKATHAVKGVTGHEVCNYFWNVDVRNDWETTIENFHV
VETLADNAIIIYQTHKRVWPASQRDVLYLSVIRKIPALTENDPETWIVCNFSVDHDSAPL
NNRCVRAKINVAMICQTLVSPPEGNQEISRDNILCKITYVANVNPGGWAPASVLRAVAKR
EYPKFLKRFTSYVQEKTAGKPILF

• PH (PF00169 )
• START (PF01852 )

• None

• None

ATGTCGGATAATCAGAGCTGGAACTCGTCGGGCTCGGAGGAGGATCCAGAGACGGAGTCT
GGGCCGCCTGTGGAGCGCTGCGGGGTCCTCAGTAAGTGGACAAACTACATTCATGGGTGG
CAGGATCGTTGGGTAGTTTTGAAAAATAATGCTCTGAGTTACTACAAATCTGAAGATGAA
ACAGAGTATGGCTGCAGAGGATCCATCTGTCTTAGCAAGGCTGTCATCACACCTCACGAT
TTTGATGAATGTCGATTTGATATTAGTGTAAATGATAGTGTTTGGTATCTTCGTGCTCAG
GATCCAGATCATAGACAGCAATGGATAGATGCCATTGAACAGCACAAGACTGAATCTGGA
TATGGATCTGAATCCAGCTTGCGTCGACATGGCTCAATGGTGTCCCTGGTGTCTGGAGCA
AGTGGCTACTCTGCAACATCCACCTCTTCATTCAAGAAAGGCCACAGTTTACGTGAGAAG
TTGGCTGAAATGGAAACATTTAGAGACATCTTATGTAGACAAGTTGACACGCTACAGAAG
TACTTTGATGCCTGTGCTGATGCTGTCTCTAAGGATGAACTTCAAAGGGATAAAGTGGTA
GAAGATGATGAAGATGACTTTCCTACAACGCGTTCTGATGGTGACTTCTTGCATAGTACC
AACGGCAATAAAGAAAAGTTATTTCCACATGTGACACCAAAAGGAATTAATGGTATAGAC
TTTAAAGGGGAAGCGATAACTTTTAAAGCAACTACTGCTGGAATCCTTGCAACACTTTCT
CATTGTATTGAACTAATGGTTAAACGTGAGGACAGCTGGCAGAAGAGACTGGATAAGGAA
ACTGAGAAGAAAAGAAGAACAGAGGAAGCATATAAAAATGCAATGACAGAACTTAAGAAA
AAATCCCACTTTGGAGGACCAGATTATGAAGAAGGCCCTAACAGTCTGATTAATGAAGAA
GAGTTCTTTGATGCTGTTGAAGCTGCTCTTGACAGACAAGATAAAATAGAAGAACAGTCA
CAGAGTGAAAAGGTGAGATTACATTGGCCTACATCCTTGCCCTCTGGAGATGCCTTTTCT
TCTGTGGGGACACATAGATTTGTCCAAAAGCCCTATAGTCGCTCTTCCTCCATGTCTTCC
ATTGATCTAGTCAGTGCCTCTGATGATGTTCACAGATTCAGCTCCCAGGTTGAAGAGATG
GTGCAGAACCACATGACTTACTCATTACAGGATGTAGGCGGAGATGCCAATTGGCAGTTG
GTTGTAGAAGAAGGAGAAATGAAGGTATACAGAAGAGAAGTAGAAGAAAATGGGATTGTT
CTGGATCCTTTAAAAGCTACCCATGCAGTTAAAGGCGTCACAGGACATGAAGTCTGCAAT
TATTTCTGGAATGTTGACGTTCGCAATGACTGGGAAACAACTATAGAAAACTTTCATGTG
GTGGAAACATTAGCTGATAATGCAATCATCATTTATCAAACACACAAGAGGGTGTGGCCT
GCTTCTCAGCGAGACGTATTATATCTTTCTGTCATTCGAAAGATACCAGCCTTGACTGAA
AATGACCCTGAAACTTGGATAGTTTGTAATTTTTCTGTGGATCATGACAGTGCTCCTCTA
AACAACCGATGTGTCCGTGCCAAAATAAATGTTGCTATGATTTGTCAAACCTTGGTAAGC
CCACCAGAGGGAAACCAGGAAATTAGCAGGGACAACATTCTATGCAAGATTACATATGTA
GCTAATGTGAACCCTGGAGGATGGGCACCAGCCTCAGTGTTAAGGGCAGTGGCAAAGCGA
GAGTATCCTAAATTTCTAAAACGTTTTACTTCTTACGTCCAAGAAAAAACTGCAGGAAAG
CCTATTTTGTTCTAG

1. Raya A, Revert F, Navarro S, Saus J: Characterization of a novel type of serine/threonine kinase that specifically phosphorylates the human goodpasture antigen. J Biol Chem. 1999 Apr 30;274(18):12642-9. [PubMed ]
2. Raya A, Revert-Ros F, Martinez-Martinez P, Navarro S, Rosello E, Vieites B, Granero F, Forteza J, Saus J: Goodpasture antigen-binding protein, the kinase that phosphorylates the goodpasture antigen, is an alternatively spliced variant implicated in autoimmune pathogenesis. J Biol Chem. 2000 Dec 22;275(51):40392-9. [PubMed ]

1. Protein A
2. Saposin B-Val
3. Saposin B
4. Sphingolipid activator protein 1
5. SAP-1
6. Cerebroside sulfate activator
7. CSAct
8. Dispersin
9. Sulfatide/GM1 activator
10. Saposin C
11. Co-beta-glucosidase
12. A1 activator
13. Glucosylceramidase activator
14. Sphingolipid activator protein 2
15. SAP-2
16. Saposin D
17. Protein C
18. Component C]

MYALFLLASLLGAALAGPVLGLKECTRGSAVWCQNVKTASDCGAVKHCLQTVWNKPTVKS
LPCDICKDVVTAAGDMLKDNATEEEILVYLEKTCDWLPKPNMSASCKEIVDSYLPVILDI
IKGEMSRPGEVCSALNLCESLQKHLAELNHQKQLESNKIPELDMTEVVAPFMANIPLLLY
PQDGPRSKPQPKDNGDVCQDCIQMVTDIQTAVRTNSTFVQALVEHVKEECDRLGPGMADI
CKNYISQYSEIAIQMMMHMQPKEICALVGFCDEVKEMPMQTLVPAKVASKNVIPALELVE
PIKKHEVPAKSDVYCEVCEFLVKEVTKLIDNNKTEKEILDAFDKMCSKLPKSLSEECQEV
VDTYGSSILSILLEEVSPELVCSMLHLCSGTRLPALTVHVTQPKDGGFCEVCKKLVGYLD
RNLEKNSTKQEILAALEKGCSFLPDPYQKQCDQFVAEYEPVLIEILVEVMDPSFVCLKIG
ACPSAHKPLLGTEKCIWGPSYWCQNTETAAQCNAVEHCKRHVWN

• SapA (PF02199 )
• SapB_1 (PF05184 )
• SapB_2 (PF03489 )

• 1-16

ATGTACGCCCTCTTCCTCCTGGCCAGCCTCCTGGGCGCGGCTCTAGCCGGCCCGGTCCTT
GGACTGAAAGAATGCACCAGGGGCTCGGCAGTGTGGTGCCAGAATGTGAAGACGGCGTCC
GACTGCGGGGCAGTGAAGCACTGCCTGCAGACCGTTTGGAACAAGCCAACAGTGAAATCC
CTTCCCTGCGACATATGCAAAGACGTTGTCACCGCAGCTGGTGATATGCTGAAGGACAAT
GCCACTGAGGAGGAGATCCTTGTTTACTTGGAGAAGACCTGTGACTGGCTTCCGAAACCG
AACATGTCTGCTTCATGCAAGGAGATAGTGGACTCCTACCTCCCTGTCATCCTGGACATC
ATTAAAGGAGAAATGAGCCGTCCTGGGGAGGTGTGCTCTGCTCTCAACCTCTGCGAGTCT
CTCCAGAAGCACCTAGCAGAGCTGAATCACCAGAAGCAGCTGGAGTCCAATAAGATCCCA
GAGCTGGACATGACTGAGGTGGTGGCCCCCTTCATGGCCAACATCCCTCTCCTCCTCTAC
CCTCAGGACGGCCCCCGCAGCAAGCCCCAGCCAAAGGATAATGGGGACGTTTGCCAGGAC
TGCATTCAGATGGTGACTGACATCCAGACTGCTGTACGGACCAACTCCACCTTTGTCCAG
GCCTTGGTGGAACATGTCAAGGAGGAGTGTGACCGCCTGGGCCCTGGCATGGCCGACATA
TGCAAGAACTATATCAGCCAGTATTCTGAAATTGCTATCCAGATGATGATGCACATGCAG
GATCAGCAACCCAAGGAGATCTGTGCGCTGGTTGGGTTCTGTGATGAGGTGAAAGAGATG
CCCATGCAGACTCTGGTCCCCGCCAAAGTGGCCTCCAAGAATGTCATCCCTGCCCTGGAA
CTGGTGGAGCCCATTAAGAAGCACGAGGTCCCAGCAAAGTCTGATGTTTACTGTGAGGTG
TGTGAATTCCTGGTGAAGGAGGTGACCAAGCTGATTGACAACAACAAGACTGAGAAAGAA
ATACTCGACGCTTTTGACAAAATGTGCTCGAAGCTGCCGAAGTCCCTGTCGGAAGAGTGC
CAGGAGGTGGTGGACACGTACGGCAGCTCCATCCTGTCCATCCTGCTGGAGGAGGTCAGC
CCTGAGCTGGTGTGCAGCATGCTGCACCTCTGCTCTGGCACGCGGCTGCCTGCACTGACC
GTTCACGTGACTCAGCCAAAGGACGGTGGCTTCTGCGAAGTGTGCAAGAAGCTGGTGGGT
TATTTGGATCGCAACCTGGAGAAAAACAGCACCAAGCAGGAGATCCTGGCTGCTCTTGAG
AAAGGCTGCAGCTTCCTGCCAGACCCTTACCAGAAGCAGTGTGATCAGTTTGTGGCAGAG
TACGAGCCCGTGCTGATCGAGATCCTGGTGGAGGTGATGGATCCTTCCTTCGTGTGCTTG
AAAATTGGAGCCTGCCCCTCGGCCCATAAGCCCTTGTTGGGAACTGAGAAGTGTATATGG
GGCCCAAGCTACTGGTGCCAGAACACAGAGACAGCAGCCCAGTGCAATGCTGTCGAGCAT
TGCAAACGCCATGTGTGGAACTAG

1. Rorman EG, Grabowski GA: Molecular cloning of a human co-beta-glucosidase cDNA: evidence that four sphingolipid hydrolase activator proteins are encoded by single genes in humans and rats. Genomics. 1989 Oct;5(3):486-92. [PubMed ]
2. Nakano T, Sandhoff K, Stumper J, Christomanou H, Suzuki K: Structure of full-length cDNA coding for sulfatide activator, a Co-beta-glucosidase and two other homologous proteins: two alternate forms of the sulfatide activator. J Biochem (Tokyo). 1989 Feb;105(2):152-4. [PubMed ]
3. O'Brien JS, Kretz KA, Dewji N, Wenger DA, Esch F, Fluharty AL: Coding of two sphingolipid activator proteins (SAP-1 and SAP-2) by same genetic locus. Science. 1988 Aug 26;241(4869):1098-101. [PubMed ]
4. Rorman EG, Scheinker V, Grabowski GA: Structure and evolution of the human prosaposin chromosomal gene. Genomics. 1992 Jun;13(2):312-8. [PubMed ]
5. Hiraiwa M, O'Brien JS, Kishimoto Y, Galdzicka M, Fluharty AL, Ginns EI, Martin BM: Isolation, characterization, and proteolysis of human prosaposin, the precursor of saposins (sphingolipid activator proteins). Arch Biochem Biophys. 1993 Jul;304(1):110-6. [PubMed ]
6. Kondoh K, Hineno T, Sano A, Kakimoto Y: Isolation and characterization of prosaposin from human milk. Biochem Biophys Res Commun. 1991 Nov 27;181(1):286-92. [PubMed ]
7. Holtschmidt H, Sandhoff K, Furst W, Kwon HY, Schnabel D, Suzuki K: The organization of the gene for the human cerebroside sulfate activator protein. FEBS Lett. 1991 Mar 25;280(2):267-70. [PubMed ]
8. Morimoto S, Martin BM, Yamamoto Y, Kretz KA, O'Brien JS, Kishimoto Y: Saposin A: second cerebrosidase activator protein. Proc Natl Acad Sci U S A. 1989 May;86(9):3389-93. [PubMed ]
9. Tyynela J, Palmer DN, Baumann M, Haltia M: Storage of saposins A and D in infantile neuronal ceroid-lipofuscinosis. FEBS Lett. 1993 Sep 6;330(1):8-12. [PubMed ]
10. Dewji NN, Wenger DA, O'Brien JS: Nucleotide sequence of cloned cDNA for human sphingolipid activator protein 1 precursor. Proc Natl Acad Sci U S A. 1987 Dec;84(23):8652-6. [PubMed ]
11. Dewji N, Wenger D, Fujibayashi S, Donoviel M, Esch F, Hill F, O'Brien JS: Molecular cloning of the sphingolipid activator protein-1 (SAP-1), the sulfatide sulfatase activator. Biochem Biophys Res Commun. 1986 Jan 29;134(2):989-94. [PubMed ]
12. Kleinschmidt T, Christomanou H, Braunitzer G: Complete amino-acid sequence of the naturally occurring A2 activator protein for enzymic sphingomyelin degradation: identity to the sulfatide activator protein (SAP-1). Biol Chem Hoppe Seyler. 1988 Dec;369(12):1361-5. [PubMed ]
13. Furst W, Schubert J, Machleidt W, Meyer HE, Sandhoff K: The complete amino-acid sequences of human ganglioside GM2 activator protein and cerebroside sulfate activator protein. Eur J Biochem. 1990 Sep 24;192(3):709-14. [PubMed ]
14. Kleinschmidt T, Christomanou H, Braunitzer G: Complete amino-acid sequence and carbohydrate content of the naturally occurring glucosylceramide activator protein (A1 activator) absent from a new human Gaucher disease variant. Biol Chem Hoppe Seyler. 1987 Dec;368(12):1571-8. [PubMed ]
15. Morimoto S, Martin BM, Kishimoto Y, O'Brien JS: Saposin D: a sphingomyelinase activator. Biochem Biophys Res Commun. 1988 Oct 14;156(1):403-10. [PubMed ]
16. Furst W, Machleidt W, Sandhoff K: The precursor of sulfatide activator protein is processed to three different proteins. Biol Chem Hoppe Seyler. 1988 May;369(5):317-28. [PubMed ]
17. Fluharty AL, Lombardo C, Louis A, Stevens RL, Whitelegge J, Waring AJ, To T, Fluharty CB, Faull KF: Preparation of the cerebroside sulfate activator (CSAct or saposin B) from human urine. Mol Genet Metab. 1999 Nov;68(3):391-403. [PubMed ]
18. Vaccaro AM, Salvioli R, Barca A, Tatti M, Ciaffoni F, Maras B, Siciliano R, Zappacosta F, Amoresano A, Pucci P: Structural analysis of saposin C and B. Complete localization of disulfide bridges. J Biol Chem. 1995 Apr 28;270(17):9953-60. [PubMed ]
19. Faull KF, Johnson J, Kim MJ, To T, Whitelegge JP, Stevens RL, Fluharty CB, Fluharty AL: Structure of the asparagine-linked sugar chains of porcine kidney and human urine cerebroside sulfate activator protein. J Mass Spectrom. 2000 Dec;35(12):1416-24. [PubMed ]
20. Tatti M, Salvioli R, Ciaffoni F, Pucci P, Andolfo A, Amoresano A, Vaccaro AM: Structural and membrane-binding properties of saposin D. Eur J Biochem. 1999 Jul;263(2):486-94. [PubMed ]
21. Ahn VE, Faull KF, Whitelegge JP, Higginson J, Fluharty AL, Prive GG: Expression, purification, crystallization, and preliminary X-ray analysis of recombinant human saposin B. Protein Expr Purif. 2003 Jan;27(1):186-93. [PubMed ]
22. Faull KF, Whitelegge JP, Higginson J, To T, Johnson J, Krutchinsky AN, Standing KG, Waring AJ, Stevens RL, Fluharty CB, Fluharty AL: Cerebroside sulfate activator protein (Saposin B): chromatographic and electrospray mass spectrometric properties. J Mass Spectrom. 1999 Oct;34(10):1040-54. [PubMed ]
23. Ahn VE, Faull KF, Whitelegge JP, Fluharty AL, Prive GG: Crystal structure of saposin B reveals a dimeric shell for lipid binding. Proc Natl Acad Sci U S A. 2003 Jan 7;100(1):38-43. Epub 2002 Dec 23. [PubMed ]
24. Gieselmann V, Zlotogora J, Harris A, Wenger DA, Morris CP: Molecular genetics of metachromatic leukodystrophy. Hum Mutat. 1994;4(4):233-42. [PubMed ]
25. Rafi MA, Zhang XL, DeGala G, Wenger DA: Detection of a point mutation in sphingolipid activator protein-1 mRNA in patients with a variant form of metachromatic leukodystrophy. Biochem Biophys Res Commun. 1990 Jan 30;166(2):1017-23. [PubMed ]
26. Kretz KA, Carson GS, Morimoto S, Kishimoto Y, Fluharty AL, O'Brien JS: Characterization of a mutation in a family with saposin B deficiency: a glycosylation site defect. Proc Natl Acad Sci U S A. 1990 Apr;87(7):2541-4. [PubMed ]
27. Holtschmidt H, Sandhoff K, Kwon HY, Harzer K, Nakano T, Suzuki K: Sulfatide activator protein. Alternative splicing that generates three mRNAs and a newly found mutation responsible for a clinical disease. J Biol Chem. 1991 Apr 25;266(12):7556-60. [PubMed ]
28. Schnabel D, Schroder M, Sandhoff K: Mutation in the sphingolipid activator protein 2 in a patient with a variant of Gaucher disease. FEBS Lett. 1991 Jun 17;284(1):57-9. [PubMed ]

1. Rafi MA, Amini S, Zhang XL, Wenger DA: Correction of sulfatide metabolism after transfer of prosaposin cDNA to cultured cells from a patient with SAP-1 deficiency. Am J Hum Genet. 1992 Jun;50(6):1252-8. [PubMed ]

1. GM2-AP
2. Cerebroside sulfate activator protein
3. Shingolipid activator protein 3
4. SAP-3[Contains: Ganglioside GM2 activator isoform short]

MQSLMQAPLLIALGLLLATPAQAHLKKPSQLSSFSWDNCDEGKDPAVIRSLTLEPDPIVV
PGNVTLSVVGSTSVPLSSPLKVDLVLEKEVAGLWIKIPCTDYIGSCTFEHFCDVLDMLIP
TGEPCPEPLRTYGLPCHCPFKEGTYSLPKSEFVVPDLELPSWLTTGNYRIESVLSSSGKR
LGCIKIAASLKGI

• 1-23

ATGCAGTCCCTGATGCAGGCTCCCCTCCTGATCGCCCTGGGCTTGCTTCTCGCGGCCCCT
GCGCAAGCCCACCTGAAAAAGCCATCCCAGCTCAGTAGCTTTTCCTGGGATAACTGTGAT
GAAGGGAAGGACCCTGCGGTGATCAGAAGCCTGACTCTGGAGCCTGACCCCATCGTCGTT
CCTGGAAATGTGACCCTCAGTGTCGTGGGCAGCACCAGTGTCCCCCTGAGTTCTCCTCTG
AAGGTGGATTTAGTTTTGGAGAAGGAGGTGGCTGGCCTCTGGATCAAGATCCCATGCACA
GACTACATTGGCAGCTGTACCTTTGAACACTTCTGTGATGTGCTTGACATGTTAATTCCT
ACTGGGGAGCCCTGCCCAGAGCCCCTGCGTACCTATGGGCTTCCTTGCCACTGTCCCTTC
AAAGAAGGAACCTACTCACTGCCCAAGAGCGAATTCGTTGTGCCTGACCTGGAGCTGCCC
AGTTGGCTCACCACCGGGAACTACCGCATAGAGAGCGTCCTGAGCAGCAGTGGGAAGCGT
CTGGGCTGCATCAAGATCGCTGCCTCTCTAAAGGGCATATAA

1. Xie B, McInnes B, Neote K, Lamhonwah AM, Mahuran D: Isolation and expression of a full-length cDNA encoding the human GM2 activator protein. Biochem Biophys Res Commun. 1991 Jun 28;177(3):1217-23. [PubMed ]
2. Klima H, Tanaka A, Schnabel D, Nakano T, Schroder M, Suzuki K, Sandhoff K: Characterization of full-length cDNAs and the gene coding for the human GM2 activator protein. FEBS Lett. 1991 Sep 9;289(2):260-4. [PubMed ]
3. Nagarajan S, Chen HC, Li SC, Li YT, Lockyer JM: Evidence for two cDNA clones encoding human GM2-activator protein. Biochem J. 1992 Mar 15;282 ( Pt 3):807-13. [PubMed ]
4. Xie B, Kennedy JL, McInnes B, Auger D, Mahuran D: Identification of a processed pseudogene related to the functional gene encoding the GM2 activator protein: localization of the pseudogene to human chromosome 3 and the functional gene to human chromosome 5. Genomics. 1992 Nov;14(3):796-8. [PubMed ]
5. Chen B, Rigat B, Curry C, Mahuran DJ: Structure of the GM2A gene: identification of an exon 2 nonsense mutation and a naturally occurring transcript with an in-frame deletion of exon 2. Am J Hum Genet. 1999 Jul;65(1):77-87. [PubMed ]
6. Schroder M, Klima H, Nakano T, Kwon H, Quintern LE, Gartner S, Suzuki K, Sandhoff K: Isolation of a cDNA encoding the human GM2 activator protein. FEBS Lett. 1989 Jul 17;251(1-2):197-200. [PubMed ]
7. Furst W, Schubert J, Machleidt W, Meyer HE, Sandhoff K: The complete amino-acid sequences of human ganglioside GM2 activator protein and cerebroside sulfate activator protein. Eur J Biochem. 1990 Sep 24;192(3):709-14. [PubMed ]
8. Wright CS, Li SC, Rastinejad F: Crystal structure of human GM2-activator protein with a novel beta-cup topology. J Mol Biol. 2000 Dec 1;304(3):411-22. [PubMed ]
9. Schroder M, Schnabel D, Suzuki K, Sandhoff K: A mutation in the gene of a glycolipid-binding protein (GM2 activator) that causes GM2-gangliosidosis variant AB. FEBS Lett. 1991 Sep 23;290(1-2):1-3. [PubMed ]
10. Schroder M, Schnabel D, Hurwitz R, Young E, Suzuki K, Sandhoff K: Molecular genetics of GM2-gangliosidosis AB variant: a novel mutation and expression in BHK cells. Hum Genet. 1993 Nov;92(5):437-40. [PubMed ]
11. Schepers U, Glombitza G, Lemm T, Hoffmann A, Chabas A, Ozand P, Sandhoff K: Molecular analysis of a GM2-activator deficiency in two patients with GM2-gangliosidosis AB variant. Am J Hum Genet. 1996 Nov;59(5):1048-56. [PubMed ]

1. MBP
2. Myelin A1 protein
3. Myelin membrane encephalitogenic protein

MGNHAGKRELNAEKASTNSETNRGESEKKRNLGELSRTTSEDNEVFGEADANQNNGTSSQ
DTAVTDSKRTADPKNAWQDAHPADPGSRPHLIRLFSRDAPGREDNTFKDRPSESDELQTI
QEDSAATSESLDVMASQKRPSQRHGSKYLATASTMDHARHGFLPRHRDTGILDSIGRFFG
GDRGAPKRGSGKDSHHPARTAHYGSLPQKSHGRTQDENPVVHFFKNIVTPRTPPPSQGKG
RGLSLSRFSWGAEGQRPGFGYGGRASDYKSAHKGFKGVDAQGTLSKIFKLGGRDSRSGSP
MARR

• Myelin_MBP (PF01669 )

• None

• None

ATGGCGTCACAGAAGAGACCCTCCCAGAGGCACGGATCCAAGTACCTGGCCACAGCAAGT
ACCATGGACCATGCCAGGCATGGCTTCCTCCCAAGGCACAGAGACACGGGCATCCTTGAC
TCCATCGGGCGCTTCTTTGGCGGTGACAGGGGTGCGCCCAAGCGGGGCTCTGGCAAGGAC
TCACACCACCCGGCAAGAACTGCTCACTACGGCTCCCTGCCCCAGAAGTCACACGGCCGG
ACCCAAGATGAAAACCCCGTAGTCCACTTCTTCAAGAACATTGTGACGCCTCGCACACCA
CCCCCGTCGCAGGGAAAGGGGGCCGAAGGCCAGAGACCAGGATTTGGCTACGGAGGCAGA
GCGTCCGACTATAAATCGGCTCACAAGGGATTCAAGGGAGTCGATGCCCAGGGCACGCTT
TCCAAAATTTTTAAGCTGGGAGGAAGAGATAGTCGCTCTGGATCACCCATGGCTAGACGC
TGA

1. Carnegie PR: Amino acid sequence of the encephalitogenic basic protein from human myelin. Biochem J. 1971 Jun;123(1):57-67. [PubMed ]
2. Roth HJ, Kronquist K, Pretorius PJ, Crandall BF, Campagnoni AT: Isolation and characterization of a cDNA coding for a novel human 17.3K myelin basic protein (MBP) variant. J Neurosci Res. 1986;16(1):227-38. [PubMed ]
3. Kamholz J, de Ferra F, Puckett C, Lazzarini R: Identification of three forms of human myelin basic protein by cDNA cloning. Proc Natl Acad Sci U S A. 1986 Jul;83(13):4962-6. [PubMed ]
4. Roth HJ, Kronquist KE, Kerlero de Rosbo N, Crandall BF, Campagnoni AT: Evidence for the expression of four myelin basic protein variants in the developing human spinal cord through cDNA cloning. J Neurosci Res. 1987;17(4):321-8. [PubMed ]
5. Streicher R, Stoffel W: The organization of the human myelin basic protein gene. Comparison with the mouse gene. Biol Chem Hoppe Seyler. 1989 May;370(5):503-10. [PubMed ]
6. Pribyl TM, Campagnoni CW, Kampf K, Kashima T, Handley VW, McMahon J, Campagnoni AT: The human myelin basic protein gene is included within a 179-kilobase transcription unit: expression in the immune and central nervous systems. Proc Natl Acad Sci U S A. 1993 Nov 15;90(22):10695-9. [PubMed ]
7. Boylan KB, Ayres TM, Popko B, Takahashi N, Hood LE, Prusiner SB: Repetitive DNA (TGGA)n 5' to the human myelin basic protein gene: a new form of oligonucleotide repetitive sequence showing length polymorphism. Genomics. 1990 Jan;6(1):16-22. [PubMed ]
8. Scoble HA, Whitaker JN, Biemann K: Analysis of the primary sequence of human myelin basic protein peptides 1-44 and 90-170 by fast atom bombardment mass spectrometry. J Neurochem. 1986 Aug;47(2):614-6. [PubMed ]
9. Wood DD, Moscarello MA: The isolation, characterization, and lipid-aggregating properties of a citrulline containing myelin basic protein. J Biol Chem. 1989 Mar 25;264(9):5121-7. [PubMed ]
10. Boulias C, Pang H, Mastronardi F, Moscarello MA: The isolation and characterization of four myelin basic proteins from the unbound fraction during CM52 chromatography. Arch Biochem Biophys. 1995 Sep 10;322(1):174-82. [PubMed ]
11. Gibson BW, Gilliom RD, Whitaker JN, Biemann K: Amino acid sequence of human myelin basic protein peptide 45-89 as determined by mass spectrometry. J Biol Chem. 1984 Apr 25;259(8):5028-31. [PubMed ]
12. Lennon VA, Wilks AV, Carnegie PR: Immunologic properties of the main encephalitogenic peptide from the basic protein of human myelin. J Immunol. 1970 Nov;105(5):1223-30. [PubMed ]
13. Proost P, Van Damme J, Opdenakker G: Leukocyte gelatinase B cleavage releases encephalitogens from human myelin basic protein. Biochem Biophys Res Commun. 1993 May 14;192(3):1175-81. [PubMed ]
14. Baldwin GS, Carnegie PR: Isolation and partial characterization of methylated arginines from the encephalitogenic basic protein of myelin. Biochem J. 1971 Jun;123(1):69-74. [PubMed ]
15. Mendz GL, Barden JA, Martenson RE: Conformation of a tetradecapeptide epitope of myelin basic protein. Eur J Biochem. 1995 Aug 1;231(3):659-66. [PubMed ]
16. Ridsdale RA, Beniac DR, Tompkins TA, Moscarello MA, Harauz G: Three-dimensional structure of myelin basic protein. II. Molecular modeling and considerations of predicted structures in multiple sclerosis. J Biol Chem. 1997 Feb 14;272(7):4269-75. [PubMed ]

1. Maggio B, Yu RK: Interaction and fusion of unilamellar vesicles containing cerebrosides and sulfatides induced by myelin basic protein. Chem Phys Lipids. 1989 Oct;51(2):127-36. [PubMed ]

1. Beta-glucocerebrosidase
2. Acid beta-glucosidase
3. D-glucosyl-N-acylsphingosine glucohydrolase
4. Alglucerase
5. Imiglucerase

MEFSSPSREECPKPLSRVSIMAGSLTGLLLLQAVSWASGARPCIPKSFGYSSVVCVCNAT
YCDSFDPPTFPALGTFSRYESTRSGRRMELSMGPIQANHTGTGLLLTLQPEQKFQKVKGF
GGAMTDAAALNILALSPPAQNLLLKSYFSEEGIGYNIIRVPMASCDFSIRTYTYADTPDD
FQLHNFSLPEEDTKLKIPLIHRALQLAQRPVSLLASPWTSPTWLKTNGAVNGKGSLKGQP
GDIYHQTWARYFVKFLDAYAEHKLQFWAVTAENEPSAGLLSGYPFQCLGFTPEHQRDFIA
RDLGPTLANSTHHNVRLLMLDDQRLLLPHWAKVVLTDPEAAKYVHGIAVHWYLDFLAPAK
ATLGETHRLFPNTMLFASEACVGSKFWEQSVRLGSWDRGMQYSHSIITNLLYHVVGWTDW
NLALNPEGGPNWVRNFVDSPIIVDITKDTFYKQPMFYHLGHFSKFIPEGSQRVGLVASQK
NDLDAVALMHPDGSAVVVVLNRSSKDVPLTIKDPAVGFLETISPGYSIHTYLWRRQ

• Sphingolipid Metabolism (map00600 )

• D-glucosyl-N-acylsphingosine + H2O = D-glucose + N-acylsphingosine

• Glyco_hydro_30 (PF02055 )

• 21-39

ATGGCTGGCAGCCTCACAGGTTTGCTTCTACTTCAGGCAGTGTCGTGGGCATCAGGTGCC
CGCCCCTGCATCCCTAAAAGCTTCGGCTACAGCTCGGTGGTGTGTGTCTGCAATGCCACA
TACTGTGACTCCTTTGACCCCCCGACCTTTCCTGCCCTTGGTACCTTCAGCCGCTATGAG
AGTACACGCAGTGGGCGACGGATGGAGCTGAGTATGGGGCCCATCCAGGCTAATCACACG
GGCACAGGCCTGCTACTGACCCTGCAGCCAGAACAGAAGTTCCAGAAAGTGAAGGGATTT
GGAGGGGCCATGACAGATGCTGCTGCTCTCAACATCCTTGCCCTGTCACCCCCTGCCCAA
AATTTGCTACTTAAATCGTACTTCTCTGAAGAAGGAATCGGATATAACATCATCCGGGTA
CCCATGGCCAGCTGTGACTTCTCCATCCGCACCTACACCTATGCAGACACCCCTGATGAT
TTCCAGTTGCACAACTTCAGCCTCCCAGAGGAAGATACCAAGCTCAAGATACCCCTGATT
CACCGAGCCCTGCAGTTGGCCCAGCGTCCCGTTTCACTCCTTGCCAGCCCCTGGACATCA
CCCACTTGGCTCAAGACCAATGGAGCGGTGAATGGGAAGGGGTCACTCAAGGGACAGCCC
GGAGACATCTACCACCAGACCTGGGCCAGATACTTTGTGAAGTTCCTGGATGCCTATGCT
GAGCACAAGTTACAGTTCTGGGCAGTGACAGCTGAAAATGAGCCTTCTGCTGGGCTGTTG
AGTGGATACCCCTTCCAGTGCCTGGGCTTCACCCCTGAACATCAGCGAGACTTCATTGCC
CGTGACCTAGGTCCTACCCTCGCCAACAGTACTCACCACAATGTCCGCCTACTCATGCTG
GATGACCAACGCTTGCTGCTGCCCCACTGGGCAAAGGTGGTACTGACAGACCCAGAAGCA
GCTAAATATGTTCATGGCATTGCTGTACATTGGTACCTGGACTTTCTGGCTCCAGCCAAA
GCCACCCTAGGGGAGACACACCGCCTGTTCCCCAACACCATGCTCTTTGCCTCAGAGGCC
TGTGTGGGCTCCAAGTTCTGGGAGCAGAGTGTGCGGCTAGGCTCCTGGGATCGAGGGATG
CAGTACAGCCACAGCATCATCACGAACCTCCTGTACCATGTGGTCGGCTGGACCGACTGG
AACCTTGCCCTGAACCCCGAAGGAGGACCCAATTGGGTGCGTAACTTTGTCGACAGTCCC
ATCATTGTAGACATCACCAAGGACACGTTTTACAAACAGCCCATGTTCTACCACCTTGGC
CACTTCAGCAAGTTCATTCCTGAGGGCTCCCAGAGAGTGGGGCTGGTTGCCAGTCAGAAG
AACGACCTGGACGCAGTGGCACTGATGCATCCCGATGGCTCTGCTGTTGTGGTCGTGCTA
AACCGCTCCTCTAAGGATGTGCCTCTTACCATCAAGGATCCTGCTGTGGGCTTCCTGGAG
ACAATCTCACCTGGCTACTCCATTCACACCTACCTGTGGCATCGCCAGTGA

1. Sorge J, West C, Westwood B, Beutler E: Molecular cloning and nucleotide sequence of human glucocerebrosidase cDNA. Proc Natl Acad Sci U S A. 1985 Nov;82(21):7289-93. [PubMed ]
2. Tsuji S, Choudary PV, Martin BM, Winfield S, Barranger JA, Ginns EI: Nucleotide sequence of cDNA containing the complete coding sequence for human lysosomal glucocerebrosidase. J Biol Chem. 1986 Jan 5;261(1):50-3. [PubMed ]
3. Horowitz M, Wilder S, Horowitz Z, Reiner O, Gelbart T, Beutler E: The human glucocerebrosidase gene and pseudogene: structure and evolution. Genomics. 1989 Jan;4(1):87-96. [PubMed ]
4. Beutler E, West C, Gelbart T: Polymorphisms in the human glucocerebrosidase gene. Genomics. 1992 Apr;12(4):795-800. [PubMed ]
5. Imai K, Nakamura M, Yamada M, Asano A, Yokoyama S, Tsuji S, Ginns EI: A novel transcript from a pseudogene for human glucocerebrosidase in non-Gaucher disease cells. Gene. 1993 Dec 22;136(1-2):365-8. [PubMed ]
6. Winfield SL, Tayebi N, Martin BM, Ginns EI, Sidransky E: Identification of three additional genes contiguous to the glucocerebrosidase locus on chromosome 1q21: implications for Gaucher disease. Genome Res. 1997 Oct;7(10):1020-6. [PubMed ]
7. Reiner O, Wigderson M, Horowitz M: Structural analysis of the human glucocerebrosidase genes. DNA. 1988 Mar;7(2):107-16. [PubMed ]
8. Sorge JA, West C, Kuhl W, Treger L, Beutler E: The human glucocerebrosidase gene has two functional ATG initiator codons. Am J Hum Genet. 1987 Dec;41(6):1016-24. [PubMed ]
9. Ginns EI, Choudary PV, Martin BM, Winfield S, Stubblefield B, Mayor J, Merkle-Lehman D, Murray GJ, Bowers LA, Barranger JA: Isolation of cDNA clones for human beta-glucocerebrosidase using the lambda gt11 expression system. Biochem Biophys Res Commun. 1984 Sep 17;123(2):574-80. [PubMed ]
10. Tsuji S, Martin BM, Barranger JA, Stubblefield BK, LaMarca ME, Ginns EI: Genetic heterogeneity in type 1 Gaucher disease: multiple genotypes in Ashkenazic and non-Ashkenazic individuals. Proc Natl Acad Sci U S A. 1988 Apr;85(7):2349-52. [PubMed ]
11. Dinur T, Osiecki KM, Legler G, Gatt S, Desnick RJ, Grabowski GA: Human acid beta-glucosidase: isolation and amino acid sequence of a peptide containing the catalytic site. Proc Natl Acad Sci U S A. 1986 Mar;83(6):1660-4. [PubMed ]
12. Zhang H, Li XJ, Martin DB, Aebersold R: Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat Biotechnol. 2003 Jun;21(6):660-6. Epub 2003 May 18. [PubMed ]
13. Horowitz M, Zimran A: Mutations causing Gaucher disease. Hum Mutat. 1994;3(1):1-11. [PubMed ]
14. Beutler E, Gelbart T: Glucocerebrosidase (Gaucher disease). Hum Mutat. 1996;8(3):207-13. [PubMed ]
15. Tayebi N, Stone DL, Sidransky E: Type 2 gaucher disease: an expanding phenotype. Mol Genet Metab. 1999 Oct;68(2):209-19. [PubMed ]
16. Stone DL, Tayebi N, Orvisky E, Stubblefield B, Madike V, Sidransky E: Glucocerebrosidase gene mutations in patients with type 2 Gaucher disease. Hum Mutat. 2000;15(2):181-8. [PubMed ]
17. Beutler E, Gelbart T: Gaucher disease associated with a unique KpnI restriction site: identification of the amino-acid substitution. Ann Hum Genet. 1990 May;54(Pt 2):149-53. [PubMed ]
18. Hong CM, Ohashi T, Yu XJ, Weiler S, Barranger JA: Sequence of two alleles responsible for Gaucher disease. DNA Cell Biol. 1990 May;9(4):233-41. [PubMed ]
19. Beutler E, Gelbart T, West C: Identification of six new Gaucher disease mutations. Genomics. 1993 Jan;15(1):203-5. [PubMed ]
20. Choy FY, Wei C, Applegarth DA, McGillivray BC: DNA analysis of an uncommon missense mutation in a Gaucher disease patient of Jewish-Polish-Russian descent. Am J Med Genet. 1994 Jun 1;51(2):156-60. [PubMed ]
21. Beutler E, Gelbart T: Two new Gaucher disease mutations. Hum Genet. 1994 Feb;93(2):209-10. [PubMed ]
22. Tuteja R, Tuteja N, Lilliu F, Bembi B, Galanello R, Cao A, Baralle FE: Y418C: a novel mutation in exon 9 of the glucocerebrosidase gene of a patient with Gaucher disease creates a new Bgl I site. Hum Genet. 1994 Sep;94(3):314-5. [PubMed ]
23. Beutler E, Demina A, Gelbart T: Glucocerebrosidase mutations in Gaucher disease. Mol Med. 1994 Nov;1(1):82-92. [PubMed ]
24. Cormand B, Vilageliu L, Burguera JM, Balcells S, Gonzalez-Duarte R, Grinberg D, Chabas A: Gaucher disease in Spanish patients: analysis of eight mutations. Hum Mutat. 1995;5(4):303-9. [PubMed ]
25. Choy FY, Wei C: Identification of a new mutation (P178S) in an African-American patient with type 2 Gaucher disease. Hum Mutat. 1995;5(4):345-7. [PubMed ]
26. Morar B, Lane AB: The molecular characterization of Gaucher disease in South Africa. Clin Genet. 1996 Aug;50(2):78-84. [PubMed ]
27. Kim JW, Liou BB, Lai MY, Ponce E, Grabowski GA: Gaucher disease: identification of three new mutations in the Korean and Chinese (Taiwanese) populations. Hum Mutat. 1996;7(3):214-8. [PubMed ]
28. Cormand B, Vilageliu L, Balcells S, Gonzalez-Duarte R, Chabas A, Grinberg D: Two novel (1098insA and Y313H) and one rare (R359Q) mutations detected in exon 8 of the beta-glucocerebrosidase gene in Gaucher's disease patients. Hum Mutat. 1996;7(3):272-4. [PubMed ]
29. Amaral O, Pinto E, Fortuna M, Lacerda L, Sa Miranda MC: Type 1 Gaucher disease: identification of N396T and prevalence of glucocerebrosidase mutations in the Portuguese. Hum Mutat. 1996;8(3):280-1. [PubMed ]
30. Seeman PJ, Finckh U, Hoppner J, Lakner V, Liebisch I, Grau G, Rolfs A: Two new missense mutations in a non-Jewish Caucasian family with type 3 Gaucher disease. Neurology. 1996 Apr;46(4):1102-7. [PubMed ]
31. Cormand B, Grinberg D, Gort L, Fiumara A, Barone R, Vilageliu L, Chabas A: Two new mild homozygous mutations in Gaucher disease patients: clinical signs and biochemical analyses. Am J Med Genet. 1997 Jun 27;70(4):437-43. [PubMed ]
32. Choy FY, Humphries ML, Shi H: Identification of two novel and four uncommon missense mutations among chinese Gaucher disease patients. Am J Med Genet. 1997 Aug 8;71(2):172-8. [PubMed ]
33. Hatton CE, Cooper A, Whitehouse C, Wraith JE: Mutation analysis in 46 British and Irish patients with Gaucher's disease. Arch Dis Child. 1997 Jul;77(1):17-22. [PubMed ]
34. Grace ME, Desnick RJ, Pastores GM: Identification and expression of acid beta-glucosidase mutations causing severe type 1 and neurologic type 2 Gaucher disease in non-Jewish patients. J Clin Invest. 1997 May 15;99(10):2530-7. [PubMed ]
35. Ida H, Rennert OM, Kawame H, Maekawa K, Eto Y: Mutation prevalence among 47 unrelated Japanese patients with Gaucher disease: identification of four novel mutations. J Inherit Metab Dis. 1997 Mar;20(1):67-73. [PubMed ]
36. Uyama E, Uchino M, Ida H, Eto Y, Owada M: D409H/D409H genotype in Gaucher-like disease. J Med Genet. 1997 Feb;34(2):175. [PubMed ]
37. Demina A, Beutler E: Six new Gaucher disease mutations. Acta Haematol. 1998;99(2):80-2. [PubMed ]
38. Germain DP, Puech JP, Caillaud C, Kahn A, Poenaru L: Exhaustive screening of the acid beta-glucosidase gene, by fluorescence-assisted mismatch analysis using universal primers: mutation profile and genotype/phenotype correlations in Gaucher disease. Am J Hum Genet. 1998 Aug;63(2):415-27. [PubMed ]
39. Choy FY, Humphries ML, Ben-Yoseph Y: Gaucher type 2 disease: identification of a novel transversion mutation in a French-Irish patient. Am J Med Genet. 1998 Jun 16;78(1):92-3. [PubMed ]
40. Beutler E, Gelbart T: Hematologically important mutations: Gaucher disease. Blood Cells Mol Dis. 1998 Mar;24(1):2-8. [PubMed ]
41. Sinclair G, Choy FY, Humphries L: A novel complex allele and two new point mutations in type 2 (acute neuronopathic) Gaucher disease. Blood Cells Mol Dis. 1998 Dec;24(4):420-7. [PubMed ]
42. Parenti G, Filocamo M, Titomanlio L, Rizzolo G, Silvestro E, Perretti A, Gatti R, Andria G: A novel mutation of the beta-glucocerebrosidase gene associated with neurologic manifestations in three sibs. Clin Genet. 1998 Apr;53(4):281-5. [PubMed ]
43. Cormand B, Grinberg D, Gort L, Chabas A, Vilageliu L: Molecular analysis and clinical findings in the Spanish Gaucher disease population: putative haplotype of the N370S ancestral chromosome. Hum Mutat. 1998;11(4):295-305. [PubMed ]
44. Wasserstein MP, Martignetti JA, Zeitlin R, Lumerman H, Solomon M, Grace ME, Desnick RJ: Type 1 Gaucher disease presenting with extensive mandibular lytic lesions: identification and expression of a novel acid beta-glucosidase mutation. Am J Med Genet. 1999 Jun 4;84(4):334-9. [PubMed ]
45. Choy FY, Wong K, Shi HP: Glucocerebrosidase mutations among Chinese neuronopathic and non-neuronopathic Gaucher disease patients. Am J Med Genet. 1999 Jun 11;84(5):484-6. [PubMed ]
46. Hodanov inverted question mark K, Hrebicek M, Cervenkov inverted question mark M, Mr inverted question markzov inverted question mark L, Veprekov inverted question mark L, Zemen J: Analysis of the beta-glucocerebrosidase gene in Czech and Slovak Gaucher patients: mutation profile and description of six novel mutant alleles. Blood Cells Mol Dis. 1999 Oct-Dec;25(5-6):287-98. [PubMed ]
47. Stone DL, van Diggelen OP, de Klerk JB, Gaillard JL, Niermeijer MF, Willemsen R, Tayebi N, Sidransky E: Is the perinatal lethal form of Gaucher disease more common than classic type 2 Gaucher disease? Eur J Hum Genet. 1999 May-Jun;7(4):505-9. [PubMed ]
48. Sarria AJ, Giraldo P, Perez-Calvo JI, Pocovi M: Detection of three rare (G377S, T134P and 1451delAC), and two novel mutations (G195W and Rec[1263del55;1342G>C]] in Spanish Gaucher disease patients. Mutation in brief no. 251. Online. Hum Mutat. 1999;14(1):88. [PubMed ]

1. Granule membrane protein 140
2. GMP-140
3. PADGEM
4. Leukocyte-endothelial cell adhesion molecule 3
5. LECAM3
6. CD62P antigen

MANCQIAILYQRFQRVVFGISQLLCFSALISELTNQKEVAAWTYHYSTKAYSWNISRKYC
QNRYTDLVAIQNKNEIDYLNKVLPYYSSYYWIGIRKNNKTWTWVGTKKALTNEAENWADN
EPNNKRNNEDCVEIYIKSPSAPGKWNDEHCLKKKHALCYTASCQDMSCSKQGECLETIGN
YTCSCYPGFYGPECEYVRECGELELPQHVLMNCSHPLGNFSFNSQCSFHCTDGYQVNGPS
KLECLASGIWTNKPPQCLAAQCPPLKIPERGNMICLHSAKAFQHQSSCSFSCEEGFALVG
PEVVQCTASGVWTAPAPVCKAVQCQHLEAPSEGTMDCVHPLTAFAYGSSCKFECQPGYRV
RGLDMLRCIDSGHWSAPLPTCEAISCEPLESPVHGSMDCSPSLRAFQYDTNCSFRCAEGF
MLRGADIVRCDNLGQWTAPAPVCQALQCQDLPVPNEARVNCSHPFGAFRYQSVCSFTCNE
GLLLVGASVLQCLATGNWNSVPPECQAIPCTPLLSPQNGTMTCVQPLGSSSYKSTCQFIC
DEGYSLSGPERLDCTRSGRWTDSPPMCEAIKCPELFAPEQGSLDCSDTRGEFNVGSTCHF
SCNNGFKLEGPNNVECTTSGRWSATPPTCKGIASLPTPGLQCPALTTPGQGTMYCRHHPG
TFGFNTTCYFGCNAGFTLIGDSTLSCRPSGQWTAVTPACRAVKCSELHVNKPIAMNCSNL
WGNFSYGSICSFHCLEGQLLNGSAQTACQENGHWSTTVPTCQAGPLTIQEALTYFGGAVA
STIGLIMGGTLLALLRKRFRQKDDGKCPLNPHSHLGTYGVFTNAAFDPSP

• EGF (PF00008 )
• Lectin_C (PF00059 )
• Sushi (PF00084 )

• None

• 772-795

ATGGCCAACTGCCAAATAGCCATCTTGTACCAGAGATTCCAGAGAGTGGTCTTTGGAATT
TCCCAACTCCTTTGCTTCAGTGCCCTGATCTCTGAACTAACAAACCAGAAAGAAGTGGCA
GCATGGACTTATCATTACAGCACAAAAGCATACTCATGGAATATTTCCCGTAAATACTGC
CAGAATCGCTACACAGACTTAGTGGCCATCCAGAATAAAAATGAAATTGATTACCTCAAT
AAGGTCCTACCCTACTACAGCTCCTACTACTGGATTGGGATCCGAAAGAACAATAAGACA
TGGACATGGGTGGGAACCAAAAAGGCTCTCACCAACGAGGCTGAGAACTGGGCTGATAAT
GAACCTAACAACAAAAGGAACAACGAGGACTGCGTGGAGATATACATCAAGAGTCCGTCA
GCCCCTGGCAAGTGGAATGATGAGCACTGCTTGAAGAAAAAGCACGCATTGTGTTACACA
GCCTCCTGCCAGGACATGTCCTGCAGCAAACAAGGAGAGTGCCTCGAGACCATCGGGAAC
TACACCTGCTCCTGTTACCCTGGATTCTATGGGCCAGAATGTGAATACGTGAGAGAGTGT
GGAGAACTTGAGCTCCCTCAACACGTGCTCATGAACTGCAGCCACCCTCTGGGAAACTTC
TCTTTTAACTCGCAGTGCAGCTTCCACTGCACTGACGGGTACCAAGTAAATGGGCCCAGC
AAGCTGGAATGCTTGGCTTCTGGAATCTGGACAAATAAGCCTCCACAGTGTTTAGCTGCC
CAGTGCCCACCCCTGAAGATTCCTGAACGAGGAAACATGATCTGCCTTCATTCTGCAAAA
GCATTCCAGCATCAGTCTAGCTGCAGCTTCAGTTGTGAAGAGGGATTTGCATTAGTTGGA
CCGGAAGTGGTGCAATGCACAGCCTCGGGGGTATGGACAGCCCCAGCCCCAGTGTGTAAA
GCTGTGCAGTGTCAGCACCTGGAAGCCCCCAGTGAAGGAACCATGGACTGTGTTCATCCG
CTCACTGCTTTTGCCTATGGCTCCAGCTGCAAATTTGAGTGCCAGCCCGGCTACAGAGTG
AGGGGCTTGGACATGCTCCGCTGCATTGACTCTGGACACTGGTCTGCACCCTTGCCAACC
TGTGAGGCTATTTCGTGTGAGCCGCTGGAGAGTCCTGTCCACGGAAGCATGGATTGCTCT
CCATCCTTGAGAGCGTTTCAGTATGACACCAACTGTAGCTTCCGCTGTGCTGAAGGTTTC
ATGCTGAGAGGAGCCGATATAGTTCGGTGTGATAACTTGGGACAGTGGACAGCACCAGCC
CCAGTCTGTCAAGCTTTGCAGTGCCAGGATCTCCCAGTTCCAAATGAGGCCCGGGTGAAC
TGCTCCCACCCCTTCGGTGCCTTTAGGTACCAGTCAGTCTGCAGCTTCACCTGCAATGAA
GGCTTGCTCCTGGTGGGAGCAAGTGTGCTACAGTGCTTGGCTACTGGAAACTGGAATTCT
GTTCCTCCAGAATGCCAAGCCATTCCCTGCACACCTTTGCTAAGCCCTCAGAATGGAACA
ATGACCTGTGTTCAACCTCTTGGAAGTTCCAGTTATAAATCCACATGTCAATTCATCTGT
GACGAGGGATATTCTTTGTCTGGACCAGAAAGATTGGATTGTACTCGATCGGGACGCTGG
ACAGACTCCCCACCAATGTGTGAAGCCATCAAGTGCCCAGAACTCTTTGCCCCAGAGCAG
GGCAGCCTGGATTGTTCTGACACTCGTGGAGAATTCAATGTTGGCTCCACCTGTCATTTC
TCTTGTAACAATGGCTTTAAGCTGGAGGGGCCCAATAATGTGGAATGCACAACTTCTGGA
AGATGGTCAGCTACTCCACCAACCTGCAAAGGCATAGCATCACTTCCTACTCCAGGGTTG
CAATGTCCAGCCCTCACCACTCCTGGGCAGGGAACCATGTACTGTAGGCATCATCCGGGA
ACCTTTGGTTTTAATACCACTTGTTACTTTGGCTGCAACGCTGGATTCACACTCATAGGA
GACAGCACTCTCAGCTGCAGACCTTCAGGACAATGGACAGCAGTAACTCCAGCATGCAGA
GCTGTGAAATGCTCAGAACTACATGTTAATAAGCCAATAGCGATGAACTGCTCCAACCTC
TGGGGAAACTTCAGTTATGGATCAATCTGCTCTTTCCATTGTCTAGAGGGCCAGTTACTT
AATGGCTCTGCACAAACAGCATGCCAAGAGAATGGCCACTGGTCAACTACCGTGCCAACC
TGCCAAGCAGGACCATTGACTATCCAGGAAGCCCTGACTTACTTTGGTGGAGCGGTGGCT
TCTACAATAGGTCTGATAATGGGTGGGACGCTCCTGGCTTTGCTAAGAAAGCGTTTCAGA
CAAAAAGATGATGGGAAATGCCCCTTGAATCCTCACAGCCACCTAGGAACATATGGAGTT
TTTACAAACGCTGCATTTGACCCGAGTCCTTAA

1. Johnston GI, Cook RG, McEver RP: Cloning of GMP-140, a granule membrane protein of platelets and endothelium: sequence similarity to proteins involved in cell adhesion and inflammation. Cell. 1989 Mar 24;56(6):1033-44. [PubMed ]
2. Fujimoto T, Stroud E, Whatley RE, Prescott SM, Muszbek L, Laposata M, McEver RP: P-selectin is acylated with palmitic acid and stearic acid at cysteine 766 through a thioester linkage. J Biol Chem. 1993 May 25;268(15):11394-400. [PubMed ]
3. Florian V, Schluter T, Bohnensack R: A new member of the sorting nexin family interacts with the C-terminus of P-selectin. Biochem Biophys Res Commun. 2001 Mar 9;281(4):1045-50. [PubMed ]
4. Freedman SJ, Sanford DG, Bachovchin WW, Furie BC, Baleja JD, Furie B: Structure and function of the epidermal growth factor domain of P-selectin. Biochemistry. 1996 Oct 29;35(43):13733-44. [PubMed ]
5. Bajorath J, Stenkamp R, Aruffo A: Knowledge-based model building of proteins: concepts and examples. Protein Sci. 1993 Nov;2(11):1798-810. [PubMed ]
6. Herrmann SM, Ricard S, Nicaud V, Mallet C, Evans A, Ruidavets JB, Arveiler D, Luc G, Cambien F: The P-selectin gene is highly polymorphic: reduced frequency of the Pro715 allele carriers in patients with myocardial infarction. Hum Mol Genet. 1998 Aug;7(8):1277-84. [PubMed ]
7. Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed ]

1. Squadrito F, Altavilla D, Squadrito G, Campo GM, Arlotta M, Quartarone C, Minutoli L, Ferlito M, Saitta A, Caputi AP: Sulfatide reduces leucocyte accumulation and reverts vascular failure in splanchnic artery occlusion shock. Eur J Pharmacol. 1998 Nov 13;361(1):101-8. [PubMed ]

1. Lymph node homing receptor
2. Leukocyte adhesion molecule 1
3. LAM-1
4. Leukocyte surface antigen Leu-8
5. TQ1
6. gp90-MEL
7. Leukocyte-endothelial cell adhesion molecule 1
8. LECAM1
9. CD62L antigen

MIFPWKCQSTQRDLWNIFKLWGWTMLCCDFLAHHGTDCWTYHYSEKPMNWQRARRFCRDN
YTDLVAIQNKAEIEYLEKTLPFSRSYYWIGIRKIGGIWTWVGTNKSLTEEAENWGDGEPN
NKKNKEDCVEIYIKRNKDAGKWNDDACHKLKAALCYTASCQPWSCSGHGECVEIINNYTC
NCDVGYYGPQCQFVIQCEPLEAPELGTMDCTHPLGNFSFSSQCAFSCSEGTNLTGIEETT
CGPFGNWSSPEPTCQVIQCEPLSAPDLGIMNCSHPLASFSFTSACTFICSEGTELIGKKK
TICESSGIWSNPSPICQKLDKSFSMIKEGDYNPLFIPVAVMVTAFSGLAFIIWLARRLKK
GKKSKRSMNDPY

• EGF (PF00008 )
• Lectin_C (PF00059 )
• Sushi (PF00084 )

• 1-28

• 333-355

ATGATATTTCCATGGAAATGTCAGAGCACCCAGAGGGACTTATGGAACATCTTCAAGTTG
TGGGGGTGGACAATGCTCTGTTGTGATTTCCTGGCACATCATGGAACCGACTGCTGGACT
TACCATTATTCTGAAAAACCCATGAACTGGCAAAGGGCTAGAAGATTCTGCCGAGACAAT
TACACAGATTTAGTTGCCATACAAAACAAGGCGGAAATTGAGTATCTGGAGAAGACTCTG
CCTTTCAGTCGTTCTTACTACTGGATAGGAATCCGGAAGATAGGAGGAATATGGACGTGG
GTGGGAACCAACAAATCTCTTACTGAAGAAGCAGAGAACTGGGGAGATGGTGAGCCCAAC
AACAAGAAGAACAAGGAGGACTGCGTGGAGATCTATATCAAGAGAAACAAAGATGCAGGC
AAATGGAACGATGACGCCTGCCACAAACTAAAGGCAGCCCTCTGTTACACAGCTTCTTGC
CAGCCCTGGTCATGCAGTGGCCATGGAGAATGTGTAGAAATCATCAATAATTACACCTGC
AACTGTGATGTGGGGTACTATGGGCCCCAGTGTCAGCTTGTGATTCAGTGTGAGCCTTTG
GAGGCCCCAGAGCTGGGTACCATGGACTGTACTCACCCTTTGGGAAACTTCAGCTTCAGC
TCACAGTGTGCCTTCAGCTGCTCTGAAGGAACAAACTTAACTGGGATTGAAGAAACCACC
TGTGGACCATTTGGAAACTGGTCATCTCCAGAACCAACCTGTCAAGTGATTCAGTGTGAG
CCTCTATCAGCACCAGATTTGGGGATCATGAACTGTAGCCATCCCCTGGCCAGCTTCAGC
TTTACCTCTGCATGTACCTTCATCTGCTCAGAAGGAACTGAGTTAATTGGGAAGAAGAAA
ACCATTTGTGAATCATCTGGAATCTGGTCAAATCCTAGTCCAATATGTCAAAAATTGGAC
AAAAGTTTCTCAATGATTAAGGAGGGTGATTATAACCCCCTCTTCATTCCAGTGGCAGTC
ATGGTTACTGCATTCTCTGGGTTGGCATTTATCATTTGGCTGGCAAGGAGATTAAAAAAA
GGCAAGAAATCCAAGAGAAGTATGAATGACCCATATTAA

1. Siegelman MH, Weissman IL: Human homologue of mouse lymph node homing receptor: evolutionary conservation at tandem cell interaction domains. Proc Natl Acad Sci U S A. 1989 Jul;86(14):5562-6. [PubMed ]
2. Tedder TF, Isaacs CM, Ernst TJ, Demetri GD, Adler DA, Disteche CM: Isolation and chromosomal localization of cDNAs encoding a novel human lymphocyte cell surface molecule, LAM-1. Homology with the mouse lymphocyte homing receptor and other human adhesion proteins. J Exp Med. 1989 Jul 1;170(1):123-33. [PubMed ]
3. Camerini D, James SP, Stamenkovic I, Seed B: Leu-8/TQ1 is the human equivalent of the Mel-14 lymph node homing receptor. Nature. 1989 Nov 2;342(6245):78-82. [PubMed ]
4. Bowen BR, Nguyen T, Lasky LA: Characterization of a human homologue of the murine peripheral lymph node homing receptor. J Cell Biol. 1989 Jul;109(1):421-7. [PubMed ]
5. Ord DC, Ernst TJ, Zhou LJ, Rambaldi A, Spertini O, Griffin J, Tedder TF: Structure of the gene encoding the human leukocyte adhesion molecule-1 (TQ1, Leu-8) of lymphocytes and neutrophils. J Biol Chem. 1990 May 15;265(14):7760-7. [PubMed ]
6. Bajorath J, Aruffo A: A template for generation and comparison of three-dimensional selectin models. Biochem Biophys Res Commun. 1995 Nov 22;216(3):1018-23. [PubMed ]

1. Kajihara J, Guoji Y, Kato K, Suzuki Y: Sulfatide, a specific sugar ligand for L-selectin, blocks CCl4-induced liver inflammation in rats. Biosci Biotechnol Biochem. 1995 Jan;59(1):155-7. [PubMed ]

1. CD1e antigen
2. R2G1

MLLLFLLFEGLCCPGENTAAAEEQLSFRMLQTSSFANHSWAHSEGSGWLGDLQTHGWDTV
LGTIRFLKPWSHGNFSKQELKNLQSLFQLYFHSFIQIVQASAGQFQLEYPFEIQILAGCR
MNAPQIFLNMAYQGSDFLSFQGISWEPSPGAGIRAQNICKVLNRYLDIKEILQSLLGHTC
PRFLAGLMEAGESELKRKVKPEAWLSCGPSPGPGRLQLVCHVSGFYPKPVWVMWMRGEQE
QRGTQRGDVLPNADETWYLRATLDVAAGEAAGLSCRVKHSSLGGHDLIIHWGGYSIFLIL
ICLTVIVTLVILVVVDSRLKKQ

• C1-set (PF07654 )

• 1-19

• 295-315

ATGCTGCTCCTGTTCCTCCTCTTCGAGGGTCTCTGCTGTCCTGGGGAAAATACAGCAGCA
GCAGAGGAGCAGCTGTCCTTCCGCATGCTCCAAACTTCCTCCTTTGCCAACCACAGCTGG
GCACACAGTGAGGGCTCAGGATGGCTGGGTGACCTGCAGACTCATGGCTGGGACACTGTC
TTGGGCACCATCCGCTTTCTGAAGCCCTGGTCCCATGGAAACTTCAGCAAGCAGGAGCTG
AAAAACTTACAGTCACTGTTCCAGTTATACTTCCATAGTTTTATCCAGATAGTGCAAGCT
TCTGCTGGTCAATTTCAGCTTGAATACCCCTTCGAGATCCAGATATTAGCTGGCTGTAGA
ATGAATGCCCCACAAATCTTCTTAAATATGGCATATCAAGGGTCAGATTTCCTGAGTTTC
CAAGGAATTTCCTGGGAGCCATCTCCAGGAGCAGGGATCCGGGCCCAGAACATCTGTAAA
GTGCTCAATCGCTACCTAGATATTAAGGAAATACTGCAAAGCCTTCTTGGTCACACCTGC
CCTCGATTTCTAGCGGGGCTCATGGAAGCAGGGGAGTCAGAACTGAAACGGAAAGTGAAG
CCAGAGGCCTGGCTGTCCTGTGGCCCCAGTCCTGGCCCTGGCCGTCTGCAGCTTGTGTGC
CATGTCTCAGGATTCTACCCAAAGCCCGTGTGGGTGATGTGGATGCGGGGTGAGCAGGAG
CAGCGGGGCACTCAGCGAGGGGACGTCCTGCCTAATGCTGACGAGACATGGTATCTCCGA
GCAACCCTGGATGTGGCGGCTGGGGAGGCAGCTGGCCTGTCCTGTCGGGTGAAACACAGC
AGTCTAGGGGGCCATGATCTAATCATCCATTGGGGTGGATATTCCATCTTTCTCATCCTG
ATCTGTTTGACTGTGATAGTTACCCTGGTCATATTGGTTGTAGTTGACTCACGGTTAAAA
AAACAGAGGTGA

1. Calabi F, Jarvis JM, Martin L, Milstein C: Two classes of CD1 genes. Eur J Immunol. 1989 Feb;19(2):285-92. [PubMed ]
2. Han M, Hannick LI, DiBrino M, Robinson MA: Polymorphism of human CD1 genes. Tissue Antigens. 1999 Aug;54(2):122-7. [PubMed ]
3. Martin LH, Calabi F, Milstein C: Isolation of CD1 genes: a family of major histocompatibility complex-related differentiation antigens. Proc Natl Acad Sci U S A. 1986 Dec;83(23):9154-8. [PubMed ]
4. Mirones I, Oteo M, Parra-Cuadrado JF, Martinez-Naves E: Identification of two novel human CD1E alleles. Tissue Antigens. 2000 Aug;56(2):159-61. [PubMed ]

1. Niemann-Pick disease type C2 protein
2. hE1

MRFLAATFLLLALSTAAQAEPVQFKDCGSVDGVIKEVNVSPCPTQPCQLSKGQSYSVNVT
FTSNIQSKSSKAVVHGILMGVPVPFPIPEPDGCKSGINCPIQKDKTYSYLNKLPVKSEYP
SIKLVVEWQLQDDKNQSLFCWEIPVQIVSHL

• E1_DerP2_DerF2 (PF02221 )

• 1-19

ATGCGTTTCCTGGCAGCTACATTCCTGCTCCTGGCGCTCAGCACCGCTGCCCAGGCCGAA
CCGGTGCAGTTCAAGGACTGCGGTTCTGTGGATGGAGTTATAAAGGAAGTGAATGTGAGC
CCATGCCCCACCCAACCCTGCCAGCTGAGCAAAGGACAGTCTTACAGCGTCAATGTCACC
TTCACCAGCAATATTCAGTCTAAAAGCAGCAAGGCCGTGGTGCATGGCATCCTGATGGGC
GTCCCAGTTCCCTTTCCCATTCCTGAGCCTGATGGTTGTAAGAGTGGAATTAACTGCCCT
ATCCAAAAAGACAAGACCTATAGCTACCTGAATAAACTACCAGTGAAAAGCGAATATCCC
TCTATAAAACTGGTGGTGGAGTGGCAACTTCAGGATGACAAAAACCAAAGTCTCTTCTGC
TGGGAAATCCCAGTACAGATCGTTTCTCATCTCTAA

1. Krull N, Ivell R, Osterhoff C, Kirchhoff C: Region-specific variation of gene expression in the human epididymis as revealed by in situ hybridization with tissue-specific cDNAs. Mol Reprod Dev. 1993 Jan;34(1):16-24. [PubMed ]
2. Naureckiene S, Sleat DE, Lackland H, Fensom A, Vanier MT, Wattiaux R, Jadot M, Lobel P: Identification of HE1 as the second gene of Niemann-Pick C disease. Science. 2000 Dec 22;290(5500):2298-301. [PubMed ]
3. Millat G, Chikh K, Naureckiene S, Sleat DE, Fensom AH, Higaki K, Elleder M, Lobel P, Vanier MT: Niemann-Pick disease type C: spectrum of HE1 mutations and genotype/phenotype correlations in the NPC2 group. Am J Hum Genet. 2001 Nov;69(5):1013-21. Epub 2001 Sep 20. [PubMed ]
4. Klunemann HH, Elleder M, Kaminski WE, Snow K, Peyser JM, O'Brien JF, Munoz D, Schmitz G, Klein HE, Pendlebury WW: Frontal lobe atrophy due to a mutation in the cholesterol binding protein HE1/NPC2. Ann Neurol. 2002 Dec;52(6):743-9. [PubMed ]

1. UOG-1 protein
2. Protein LAG1

MAAAGPAAGPTGPEPMPSYAQLVQRGWGSALAAARGCTDCGWGLARRGLAEHAHLAPPEL
LLLALGALGWTALRSAATARLFRPLAKRCCLQPRDAAKMPESAWKFLFYLGSWSYSAYLL
FGTDYPFFHDPPSVFYDWTPGMAVPRDIAAAYLLQGSFYGHSIYATLYMDTWRKDSVVML
LHHVVTLILIVSSYAFRYHNVGILVLFLHDISDVQLEFTKLNIYFKSRGGSYHRLHALAA
DLGCLSFGFSWFWFRLYWFPLKVLYATSHCSLRTVPDIPFYFFFNALLLLLTLMNLYWFL
YIVAFAAKVLTGQVHELKDLREYDTAEAQSLKPSKAEKPLRNGLVKDKRF

• LAG1 (PF03798 )

• None

• 53-73 103-123 148-168 176-196 239-259 287-307

ATGGCGGCGGCGGGGCCCGCGGCGGGGCCGACGGGGCCCGAGCCCATGCCGAGCTACGCG
CAGCTAGTGCAGCGCGGCTGGGGCAGCGCGCTGGCGGCGGCGCGGGGCTGCACGGACTGC
GGCTGGGGGCTGGCGCGTCGCGGCCTGGCTGAGCACGCGCACCTGGCGCCGCCCGAGCTG
CTGCTGCTGGCGCTCGGCGCGCTGGGCTGGACCGCGCTGCGCTCCGCGGCCACTGCGCGC
CTCTTTCGGCCCCTGGCGAAGCGGTGCTGCCTCCAGCCCAGAGATGCCGCCAAGATGCCC
GAGAGCGCTTGGAAGTTTCTCTTCTACCTGGGCAGCTGGAGCTACAGTGCCTACCTGCTG
TTTGGCACCGACTACCCCTTCTTCCATGACCCACCATCTGTCTTCTACGACTGGACGCCG
GGCATGGCAGTGCCACGGGACATTGCAGCCGCCTACCTGCTCCAGGGAAGCTTCTATGGC
CACTCCATCTACGCTACGCTATACATGGACACCTGGCGCAAGGACTCGGTGGTCATGCTG
CTCCACCACGTGGTCACTCTCATCCTCATCGTCTCCTCCTACGCCTTCCGGTACCACAAT
GTGGGCATCCTTGTGCTCTTCCTGCACGATATCAGTGACGTGCAGCTTGAGTTCACCAAG
CTCAACATTTACTTCAAGTCCCGCGGCGGCTCCTACCATCGGCTGCATGCCTTGGCAGCA
GACTTGGGCTGCCTCAGCTTCGGCTTCAGCTGGTTCTGGTTCCGCCTCTACTGGTTCCCG
CTCAAGGTCCTGTATGCCACCAGTCACTGCAGTCTGCGCACGGTGCCTGACATCCCCTTC
TACTTCTTCTTCAATGCGCTCCTGCTGCTGCTCACCCTTATGAACCTCTACTGGTTCCTG
TACATCGTGGCGTTTGCAGCCAAGGTGTTGACAGGCCAGGTGCACGAGCTGAAGGACCTG
CGGGAGTATGACACAGCCGAGGCCCAGAGCCTGAAGCCCAGCAAAGCCGAGAAGCCACTG
AGGAACGGCCTGGTGAAGGACAAGCGCTTCTGA

1. Lee SJ: Expression of growth/differentiation factor 1 in the nervous system: conservation of a bicistronic structure. Proc Natl Acad Sci U S A. 1991 May 15;88(10):4250-4. [PubMed ]
2. Jiang JC, Kirchman PA, Zagulski M, Hunt J, Jazwinski SM: Homologs of the yeast longevity gene LAG1 in Caenorhabditis elegans and human. Genome Res. 1998 Dec;8(12):1259-72. [PubMed ]

1. CD1d antigen
2. R3G1

MGCLLFLLLWALLQAWGSAEVPQRLFPLRCLQISSFANSSWTRTDGLAWLGELQTHSWSN
DSDTVRSLKPWSQGTFSDQQWETLQHIFRVYRSSFTRDVKEFAKMLRLSYPLELQVSAGC
EVHPGNASNNFFHVAFQGKDILSFQGTSWEPTQEAPLWVNLAIQVLNQDKWTRETVQWLL
NGTCPQFVSGLLESGKSELKKQVKPKAWLSRGPSPGPGRLLLVCHVSGFYPKPVWVKWMR
GEQEQQGTQPGDILPNADETWYLRATLDVVAGEAAGLSCRVKHSSLEGQDIVLYWGGSYT
SMGLIALAVLACLLFLLIVGFTSRFKRQTSYQGVL

• C1-set (PF07654 )

• 1-19

• 302-322

ATGGGGTGCCTGCTGTTTCTGCTGCTCTGGGCGCTCCTCCAGGCTTGGGGAAGCGCTGAA
GTCCCGCAAAGGCTTTTCCCCCTCCGCTGCCTCCAGATCTCGTCCTTCGCCAATAGCAGC
TGGACGCGCACCGACGGCTTGGCGTGGCTGGGGGAGCTGCAGACGCACAGCTGGAGCAAC
GACTCGGACACCGTCCGCTCTCTGAAGCCTTGGTCCCAGGGCACGTTCAGCGACCAGCAG
TGGGAGACGCTGCAGCATATATTTCGGGTTTATCGAAGCAGCTTCACCAGGGACGTGAAG
GAATTCGCCAAAATGCTACGCTTATCCTATCCCTTGGAGCTCCAGGTGTCCGCTGGCTGT
GAGGTGCACCCTGGGAACGCCTCAAATAACTTCTTCCATGTAGCATTTCAAGGAAAAGAT
ATCCTGAGTTTCCAAGGAACTTCTTGGGAGCCAACCCAAGAGGCCCCACTTTGGGTAAAC
TTGGCCATTCAAGTGCTCAACCAGGACAAGTGGACGAGGGAAACAGTGCAGTGGCTCCTT
AATGGCACCTGCCCCCAATTTGTCAGTGGCCTCCTTGAGTCAGGGAAGTCGGAACTGAAG
AAGCAAGTGAAGCCCAAGGCCTGGCTGTCCCGTGGCCCCAGTCCTGGCCCTGGCCGTCTG
CTGCTGGTGTGCCATGTCTCAGGATTCTACCCAAAGCCTGTATGGGTGAAGTGGATGCGG
GGTGAGCAGGAGCAGCAGGGCACTCAGCCAGGGGACATCCTGCCCAATGCTGACGAGACA
TGGTATCTCCGAGCAACCCTGGATGTGGTGGCTGGGGAGGCAGCTGGCCTGTCCTGTCGG
GTGAAGCACAGCAGTCTAGAGGGCCAGGACATCGTCCTCTACTGGGGTGGGAGCTACACC
TCCATGGGCTTGATTGCCTTGGCAGTCCTGGCGTGCTTGCTGTTCCTCCTCATTGTGGGC
TTTACCTCCCGGTTTAAGAGGCAAACTTCCTATCAGGGCGTCCTGTGA

1. Calabi F, Jarvis JM, Martin L, Milstein C: Two classes of CD1 genes. Eur J Immunol. 1989 Feb;19(2):285-92. [PubMed ]
2. Balk SP, Bleicher PA, Terhorst C: Isolation and characterization of a cDNA and gene coding for a fourth CD1 molecule. Proc Natl Acad Sci U S A. 1989 Jan;86(1):252-6. [PubMed ]
3. Han M, Hannick LI, DiBrino M, Robinson MA: Polymorphism of human CD1 genes. Tissue Antigens. 1999 Aug;54(2):122-7. [PubMed ]
4. Martin LH, Calabi F, Milstein C: Isolation of CD1 genes: a family of major histocompatibility complex-related differentiation antigens. Proc Natl Acad Sci U S A. 1986 Dec;83(23):9154-8. [PubMed ]

1. ADAMTSL-1
2. Punctin-1

MECCRRATPGTLLLFLAFLLLSSRTARSEEDRDGLWDAWGPWSECSRTCGGGASYSLRRC
LSSKSCEGRNIRYRTCSNVDCPPEAGDFRAQQCSAHNDVKHHGQFYEWLPVSNDPDNPCS
LKCQAKGTTLVVELAPKVLDGTRCYTESLDMCISGLCQIVGCDHQLGSTVKEDNCGVCNG
DGSTCRLVRGQYKSQLSATKSDDTVVAIPYGSRHIRLVLKGPDHLYLETKTLQGTKGENS
LSSTGTFLVDNSSVDFQKFPDKEILRMAGPLTADFIVKIRNSGSADSTVQFIFYQPIIHR
WRETDFFPCSATCGGGYQLTSAECYDLRSNRVVADQYCHYYPENIKPKPKLQECNLDPCP
ASDGYKQIMPYDLYHPLPRWEATPWTACSSSCGGGIQSRAVSCVEEDIQGHVTSVEEWKC
MYTPKMPIAQPCNIFDCPKWLAQEWSPCTVTCGQGLRYRVVLCIDHRGMHTGGCSPKTKP
HIKEECIVPTPCYKPKEKLPVEAKLPWFKQAQELEEGAAVSEEPS

• TSP_1 (PF00090 )

• 1-28

ATGGAATGCTGCCGTCGGGCAACTCCTGGCACACTGCTCCTCTTTCTGGCTTTCCTGCTC
CTGAGTTCCAGGACCGCACGCTCCGAGGAGGACCGGGACGGCCTATGGGATGCCTGGGGC
CCATGGAGTGAATGCTCACGCACCTGCGGGGGTGGGGCCGCCAACTCTCTGAGGCGCTGC
CTGAGCAGCAAGAGCTGTGAAGGAAGAAATATCCGATACAGAACATGCAGTAATGTGGAC
TGCCCACCAGAAGCAGGTGATTTCCGAGCTCAGCAATGCTCAGCTCATAATGATGTCAAG
CACCATGGCCAGTTTTATGAATGGCTTCCTGTGTCTAATGACCCTGACAACCCATGTTCA
CTCAAGTGCCAAGCCAAAGGAACAACCCTGGTTGTTGAACTAGCACCTAAGGTCTTAGAT
GGTACGCGTTGCTATACAGAATCTTTGGATATGTGCATCAGTGGTTTATGCCAAATTGTT
GGCTGCGATCACCAGCTGGGAAGCACCGTCAAGGAAGATAACTGTGGGGTCTGCAACGGA
GATGGGTCCACCTGCCGGCTGGTCCGAGGGCAGTATAAATCCCAGCTCTCCGCAACCAAA
TCGGATGATACTGTGGTTGCAATTCCCTATGGAAGTAGACATATTCGCCTTGTCTTAAAA
GGTCCTGATCACTTATATCTGGAAACCAAAACCCTCCAGGGGACTAAAGGTGAAAACAGT
CTCAGCTCCACAGGAACTTTCCTTGTGGACAATTCTAGTGTGGACTTCCAGAAATTTCCA
GACAAAGAGATACTGAGAATGGCTGGACCACTCACAGCAGATTTCATTGTCAAGATTCGT
AACTCGGGCTCCGCTGACAGTACAGTCCAGTTCATCTTCTATCAACCCATCATCCACCGA
TGGAGGGAGACGGATTTCTTTCCTTGCTCAGCAACCTGTGGAGGAGGTTATCAGCTGACA
TCGGCTGAGTGCTACGATCTGAGGAGCAACCGTGTGGTTGCTGACCAATACTGTCACTAT
TACCCAGAGAACATCAAACCCAAACCCAAGCTTCAGGAGTGCAACTTGGATCCTTGTCCA
GCCAGTGACGGATACAAGCAGATCATGCCTTATGACCTCTACCATCCCCTTCCTCGGTGG
GAGGCCACCCCATGGACCGCGTGCTCCTCCTCGTGTGGGGGGGGCATCCAGAGCCGGGCA
GTTTCCTGTGTGGAGGAGGACATCCAGGGGCATGTCACTTCAGTGGAAGAGTGGAAATGC
ATGTACACCCCTAAGATGCCCATCGCGCAGCCCTGCAACATTTTTGACTGCCCTAAATGG
CTGGCACAGGAGTGGTCTCCGTGCACAGTGACGTGTGGCCAGGGCCTCAGATACCGTGTG
GTCCTCTGCATCGACCATCGAGGAATGCACACAGGAGGCTGTAGCCCAAAAACAAAGCCC
CACATAAAAGAGGAATGCATCGTACCCACTCCCTGCTATAAACCCAAAGAGAAACTTCCA
GTCGAGGCCAAGTTGCCATGGTTCAAACAAGCTCAAGAGCTAGAAGAAGGAGCTGCTGTG
TCAGAGGAGCCCTCGTAA

1. Hirohata S, Wang LW, Miyagi M, Yan L, Seldin MF, Keene DR, Crabb JW, Apte SS: Punctin, a novel ADAMTS-like molecule, ADAMTSL-1, in extracellular matrix. J Biol Chem. 2002 Apr 5;277(14):12182-9. Epub 2002 Jan 22. [PubMed ]
2. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed ]

1. Guo NH, Krutzsch HC, Negre E, Zabrenetzky VS, Roberts DD: Heparin-binding peptides from the type I repeats of thrombospondin. Structural requirements for heparin binding and promotion of melanoma cell adhesion and chemotaxis. J Biol Chem. 1992 Sep 25;267(27):19349-55. [PubMed ]

1. GPI mannosyltransferase I
2. GPI-MT-I
3. Phosphatidylinositol-glycan biosynthesis class M protein
4. PIG-M

MGSTKHWGEWLLNLKVAPAGVFGVAFLARVALVFYGVFQDRTLHVRYTDIDYQVFTDAAR
FVTEGRSPYLRATYRYTPLLGWLLTPNIYLSELFGKFLFISCDLLTAFLLYRLLLLKGLG
RRQACGYCVFWLLNPLPMAVSSRGNADSIVASLVLMVLYLIKKRLVACAAVFYGFAVHMK
IYPVTYILPITLHLLPDRDNDKSLRQFRYTFQACLYELLKRLCNRAVLLFVAVAGLTFFA
LSFGFYYEYGWEFLEHTYFYHLTRRDIRHNFSPYFYMLYLTAESKWSFSLGIAAFLPQLI
LLSAVSFAYYRDLVFCCFLHTSIFVTFNKVCTSQYFLWYLCLLPLVMPLVRMPWKRAVVL
LMLWFIGQAMWLAPAYVLEFQGKNTFLFIWLAGLFFLLINCSILIQIISHYKEEPLTERI
KYD

• Mannosyl_trans (PF05007 )

• 1-369

• 18-38 80-100 139-161 170-190 226-246 288-308 315-337 339-350 358-378 385-405

ATGGGCTCCACCAAGCACTGGGGCGAATGGCTCCTGAACTTGAAGGTGGCTCCAGCCGGC
GTCTTTGGTGTGGCCTTTCTAGCCAGAGTCGCCCTGGTTTTCTATGGCGTCTTCCAGGAC
CGGACCCTGCACGTGAGGTATACGGACATCGACTACCAGGTCTTCACCGACGCCGCGCGC
TTCGTCACGGAGGGGCGCTCGCCTTACCTGAGAGCCACGTACCGTTACACCCCGCTGCTG
GGTTGGCTCCTCACTCCCAACATCTACCTCAGCGAGCTCTTTGGAAAGTTTCTCTTCATC
AGCTGCGACCTCCTCACCGCTTTCCTCTTATACCGCCTGCTGCTGCTGAAGGGGCTGGGG
CGCCGCCAGGCTTGTGGCTACTGTGTCTTTTGGCTTCTTAACCCCCTGCCTATGGCAGTA
TCCAGCCGCGGTAATGCGGACTCTATTGTCGCCTCCCTGGTCCTGATGGTCCTCTACTTG
ATAAAGAAAAGACTCGTCGCGTGTGCAGCTGTATTCTATGGTTTCGCGGTGCATATGAAG
ATATATCCAGTGACTTACATCCTTCCCATAACCCTCCACCTGCTTCCAGATCGCGACAAT
GACAAAAGCCTCCGTCAATTCCGGTACACTTTCCAGGCTTGTTTGTACGAGCTCCTGAAA
AGGCTGTGTAATCGGGCTGTGCTGCTGTTTGTAGCAGTTGCTGGACTCACGTTTTTTGCC
CTGAGCTTTGGTTTTTACTATGAGTACGGCTGGGAATTTTTGGAACACACCTACTTTTAT
CACCTGACTAGGCGGGATATCCGTCACAACTTTTCTCCGTACTTCTACATGCTGTATTTG
ACTGCAGAGAGCAAGTGGAGTTTTTCCCTGGGAATTGCTGCATTCCTGCCACAGCTCATC
TTGCTTTCAGCTGTGTCTTTCGCCTATTACAGAGACCTCGTTTTTTGTTGTTTTCTTCAT
ACGTCCATTTTTGTGACTTTTAACAAAGTCTGCACCTCCCAGTACTTTCTTTGGTACCTC
TGCTTACTGCCTCTTGTGATGCCACTAGTCAGAATGCCTTGGAAAAGAGCTGTAGTTCTC
CTAATGTTATGGTTTATAGGGCAGGCCATGTGGCTGGCTCCTGCCTATGTTCTAGAGTTT
CAAGGAAAGAACACCTTTCTGTTTATTTGGTTAGCTGGTTTGTTCTTTCTTCTTATCAAT
TGTTCCATCCTGATTCAAATTATTTCCCATTACAAAGAAGAACCCCTGACAGAGAGAATC
AAATATGACTAG

1. Maeda Y, Watanabe R, Harris CL, Hong Y, Ohishi K, Kinoshita K, Kinoshita T: PIG-M transfers the first mannose to glycosylphosphatidylinositol on the lumenal side of the ER. EMBO J. 2001 Jan 15;20(1-2):250-61. [PubMed ]

1. PIG-W

MSEKQMKEAFVSNLNGTTVLEITQGLCFPAFCILCRGFLIIFSQYLCSFSPTWKTRFLTD
FVVLIVPMVATLTIWASFILLELLGVIIFGAGLLYQIYRRRTCYARLPFLKILEKFLNIS
LESEYNPAISCFRVITSAFTAIAILAVDFPLFPRRFAKTELYGTGAMDFGVGGFVFGSAM
VCLEVRRRKYMEGSKLHYFTNSLYSVWPLVFLGIGRLAIIKSIGYQEHLTEYGVHWNFFF
TIIVVKLITPLLLIIFPLNKSWIIALGITVLYQLALDFTSLKRLILYGTDGSGTRVGLLN
ANREGIISTLGYVAIHMAGVQTGLYMHKNRSHIKDLIKVACFLLLAAISLFISLYVVQVN
VEAVSRRMANLAFCIWIVASSLILLSSLLLGDIILSFAKFLIKGALVPCSWKLIQSPVTN
KKHSESLVPEAERMEPSLCLITALNRKQLIFFLLSNITTGLINLMVDTLHSSTLWALFVV
NLYMFSNCLIVYVLYLQDKTVQFW

• GWT1 (PF06423 )

• 1-43

• 22-42 74-94 132-152 163-183 203-223 238-258 261-281 306-326 339-359 371-391 449-469 474-494

1. PIG-X

MAARVAAVRAAAWLLLGAATGLTRGPATAFTAARSDAGIRAMCSEIILRQEVLKDGFHRD
LLIKVKFGESIEDLHTCRLLIKQDIPAGLYVDPYELASLRERNITEAVMVSENFDIEAPN
YLSKESEVLIYARRDSQCIDCFQAFLPVHCRYHRPHSEDGEASIVVNNPDLLMFCDQEFP
ILKCWAHSEVAAPCALDNEDICQWNKMKYKSVYKNVILQVPVGLTVHTSLVCSVTLLITI
LCSTLILVAVFKYGHFSL

• PIG-X (PF08320 )

• 1-21

• 231-251

ATGTGTTCTGAAATTATTTTGAGGCAAGAAGTTTTGAAAGATGGTTTCCACAGAGACCTT
TTAATCAAAGTGAAGTTTGGGGAAAGCATTGAGGACTTGCACACGTGCCGTCTCTTAATT
AAACAGGACATTCCTGCAGGACTTTATGTGGATCCGTATGAGTTGGCTTCATTACGAGAG
AGAAACATAACAGAGGCAGTGATGGTTTCAGAAAATTTTGATATAGAGGCCCCTAACTAT
TTGTCCAAGGAGTCTGAAGTTCTCATTTATGCCAGACGAGATTCACAGTGCATTGACTGT
TTTCAAGCCTTTTTGCCTGTGCACTGCCGCTATCATCGGCCGCACAGTGAAGATGGAGAA
GCCTCGATTGTGGTCAATAACCCAGATTTGTTGATGTTTTGTGACCAAGAGTTCCCGATT
TTGAAATGCTGGGCTCACTCAGAAGTGGCAGCCCCTTGTGCTTTGGATAATGAGGATATA
TGCCAATGGAACAAGATGAAGTATAAATCAGTATATAAGAATGTGATTCTACAAGTTCCA
GTGGGACTGACTGTACATACCTCTCTAGTATGTTCTGTGACTCTGCTCATTACAATCCTG
TGCTCTACATTGATCCTTGTAGCAGTTTTCAAATATGGCCATTTTTCCCTATAA

1. GPI mannosyltransferase IV
2. GPI-MT-IV
3. Phosphatidylinositol-glycan biosynthesis class Z protein
4. PIG-Z
5. hSMP3

MAVRVLWGGLSLLRVLWCLLPQTGYVHPDEFFQSPEVMAEDILGVQAARPWEFYPSSSCR
SVLFPLLISGSTFWLLRLWEELGPWPGLVSGYALLVGPRLLLTALSFALDGAVYHLAPPM
GADRWNALALLSGSYVTLVFYTRTFSNTIEGLLFTWLLVLVSSHVTWGPTRKEPAPGPRW
RSWLLGGIVAAGFFNRPTFLAFAVVPLYLWGTRGATNPGLKSLTREALVLLPGATLTAAV
FVATDSWYFSSPATSRNLVLTPVNFLHYNLNPQNLARHGTHARLTHLAVNGFLLFGVLHA
QALQAAWQQLQVGLQASAQMGLLRALGARSLLSSPRSYLLLLYFMPLALLSAFSHQEARF
LIPLLVPLVLLCSPQTQPVPWKGTVVLFNALGALLFGCLHQGGLVPGLEYLEQVVHAPVL
PSTPTHYTLLFTHTYMPPRHLLHLPGLGAPVEVVDIGGTEDWALCQTLKSFTRQPACQVA
GGPWLCRLFVVTPGTTRRAVEKCSFPFKNETLLFPHLTLEDPPALSSLLSGAWRDHLSLH
IVELGEET

• Glyco_transf_22 (PF03901 )

• 1-28

• 100-120 125-142 149-169 185-205 227-247 338-358

1. Beta3Gn-T5
2. BGnT-5
3. Beta-1,3-N- acetylglucosaminyltransferase-5
4. Lactotriaosylceramide synthase
5. Lc(3Cer synthase
6. Lc3 synthase

MRMLVSGRRVKKWQLIIQLFATCFLASLMFFWEPIDNHIVSHMKSYSYRYLINSYDFVND
TLSLKHTSAGPRYQYLINHKEKCQAQDVLLLLFVKTAPENYDRRSGIRRTWGNENYVRSQ
LNANIKTLFALGTPNPLEGEELQRKLAWEDQRYNDIIQQDFVDSFYNLTLKLLMQFSWAN
TYCPHAKFLMTADDDIFIHMPNLIEYLQSLEQIGVQDFWIGRVHRGAPPIRDKSSKYYVS
YEMYQWPAYPDYTAGAAYVISGDVAAKVYEASQTLNSSLYIDDVFMGLCANKIGIVPQDH
VFFSGEGKTPYHPCIYEKMMTSHGHLEDLQDLWKNATDPKVKTISKGFFGQIYCRLMKII
LLCKISYVDTYPCRAAFI

• galactosyl glucosyl ceramide + UDP-N-acetyl-D-glucosamine --> (Gal)1 (Glc)1 (GlcNAc)1 (Cer)1 + H+ + UDP

• Galactosyl_T (PF01762 )

• None

• 15-35

1. Togayachi A, Akashima T, Ookubo R, Kudo T, Nishihara S, Iwasaki H, Natsume A, Mio H, Inokuchi J, Irimura T, Sasaki K, Narimatsu H: Molecular cloning and characterization of UDP-GlcNAc:lactosylceramide beta 1,3-N-acetylglucosaminyltransferase (beta 3Gn-T5), an essential enzyme for the expression of HNK-1 and Lewis X epitopes on glycolipids. J Biol Chem. 2001 Jun 22;276(25):22032-40. Epub 2001 Mar 30. [PubMed ]
2. Henion TR, Zhou D, Wolfer DP, Jungalwala FB, Hennet T: Cloning of a mouse beta 1,3 N-acetylglucosaminyltransferase GlcNAc(beta 1,3)Gal(beta 1,4)Glc-ceramide synthase gene encoding the key regulator of lacto-series glycolipid biosynthesis. J Biol Chem. 2001 Aug 10;276(32):30261-9. Epub 2001 May 30. [PubMed ]

1. Neutral sphingomyelinase 2
2. Neutral sphingomyelinase II
3. nSMase2
4. nSMase- 2

MVLYTTPFPNSCLSALHCVSWALIFPCYWLVDRLAASFIPTTYEKRQRADDPCCLQLLCT
ALFTPIYLALLVASLPFAFLGFLFWSPLQSARRPYIYSRLEDKGLAGGAALLSEWKGTGP
GKSFCFATANVCLLPDSLARVNNLFNTQARAKEIGQRIRNGAARPQIKIYIDSPTNTSIS
AASFSSLVSPQGGDGVARAVPGSIKRTASVEYKGDGGRHPGDEAANGPASGDPVDSSSPE
DACIVRIGGEEGGRPPEADDPVPGGQARNGAGGGPRGQTPNHNQQDGDSGSLGSPSASRE
SLVKGRAGPDTSASGEPGANSKLLYKASVVKKAAARRRRHPDEAFDHEVSAFFPANLDFL
CLQEVFDKRAATKLKEQLHGYFEYILYDVGVYGCQGCCSFKCLNSGLLFASRYPIMDVAY
HCYPNKCNDDALASKGALFLKVQVGSTPQDQRIVGYIACTHLHAPQEDSAIRCGQLDLLQ
DWLADFRKSTSSSSAANPEELVAFDVVCGDFNFDNCSSDDKLEQQHSLFTHYRDPCRLGP
GEEKPWAIGTLLDTNGLYDEDVCTPDNLQKVLESEEGRREYLAFPTSKSSGQKGRKELLK
GNGRRIDYMLHAEEGLCPDWKAEVEEFSFITQLSGLTDHLPVAMRLMVSSGEEEA

• Sphingolipid Metabolism (map00600 )

• H2O + sphingomyelin (homo sapiens) --> Choline phosphate + ceramide (homo sapiens) + H+

• Exo_endo_phos (PF03372 )

• None

• 11-31 65-85

1. Hofmann K, Tomiuk S, Wolff G, Stoffel W: Cloning and characterization of the mammalian brain-specific, Mg2+-dependent neutral sphingomyelinase. Proc Natl Acad Sci U S A. 2000 May 23;97(11):5895-900. [PubMed ]

1. Beta-1,3-GalTase 5
2. Beta3Gal-T5
3. b3Gal-T5
4. UDP-galactose:beta-N-acetylglucosamine beta- 1,3-galactosyltransferase 5
5. UDP-Gal:beta-GlcNAc beta-1,3- galactosyltransferase 5
6. Beta-3-Gx-T5

MAFPKMRLMYICLLVLGALCLYFSMYSLNPFKEQSFVYKKDGNFLKLPDTDCRQTPPFLV
LLVTSSHKQLAERMAIRQTWGKERMVKGKQLKTFFLLGTTSSAAETKEVDQESQRHGDII
QKDFLDVYYNLTLKTMMGIEWVHRFCPQAAFVMKTDSDMFINVDYLTELLLKKNRTTRFF
TGFLKLNEFPIRQPFSKWFVSKSEYPWDRYPPFCSGTGYVFSGDVASQVYNVSKSVPYIK
LEDVFVGLCLERLNIRLEELHSQPTFFPGGLRFSVCLFRRIVACHFIKPRTLLDYWQALE
NSRGEDCPPV

• globoside (homo sapiens) + UDPgalactose --> galactosylgloboside (homo sapiens) + H+ + UDP

• Galactosyl_T (PF01762 )

• None

• 8-28

1. Isshiki S, Togayachi A, Kudo T, Nishihara S, Watanabe M, Kubota T, Kitajima M, Shiraishi N, Sasaki K, Andoh T, Narimatsu H: Cloning, expression, and characterization of a novel UDP-galactose:beta-N-acetylglucosamine beta1,3-galactosyltransferase (beta3Gal-T5) responsible for synthesis of type 1 chain in colorectal and pancreatic epithelia and tumor cells derived therefrom. J Biol Chem. 1999 Apr 30;274(18):12499-507. [PubMed ]
2. Zhou D, Berger EG, Hennet T: Molecular cloning of a human UDP-galactose:GlcNAcbeta1,3GalNAc beta1, 3 galactosyltransferase gene encoding an O-linked core3-elongation enzyme. Eur J Biochem. 1999 Jul;263(2):571-6. [PubMed ]
3. Hattori M, Fujiyama A, Taylor TD, Watanabe H, Yada T, Park HS, Toyoda A, Ishii K, Totoki Y, Choi DK, Groner Y, Soeda E, Ohki M, Takagi T, Sakaki Y, Taudien S, Blechschmidt K, Polley A, Menzel U, Delabar J, Kumpf K, Lehmann R, Patterson D, Reichwald K, Rump A, Schillhabel M, Schudy A, Zimmermann W, Rosenthal A, Kudoh J, Schibuya K, Kawasaki K, Asakawa S, Shintani A, Sasaki T, Nagamine K, Mitsuyama S, Antonarakis SE, Minoshima S, Shimizu N, Nordsiek G, Hornischer K, Brant P, Scharfe M, Schon O, Desario A, Reichelt J, Kauer G, Blocker H, Ramser J, Beck A, Klages S, Hennig S, Riesselmann L, Dagand E, Haaf T, Wehrmeyer S, Borzym K, Gardiner K, Nizetic D, Francis F, Lehrach H, Reinhardt R, Yaspo ML: The DNA sequence of human chromosome 21. Nature. 2000 May 18;405(6784):311-9. [PubMed ]
4. Amado M, Almeida R, Schwientek T, Clausen H: Identification and characterization of large galactosyltransferase gene families: galactosyltransferases for all functions. Biochim Biophys Acta. 1999 Dec 6;1473(1):35-53. [PubMed ]

1. Beta-1,4-GalTase 6
2. Beta4Gal-T6
3. b4Gal-T6
4. UDP-galactose:beta-N-acetylglucosamine beta- 1,4-galactosyltransferase 6
5. UDP-Gal:beta-GlcNAc beta-1,4- galactosyltransferase 6[Includes: Lactosylceramide synthase
6. LacCer synthase
7. UDP-Gal:glucosylceramide beta-1,4- galactosyltransferase]

MSVLRRMMRVSNRSLLAFIFFFSLSSSCLYFIYVAPGIANTYLFMVQARGIMLRENVKTI
GHMIRLYTNKNSTLNGTDYPEGNNSSDYLVQTTTYLPENFTYSPYLPCPEKLPYMRGFLN
VNVSEVSFDEIHQLFSKDLDIEPGGHWRPKDCKPRWKVAVLIPFRNRHEHLPIFFLHLIP
MLQKQRLEFAFYVIEQTGTQPFNRAMLFNVGFKEAMKDSVWDCVIFHDVDHLPENDRNYY
GCGEMPRHFAAKLDKYMYILPYKEFFGGVSGLTVEQFRKINGFPNAFWGWGGEDDDLWNR
VHYAGYNVTRPEGDLGKYKSIPHHHRGEVQFLGRYKLLRYSKERQYIDGLNNLIYRPKIL
VDRLYTNISVNLMPELAPIEDY

• Galactosyl_T_2 (PF02709 )

• None

• 15-35

1. Lo NW, Shaper JH, Pevsner J, Shaper NL: The expanding beta 4-galactosyltransferase gene family: messages from the databanks. Glycobiology. 1998 May;8(5):517-26. [PubMed ]
2. Takizawa M, Nomura T, Wakisaka E, Yoshizuka N, Aoki J, Arai H, Inoue K, Hattori M, Matsuo N: cDNA cloning and expression of human lactosylceramide synthase. Biochim Biophys Acta. 1999 May 18;1438(2):301-4. [PubMed ]
3. Amado M, Almeida R, Schwientek T, Clausen H: Identification and characterization of large galactosyltransferase gene families: galactosyltransferases for all functions. Biochim Biophys Acta. 1999 Dec 6;1473(1):35-53. [PubMed ]

1. GPI mannosyltransferase III
2. GPI-MT-III
3. Phosphatidylinositol-glycan biosynthesis class B protein
4. PIG-B

MRRPLSKCGMEPGGGDASLTLHGLQNRSHGKIKLRKRKSTLYFNTQEKSARRRGDLLGEN
IYLLLFTIALRILNCFLVQTSFVPDEYWQSLEVSHHMVFNYGYLTWEWTERLRSYTYPLI
FASIYKILHLLGKDSVQLLIWIPRLAQALLSAVADVRLYSLMKQLENQEVARWVFFCQLC
SWFTWYCCTRTLTNTMETVLTIIALFYYPLEGSKSMNSVKYSSLVALAFIIRPTAVILWT
PLLFRHFCQEPRKLDLILHHFLPVGFVTLSLSLMIDRIFFGQWTLVQFNFLKFNVLQNWG
TFYGSHPWHWYFSQGFPVILGTHLPFFIHGCYLAPKRYRILLVTVLWTLLVYSMLSHKEF
RFIYPVLPFCMVFCGYSLTHLKTWKKPALSFLFLSNLFLALYTGLVHQRGTLDVMSHIQK
VCYNNPNKSSASIFIMMPCHSTPYYSHVHCPLPMRFLQCPPDLTGKSHYLDEADVFYLNP
LNWLHREFHDDASLPTHLITFSILEEEISAFLISSNYKRTAVFFHTHLPEGRIGSHIYVY
ERKLKGKFNMKMKF

• Glyco_transf_22 (PF03901 )

• None

• 63-83 136-156 192-212 224-244 255-275 315-335 340-360 362-382 387-407

1. Takahashi M, Inoue N, Ohishi K, Maeda Y, Nakamura N, Endo Y, Fujita T, Takeda J, Kinoshita T: PIG-B, a membrane protein of the endoplasmic reticulum with a large lumenal domain, is involved in transferring the third mannose of the GPI anchor. EMBO J. 1996 Aug 15;15(16):4254-61. [PubMed ]

1. PIG-F
2. GPI11 homolog

MKDNDIKRLLYTHLLCIFSIILSVFIPSLFLENFSILETHLTWLCICSGFVTAVNLVLYL
VVKPNTSSKRSSLSHKVTGFLKCCIYFLMSCFSFHVIFVLYGAPLIELALETFLFAVILS
TFTTVPCLCLLGPNLKAWLRVFSRNGVTSIWENSLQITTISSFVGAWLGALPIPLDWERP
WQVWPISCTLGATFGYVAGLVISPLWIYWNRKQLTYKNN

• PIG-F (PF06699 )

• None

• 11-31 42-62 86-106 113-133 155-175 189-209

1. Inoue N, Kinoshita T, Orii T, Takeda J: Cloning of a human gene, PIG-F, a component of glycosylphosphatidylinositol anchor biosynthesis, by a novel expression cloning strategy. J Biol Chem. 1993 Apr 5;268(10):6882-5. [PubMed ]