1. Galactocerebroside
2. D-Galactosyl-N-acylsphingosine
3. Cerebroside
4. D-Galactosylceramide
5. N-(hexadecanoyl)-1-b-galactosyl-sphing-4-enine
6. delta-Galactosyl-N-acylsphingosine
7. delta-Galactosylceramide
8. N-(hexadecanoyl)-1-beta-galactosyl-sphing-4-enine
9. GalCer
10. a-GalCer
11. alpha-GalCer
12. Gal-beta-1-1'Cer
13. Gal-b-Cer
14. Gal-beta-Cer
15. Galactosylceramide

• Membrane

1. Galactocerebrosidase precursor
2. Arylsulfatase D precursor
3. Sialidase-2
4. Galactosylceramide sulfotransferase
5. Arylsulfatase A precursor
6. Sialidase-4
7. Arylsulfatase E precursor
8. Globoside alpha-1,3-N-acetylgalactosaminyltransferase 1
9. N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
10. Alpha-galactosidase A precursor
11. Sphingomyelin phosphodiesterase precursor
12. Ceramide glucosyltransferase
13. Lactosylceramide 4-alpha-galactosyltransferase
14. Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q
15. Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
16. Phosphatidylinositol N-acetylglucosaminyltransferase subunit H
17. Phosphatidylinositol N-acetylglucosaminyltransferase subunit P
18. Phosphatidylinositol N-acetylglucosaminyltransferase subunit C
19. Acid ceramidase precursor
20. Ectonucleotide pyrophosphatase/phosphodiesterase family member 7 precursor
21. Sphingomyelin phosphodiesterase 2
22. Goodpasture antigen-binding protein
23. Ganglioside GM2 activator precursor
24. Glucosylceramidase precursor
25. T-cell surface glycoprotein CD1e precursor
26. Epididymal secretory protein E1 precursor
27. LAG1 longevity assurance homolog 1
28. T-cell surface glycoprotein CD1d precursor
29. GPI mannosyltransferase 1
30. Phosphatidylinositol-glycan biosynthesis class W protein
31. Phosphatidylinositol-glycan biosynthesis class X protein precursor
32. GPI mannosyltransferase 4
33. UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 5
34. Sphingomyelin phosphodiesterase 3
35. Beta-1,3-galactosyltransferase 5
36. Beta-1,4-galactosyltransferase 6
37. GPI mannosyltransferase 3
38. Phosphatidylinositol-glycan biosynthesis class F protein
39. GPI ethanolamine phosphate transferase 2
40. GPI ethanolamine phosphate transferase 1
41. GPI ethanolamine phosphate transferase 3
42. GPI transamidase component PIG-S
43. GPI transamidase component PIG-T precursor
44. Phosphatidylinositol glycan anchor biosynthesis class U protein
45. GPI mannosyltransferase 2
46. Phosphatidylinositol N-acetylglucosaminyltransferase subunit Y
47. Pleckstrin homology domain-containing family A member 8
48. cDNA FLJ78026
49. Sphingomyelin phosphodiesterase 4
50. Putative neutral ceramidase C
51. Alkaline ceramidase 2
52. Alkaline ceramidase 2
53. Neutral ceramidase
54. Non-lysosomal glucosylceramidase
55. Sialidase 1 (Lysosomal sialidase) (Sialidase 1 (Lysosomal sialidase), isoform CRA_a) (NEU1 protein)
56. cDNA FLJ46085 fis, clone TESTI2007490, highly similar to 2-hydroxyacylsphingosine1-beta-galactosyltransferase (EC 2.4.1.45)
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. Cytosolic sialidase
2. N-acetyl-alpha- neuraminidase 2

MASLPVLQKESVFQSGAHAYRIPALLYLPGQQSLLAFAEQRASKKDEHAELIVLRRGDYD
APTHQVQWQAQEVVAQARLDGHRSMNPCPLYDAQTGTLFLFFIAIPGQVTEQQQLQTRAN
VTRLCQVTSTDHGRTWSSPRDLTDAAIGPAYREWSTFAVGPGHCLQLNDRARSLVVPAYA
YRKLHPIQRPIPSAFCFLSHDHGRTWARGHFVAQDTLECQVAEVETGEQRVVTLNARSHL
RARVQAQSTNDGLDFQESQLVKKLVEPPPQGCQGSVISFPSPRSGPGSPAQWLLYTHPTH
SWQRADLGAYLNPRPPAPEAWSEPVLLAKGSCAYSDLQSMGTGPDGSPLFGCLYEANDYE
EIVFLMFTLKQAFPAEYLPQ

• N-Glycan degradation (map00511 )
• Sphingolipid Metabolism (map00600 )

• Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates

• BNR (PF02012 )

• None

• None

ATGGCGTCCCTTCCTGTCCTGCAGAAGGAGAGCGTGTTCCAGTCGGGAGCCCATGCCTAC
AGAATCCCTGCCCTGCTCTACCTGCCTGGGCAGCAGTCCCTGCTGGCCTTCGCGGAACAG
CGGGCAAGCAAGAAGGATGAGCACGCAGAGCTGATTGTCCTGCGCAGAGGAGACTACGAC
GCACCCACCCACCAGGTTCAGTGGCAAGCTCAGGAGGTGGTGGCCCAGGCCCGGCTGGAT
GGCCACCGGTCCATGAACCCATGCCCCTTGTATGACGCGCAGACGGGGACCCTCTTCCTC
TTCTTCATTGCCATCCCTGGGCAAGTCACGGAGCAACAGCAGCTGCAGACCAGGGCCAAT
GTGACGCGGCTGTGCCAAGTCACCAGCACTGACCACGGGAGGACCTGGAGCTCCCCCAGA
GACCTCACTGATGCGGCCATCGGCCCAGCCTACCGGGAGTGGTCCACCTTTGCAGTGGGC
CCGGGGCATTGTTTGCAGCTTAACGACAGGGCCCGGAGCCTGGTGGTGCCCGCCTACGCC
TACCGGAAACTTCACCCCATCCAAAGGCCGATCCCCTCTGCCTTCTGCTTCCTCAGCCAT
GACCATGGGCGCACGTGGGCGCGAGGGCACTTTGTGGCCCAGGACACCCTGGAGTGCCAG
GTGGCCGAAGTCGAGACTGGGGAGCAGAGGGTGGTGACCCTCAACGCGAGAAGCCACCTC
CGAGCCAGGGTCCAGGCCCAGAGCACCAATGACGGGCTTGATTTCCAGGAGTCTCAGCTG
GTGAAGAAGCTGGTGGAGCCGCCGCCCCAGGGCTGCCAGGGGAGCGTCATCAGCTTCCCC
AGCCCCCGCTCGGGGCCTGGCTCCCCAGCCCAGTGGCTGCTCTACACTCACCCCACACAC
TCCTGGCAGAGGGCCGACCTGGGTGCCTACCTCAACCCGCGACCTCCAGCCCCTGAGGCC
TGGTCAGAGCCGGTACTGCTGGCCAAGGGCAGCTGTGCCTACTCAGACCTCCAGAGCATG
GGCACCGGCCCTGATGGGTCCCCCTTGTTTGGGTGTCTGTACGAAGCCAATGATTACGAG
GAGATTGTCTTTCTCATGTTCACCCTGAAGCAAGCCTTCCCAGCTGAGTACCTGCCTCAG
TGA

1. Monti E, Preti A, Rossi E, Ballabio A, Borsani G: Cloning and characterization of NEU2, a human gene homologous to rodent soluble sialidases. Genomics. 1999 Apr 1;57(1):137-43. [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. N-acetyl-alpha-neuraminidase 4

MGVPRTPSRTVLFERERTGLTYRVPSLLPVPPGPTLLAFVEQRLSPDDSHAHRLVLRRGT
LAGGSVRWGALHVLGTAALAEHRSMNPCPVHDAGTGTVFLFFIAVLGHTPEAVQIATGRN
AARLCCVASRDAGLSWGSARDLTEEAIGGAVQDWATFAVGPGHGVQLPSGRLLVPAYTYR
VDRRECFGKICRTSPHSFAFYSDDHGRTWRCGGLVPNLRSGECQLAAVDGGQAGSFLYCN
ARSPLGSRVQALSTDEGTSFLPAERVASLPETAWGCQGSIVGFPAPAPNRPRDDSWSVGP
GSPLQPPLLGPGVHEPPEEAAVDPRGGQVPGGPFSRLQPRGDGPRQPGPRPGVSGDVGSW
TLALPMPFAAPPQSPTWLLYSHPVGRRARLHMGIRLSQSPLDPRSWTEPWVIYEGPSGYS
DLASIGPAPEGGLVFACLYESGARTSYDEISFCTFSLREVLENVPASPKPPNLGDKPRGC
CWPS

• N-Glycan degradation (map00511 )
• Sphingolipid Metabolism (map00600 )

• Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates

• None

• None

ATGGGGGTCCCTCGTACCCCTTCACGGACAGTGCTCTTCGAGCGGGAGAGGACGGGCCTG
ACCTACCGCGTGCCCTCGCTGCTCCCCGTGCCCCCCGGGCCCACCCTGCTGGCCTTTGTG
GAGCAGCGGCTCAGCCCTGACGACTCCCACGCCCACCGCCTGGTGCTGAGGAGGGGCACG
CTGGCCGGGGGCTCCGTGCGGTGGGGTGCCCTGCACGTGCTGGGGACAGCAGCCCTGGCG
GAGCACCGGTCCATGAACCCCTGCCCTGTGCACGATGCTGGCACGGGCACCGTCTTCCTC
TTCTTCATCGCGGTGCTGGGCCACACGCCTGAGGCCGTGCAGATCGCCACGGGAAGGAAC
GCCGCGCGCCTCTGCTGTGTGGCCAGCCGTGACGCCGGCCTCTCGTGGGGCAGCGCCCGG
GACCTCACCGAGGAGGCCATCGGTGGTGCCGTGCAGGACTGGGCCACATTCGCTGTGGGT
CCCGGCCACGGCGTGCAGCTGCCCTCAGGCCGCCTGCTGGTACCCGCCTACACCTACCGC
GTGGACCGCCTAGAGTGTTTTGGCAAGATCTGCCGGACCAGCCCTCACTCCTTCGCCTTC
TACAGCGATGACCACGGCCGCACCTGGCGCTGTGGAGGCCTCGTGCCCAACCTGCGCTCA
GGCGAGTGCCAGCTGGCGGCGGTGGACGGTGGGCAGGCCGGCAGCTTCCTCTACTGCAAT
GCCCGGAGCCCACTGGGCAGCCGTGTGCAGGCGCTCAGCACTGACGAGGGCACCTCCTTC
CTGCCCGCAGAGCGCGTGGCTTCCCTGCCCGAGACTGCCTGGGGCTGCCAGGGCAGCATC
GTGGGCTTCCCAGCCCCCGCCCCCAACAGGCCACGGGATGACAGTTGGTCAGTGGGCCCC
AGGAGTCCCCTCCAGCCTCCACTCCTCGGTCCTGGAGTCCACGAACCCCCAGAGGAGGCT
GCTGTAGACCCCCGTGGAGGCCAGGTGCCTGGTGGGCCCTTCAGCCGTCTGCAGCCTCGG
GGGGATGGCCCCAGGCAGCCTGGCCCCAGGCCTGGGGTCAGTGGGGATGTGGGGTCCTGG
ACCCTGGCACTCCCCATGCCCTTTGCTGCCCCGCCCCAGAGCCCCACGTGGCTGCTGTAC
TCCCACCCAGTGGGGCGCAGGGCTCGGCTACACATGGGTATCCGCCTGAGCCAGTCCCCG
CTGGACCCGCGCAGCTGGACAGAGCCCTGGGTGATCTACGAGGGCCCCAGCGGCTACTCC
GACCTGGCGTCCATCGGGCCGGCTCCTGAGGGGGGCCTGGTTTTTGCCTGCCTGTACGAG
AGCGGGGCCAGGACCTCCTATGATGAGATTTCCTTTTGTACATTCTCCCTGCGTGAGGTC
CTGGAGAACGTGCCCGCCAGCCCCAAGCCGCCCAACCTTGGGGACAAGCCTCGGGGGTGC
TGCTGGCCCTCCTGA

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. Melibiase
2. Alpha-D- galactoside galactohydrolase
3. Alpha-D-galactosidase A
4. Agalsidase alfa

MQLRNPELHLGCALALRFLALVSWDIPGARALDNGLARTPTMGWLHWERFMCNLDCQEEP
DSCISEKLFMEMAELMVSEGWKDAGYEYLCIDDCWMAPQRDSEGRLQADPQRFPHGIRQL
ANYVHSKGLKLGIYADVGNKTCAGFPGSFGYYDIDAQTFADWGVDLLKFDGCYCDSLENL
ADGYKHMSLALNRTGRSIVYSCEWPLYMWPFQKPNYTEIRQYCNHWRNFADIDDSWKSIK
SILDWTSFNQERIVDVAGPGGWNDPDMLVIGNFGLSWNQQVTQMALWAIMAAPLFMSNDL
RHISPQAKALLQDKDVIAINQDPLGKQGYQLRQGDNFEVWERPLSGLAWAVAMINRQEIG
GPRSYTIAVASLGKGVACNPACFITQLLPVKRKLGFYEWTSRLRSHINPTGTVLLQLENT
MQMSLKDLL

• Galactose Metabolism (map00052 )
• Globoside metabolism (map00603 )
• Glycerolipid Metabolism (map00561 )
• Sphingolipid Metabolism (map00600 )

• Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactohydrolase

• Melibiase (PF02065 )

• 1-31

ATGCAGCTGAGGAACCCAGAACTACATCTGGGCTGCGCGCTTGCGCTTCGCTTCCTGGCC
CTCGTTTCCTGGGACATCCCTGGGGCTAGAGCACTGGACAATGGATTGGCAAGGACGCCT
ACCATGGGCTGGCTGCACTGGGAGCGCTTCATGTGCAACCTTGACTGCCAGGAAGAGCCA
GATTCCTGCATCAGTGAGAAGCTCTTCATGGAGATGGCAGAGCTCATGGTCTCAGAAGGC
TGGAAGGATGCAGGTTATGAGTACCTCTGCATTGATGACTGTTGGATGGCTCCCCAAAGA
GATTCAGAAGGCAGACTTCAGGCAGACCCTCAGCGCTTTCCTCATGGGATTCGCCAGCTA
GCTAATTATGTTCACAGCAAAGGACTGAAGCTAGGGATTTATGCAGATGTTGGAAATAAA
ACCTGCGCAGGCTTCCCTGGGAGTTTTGGATACTACGACATTGATGCCCAGACCTTTGCT
GACTGGGGAGTAGATCTGCTAAAATTTGATGGTTGTTACTGTGACAGTTTGGAAAATTTG
GCAGATGGTTATAAGCACATGTCCTTGGCCCTGAATAGGACTGGCAGAAGCATTGTGTAC
TCCTGTGAGTGGCCTCTTTATATGTGGCCCTTTCAAAAGCCCAATTATACAGAAATCCGA
CAGTACTGCAATCACTGGCGAAATTTTGCTGACATTGATGATTCCTGGAAAAGTATAAAG
AGTATCTTGGACTGGACATCTTTTAACCAGGAGAGAATTGTTGATGTTGCTGGACCAGGG
GGTTGGAATGACCCAGATATGTTAGTGATTGGCAACTTTGGCCTCAGCTGGAATCAGCAA
GTAACTCAGATGGCCCTCTGGGCTATCATGGCTGCTCCTTTATTCATGTCTAATGACCTC
CGACACATCAGCCCTCAAGCCAAAGCTCTCCTTCAGGATAAGGACGTAATTGCCATCAAT
CAGGACCCCTTGGGCAAGCAAGGGTACCAGCTTAGACAGGGAGACAACTTTGAAGTGTGG
GAACGACCTCTCTCAGGCTTAGCCTGGGCTGTAGCTATGATAAACCGGCAGGAGATTGGT
GGACCTCGCTCTTATACCATCGCAGTTGCTTCCCTGGGTAAAGGAGTGGCCTGTAATCCT
GCCTGCTTCATCACACAGCTCCTCCCTGTGAAAAGGAAGCTAGGGTTCTATGAATGGACT
TCAAGGTTAAGAAGTCACATAAATCCCACAGGCACTGTTTTGCTTCAGCTAGAAAATACA
ATGCAGATGTCATTAAAAGACTTACTTTAA

1. Tsuji S, Martin BM, Kaslow DC, Migeon BR, Choudary PV, Stubbleflied BK, Mayor JA, Murray GJ, Barranger JA, Ginns EI: Signal sequence and DNA-mediated expression of human lysosomal alpha-galactosidase A. Eur J Biochem. 1987 Jun 1;165(2):275-80. [PubMed ]
2. Kornreich R, Desnick RJ, Bishop DF: Nucleotide sequence of the human alpha-galactosidase A gene. Nucleic Acids Res. 1989 Apr 25;17(8):3301-2. [PubMed ]
3. Oeltjen JC, Liu X, Lu J, Allen RC, Muzny D, Belmont JW, Gibbs RA: Sixty-nine kilobases of contiguous human genomic sequence containing the alpha-galactosidase A and Bruton's tyrosine kinase loci. Mamm Genome. 1995 May;6(5):334-8. [PubMed ]
4. Bishop DF, Calhoun DH, Bernstein HS, Hantzopoulos P, Quinn M, Desnick RJ: Human alpha-galactosidase A: nucleotide sequence of a cDNA clone encoding the mature enzyme. Proc Natl Acad Sci U S A. 1986 Jul;83(13):4859-63. [PubMed ]
5. Quinn M, Hantzopoulos P, Fidanza V, Calhoun DH: A genomic clone containing the promoter for the gene encoding the human lysosomal enzyme, alpha-galactosidase A. Gene. 1987;58(2-3):177-88. [PubMed ]
6. Bishop DF, Kornreich R, Desnick RJ: Structural organization of the human alpha-galactosidase A gene: further evidence for the absence of a 3' untranslated region. Proc Natl Acad Sci U S A. 1988 Jun;85(11):3903-7. [PubMed ]
7. Novo FJ, Kruszewski A, MacDermot KD, Goldspink G, Gorecki DC: Editing of human alpha-galactosidase RNA resulting in a pyrimidine to purine conversion. Nucleic Acids Res. 1995 Jul 25;23(14):2636-40. [PubMed ]
8. Eng CM, Desnick RJ: Molecular basis of Fabry disease: mutations and polymorphisms in the human alpha-galactosidase A gene. Hum Mutat. 1994;3(2):103-11. [PubMed ]
9. Koide T, Ishiura M, Iwai K, Inoue M, Kaneda Y, Okada Y, Uchida T: A case of Fabry's disease in a patient with no alpha-galactosidase A activity caused by a single amino acid substitution of Pro-40 by Ser. FEBS Lett. 1990 Jan 1;259(2):353-6. [PubMed ]
10. von Scheidt W, Eng CM, Fitzmaurice TF, Erdmann E, Hubner G, Olsen EG, Christomanou H, Kandolf R, Bishop DF, Desnick RJ: An atypical variant of Fabry's disease with manifestations confined to the myocardium. N Engl J Med. 1991 Feb 7;324(6):395-9. [PubMed ]
11. Sakuraba H, Oshima A, Fukuhara Y, Shimmoto M, Nagao Y, Bishop DF, Desnick RJ, Suzuki Y: Identification of point mutations in the alpha-galactosidase A gene in classical and atypical hemizygotes with Fabry disease. Am J Hum Genet. 1990 Nov;47(5):784-9. [PubMed ]
12. Bernstein HS, Bishop DF, Astrin KH, Kornreich R, Eng CM, Sakuraba H, Desnick RJ: Fabry disease: six gene rearrangements and an exonic point mutation in the alpha-galactosidase gene. J Clin Invest. 1989 Apr;83(4):1390-9. [PubMed ]
13. Ishii S, Sakuraba H, Suzuki Y: Point mutations in the upstream region of the alpha-galactosidase A gene exon 6 in an atypical variant of Fabry disease. Hum Genet. 1992 Apr;89(1):29-32. [PubMed ]
14. Eng CM, Resnick-Silverman LA, Niehaus DJ, Astrin KH, Desnick RJ: Nature and frequency of mutations in the alpha-galactosidase A gene that cause Fabry disease. Am J Hum Genet. 1993 Dec;53(6):1186-97. [PubMed ]
15. Davies JP, Winchester BG, Malcolm S: Mutation analysis in patients with the typical form of Anderson-Fabry disease. Hum Mol Genet. 1993 Jul;2(7):1051-3. [PubMed ]
16. Davies J, Christomanou H, Winchester B, Malcolm S: Detection of 8 new mutations in the alpha-galactosidase A gene in Fabry disease. Hum Mol Genet. 1994 Apr;3(4):667-9. [PubMed ]
17. Eng CM, Niehaus DJ, Enriquez AL, Burgert TS, Ludman MD, Desnick RJ: Fabry disease: twenty-three mutations including sense and antisense CpG alterations and identification of a deletional hot-spot in the alpha-galactosidase A gene. Hum Mol Genet. 1994 Oct;3(10):1795-9. [PubMed ]
18. Okumiya T, Ishii S, Takenaka T, Kase R, Kamei S, Sakuraba H, Suzuki Y: Galactose stabilizes various missense mutants of alpha-galactosidase in Fabry disease. Biochem Biophys Res Commun. 1995 Sep 25;214(3):1219-24. [PubMed ]
19. Okumiya T, Ishii S, Kase R, Kamei S, Sakuraba H, Suzuki Y: Alpha-galactosidase gene mutations in Fabry disease: heterogeneous expressions of mutant enzyme proteins. Hum Genet. 1995 May;95(5):557-61. [PubMed ]
20. Madsen KM, Hasholt L, Sorensen SA, Fermer ML, Dahl N: Two novel mutations (L32P) and (G85N) among five different missense mutations in six Danish families with Fabry's disease. Hum Mutat. 1995;5(3):277-8. [PubMed ]
21. Nakao S, Takenaka T, Maeda M, Kodama C, Tanaka A, Tahara M, Yoshida A, Kuriyama M, Hayashibe H, Sakuraba H, et al.: An atypical variant of Fabry's disease in men with left ventricular hypertrophy. N Engl J Med. 1995 Aug 3;333(5):288-93. [PubMed ]
22. Davies JP, Eng CM, Hill JA, Malcolm S, MacDermot K, Winchester B, Desnick RJ: Fabry disease: fourteen alpha-galactosidase A mutations in unrelated families from the United Kingdom and other European countries. Eur J Hum Genet. 1996;4(4):219-24. [PubMed ]
23. Cariolou MA, Christodoulides M, Manoli P, Kokkofitou A, Tsambaos D: Novel trinucleotide deletion in Fabry's disease. Hum Genet. 1996 Apr;97(4):468-70. [PubMed ]
24. Germain D, Biasotto M, Tosi M, Meo T, Kahn A, Poenaru L: Fluorescence-assisted mismatch analysis (FAMA) for exhaustive screening of the alpha-galactosidase A gene and detection of carriers in Fabry disease. Hum Genet. 1996 Dec;98(6):719-26. [PubMed ]
25. Blanch LC, Meaney C, Morris CP: A sensitive mutation screening strategy for Fabry disease: detection of nine mutations in the alpha-galactosidase A gene. Hum Mutat. 1996;8(1):38-43. [PubMed ]
26. Redonnet-Vernhet I, Ploos van Amstel JK, Jansen RP, Wevers RA, Salvayre R, Levade T: Uneven X inactivation in a female monozygotic twin pair with Fabry disease and discordant expression of a novel mutation in the alpha-galactosidase A gene. J Med Genet. 1996 Aug;33(8):682-8. [PubMed ]
27. Takata T, Okumiya T, Hayashibe H, Shimmoto M, Kase R, Itoh K, Utsumi K, Kamei S, Sakuraba H: Screening and detection of gene mutations in Japanese patients with Fabry disease by non-radioactive single-stranded conformation polymorphism analysis. Brain Dev. 1997 Mar;19(2):111-6. [PubMed ]
28. Eng CM, Ashley GA, Burgert TS, Enriquez AL, D'Souza M, Desnick RJ: Fabry disease: thirty-five mutations in the alpha-galactosidase A gene in patients with classic and variant phenotypes. Mol Med. 1997 Mar;3(3):174-82. [PubMed ]
29. Miyazaki T, Kajita M, Ohmori S, Mizutani N, Niwa T, Murata Y, Seo H: A novel mutation (E358K) in the alpha-galactosidase A gene detected in a Japanese family with Fabry disease. Hum Mutat. 1998;Suppl 1:S139-40. [PubMed ]
30. Okumiya T, Kawamura O, Itoh K, Kase R, Ishii S, Kamei S, Sakuraba H: Novel missense mutation (M72V) of alpha-galactosidase gene and its expression product in an atypical Fabry hemizygote. Hum Mutat. 1998;Suppl 1:S213-6. [PubMed ]
31. Guffon N, Froissart R, Chevalier-Porst F, Maire I: Mutation analysis in 11 French patients with Fabry disease. Hum Mutat. 1998;Suppl 1:S288-90. [PubMed ]
32. Germain DP, Poenaru L: Fabry disease: identification of novel alpha-galactosidase A mutations and molecular carrier detection by use of fluorescent chemical cleavage of mismatches. Biochem Biophys Res Commun. 1999 Apr 21;257(3):708-13. [PubMed ]
33. Beyer EM, Karpova EA, Udalova OV, Ploos van Amstel JK, van Diggelen OP, Tsvetkova IV: The multiple cases of Fabry disease in a Russian family caused by an E341K amino acid substitution in the alpha-galactosidase A. Clin Chim Acta. 1999 Feb;280(1-2):81-9. [PubMed ]
34. Topaloglu AK, Ashley GA, Tong B, Shabbeer J, Astrin KH, Eng CM, Desnick RJ: Twenty novel mutations in the alpha-galactosidase A gene causing Fabry disease. Mol Med. 1999 Dec;5(12):806-11. [PubMed ]
35. Lee JK, Kim GH, Kim JS, Kim KK, Lee MC, Yoo HW: Identification of four novel mutations in five unrelated Korean families with Fabry disease. Clin Genet. 2000 Sep;58(3):228-33. [PubMed ]
36. Ashton-Prolla P, Tong B, Shabbeer J, Astrin KH, Eng CM, Desnick RJ: Fabry disease: twenty-two novel mutations in the alpha-galactosidase A gene and genotype/phenotype correlations in severely and mildly affected hemizygotes and heterozygotes. J Investig Med. 2000 Jul;48(4):227-35. [PubMed ]
37. Germain DP, Salard D, Fellmann F, Azibi K, Caillaud C, Bernard MC, Poenaru L: Identification of a novel de novo mutation (G373D) in the alpha-galactosidase A gene (GLA) in a patient affected with Fabry disease. Hum Mutat. 2001 Apr;17(4):353. [PubMed ]
38. Blaydon D, Hill J, Winchester B: Fabry disease: 20 novel GLA mutations in 35 families. Hum Mutat. 2001 Nov;18(5):459. [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. 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. 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. 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. 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 ]

1. Phosphatidylinositol-glycan biosynthesis class G protein
2. PIG-G
3. GPI7 homolog
4. hGPI7

MRLGSGTFATCCVAIEVLGIAVFLRGFFPAPVRSSARAEHGAEPPAPEPSAGASSNWTTL
PPPLFSKVVIVLIDALRDDFVFGSKGVKFMPYTTYLVEKGASHSFVAEAKPPTVTMPRIK
ALMTGSLPGFVDVIRNLNSPALLEDSVIRQAKAAGKRIVFYGDETWVKLFPKHFVEYDGT
TSFFVSDYTEVDNNVTRHLDKVLKRGDWDILILHYLGLDHIGHISGPNSPLIGQKLSEMD
SVLMKIHTSLQSKERETPLPNLLVLCGDHGMSETGSHGASSTEEVNTPLILISSAFERKP
GDIRHPKHVQQTDVAATLAIALGLPIPKDSVGSLLFPVVEGRPMREQLRFLHLNTVQLSK
LLQENVPSYEKDPGFEQFKMSERLHGNWIRLYLEEKHSEVLFNLGSKVLRQYLDALKTLS
LSLSAQVAQYDIYSMMVGTVVVLEVLTLLLLSVPQALRRKAELEVPLSSPGFSLLFYLVI
LVLSAVHVIVCTSAESSCYFCGLSWLAAGGVMVLASALLCVIVSVLTNVLVGGNTPRKNP
MHPSSRWSELDLLILLGTAGHVLSLGASSFVEEEHQTWYFLVNTLCLALSQETYRNYFLG
DDGEPPCGLCVEQGHDGATAAWQDGPGCDVLERDKGHGSPSTSEVLRGREKWMVLASPWL
ILACCRLLRSLNQTGVQWAHRPDLGHWLTSSDHKAELSVLAALSLLVVFVLVQRGCSPVS
KAALALGLLGVYCYRAAIGSVRFPWRPDSKDISKGIIEARFVYVFVLGILFTGTKDLLKS
QVIAADFKLKTVGLWEIYSGLVLLAALLFRPHNLPVLAFSLLIQTLMTKFIWKPLRHDAA
EITVMHYWFGQAFFYFQGNSNNIATVDISAGFVGLDTYVEIPAVLLTAFGTYAGPVLWAS
HLVHFLSSETRSGSALSHACFCYALICSIPVFTYIVLVTSLRYHLFIWSVFSPKLLYEGM
HLLITAAVCVFFTAMDQTRLTQS

• Sulfatase (PF00884 )

• None

• 432-452 471-491 506-526 552-572 699-719 721-741 752-772 789-809 812-832 879-899 919-939 955-975

1. 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 N protein
2. PIG-N
3. MCD4 homolog

MLLFFTLGLLIHFVFFASIFDIYFTSPLVHGMTPQFTPLPPPARRLVLFVADGLRADALY
ELDENGNSRAPFIRNIIMHEGSWGISHTRVPTESRPGHVALIAGFYEDVSAVAKGWKENP
VEFDSLFNESKYTWSWGSPDILPMFAKGASGDHVYTYSYDAKREDFGAQDATKLDTWVFD
NVKDFFHHARNNQSLFSKINEEKIVFFLHLLGIDTNGHAHRPSSRDYKHNIKKVDDGVKE
IVSMFNHFYGNDGKTTFIFTSDHGMTDWGSHGAGHPSETLTPLVTWGAGIKYPQRVSAQQ
FDDAFLKEWRLENWKRLDVNQADIAPLMTSLIGVPFPLNSVGILPVDYLNNTDLFKAESM
FTNAVQILEQFKVKMTQKKEVTLPFLFTPFKLLSDSKQFNILRKARSYIKHRKFDEVVSL
CKELIHLALKGLSYYHTYDRFFLGVNVVIGFVGWISYASLLIIKSHSNLIKGVSKEVKKP
SHLLPCSFVAIGILVAFFLLIQACPWTYYVYGLLPLPIWYAVLREFQVIQDLVVSVLTYP
LSHFVGYLLAFTLGIEVLVLSFFYRYMLTAGLTAFAAWPFLTRLWTRAKMTSLSWTFFSL
LLAVFPLMPVVGRKPDISLVMGAGLLVLLLSLCVVTSLMKRKDSFIKEELLVHLLQVLST
VLSMYVVYSTQSSLLRKQGLPLMNQIISWATLASSLVVPLLSSPVLFQRLFSILLSLMST
YLLLSTGYEALFPLVLSCLMFVWINIEQETLQQSGVCCKQKLTSIQFSYNTDITQFRQLY
LDDIRRAFFLVFFLVTAFFGTGNIASINSFDLASVYCFLTVFSPFMMGALMMWKILIPFV
LVMCAFEAVQLTTQLSSKSLFLIVLVISDIMALHFFFLVKDYGSWLDIGTSISHYVIVMS
MTIFLVFLNGLAQLLTTKKLRLCGKPKSHFM

• Phosphodiest (PF01663 )
• PigN (PF04987 )

• None

• 2-24 443-463 483-503 509-529 544-564 566-586 592-612 619-639 650-670 686-706 724-744 787-807 825-845 859-879 895-915

1. Gaynor EC, Mondesert G, Grimme SJ, Reed SI, Orlean P, Emr SD: MCD4 encodes a conserved endoplasmic reticulum membrane protein essential for glycosylphosphatidylinositol anchor synthesis in yeast. Mol Biol Cell. 1999 Mar;10(3):627-48. [PubMed ]

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

MQKASVLLFLAWVCFLFYAGIALFTSGFLLTRLELTNHSSCQEPPGPGSLPWGSQGKPGA
CWMASRFSRVVLVLIDALRFDFAQPQHSHVPREPPVSLPFLGKLSSLQRILEIQPHHARL
YRSQVDPPTTTMQRLKALTTGSLPTFIDAGSNFASHAIVEDNLIKQLTSAGRRVVFMGDD
TWKDLFPGAFSKAFFFPSFNVRDLDTVDNGILEHLYPTMDSGEWDVLIAHFLGVDHCGHK
HGPHHPEMAKKLSQMDQVIQGLVERLENDTLLVVAGDHGMTTNGDHGGDSELEVSAALFL
YSPTAVFPSTPPEEPEVIPQVSLVPTLALLLGLPIPFGNIGEVMAELFSGGEDSQPHSSA
LAQASALHLNAQQVSRFLHTYSAATQDLQAKELHQLQNLFSKASADYQWLLQSPKGAEAT
LPTVIAELQQFLRGARAMCIESWARFSLVRMAGGTALLAASCFICLLASQWAISPGFPFC
PLLLTPVAWGLVGAIAYAGLLGTIELKLDLVLLGAVAAVSSFLPFLWKAWAGWGSKRPLA
TLFPIPGPVLLLLLFRLAVFFSDSFVVAEARATPFLLGSFILLLVVQLHWEGQLLPPKLL
TMPRLGTSATTNPPRHNGAYALRLGIGLLLCTRLAGLFHRCPEETPVCHSSPWLSPLASM
VGGRAKNLWYGACVAALVALLAAVRLWLRRYGNLKSPEPPMLFVRWGLPLMALGTAAYWA
LASGADEAPPRLRVLVSGASMVLPRAVAGLAASGLALLLWKPVTVLVKAGAGAPRTRTVL
TPFSGPPTSQADLDYVVPQIYRHMQEEFRGRLERTKSQGPLTVAAYQLGSVYSAAMVTAL
TLLAFPLLLLHAERISLVFLLLFLQSFLLLHLLAAGIPVTTPGPFTVPWQAVSAWALMAT
QTFYSTGHQPVFPAIHWHAAFVGFPEGHGSCTWLPALLVGANTFASHLLFAVGCPLLLLW
PFLCESQGLRKRQQPPGNEADARVRPEEEEEPLMEMRLRDAPQHFYAALLQLGLKYLFIL
GIQILACALAASILRRHLMVWKVFAPKFIFEAVGFIVSSVGLLLGIALVMRVDGAVSSWF
RQLFLAQQR

• Phosphodiest (PF01663 )

• None

• 4-24 457-477 482-502 510-530 541-561 575-595 668-688 701-721 747-767 830-850 857-877 944-964 1014-1034 1048-1068

1. 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 ]
2. Takeda S, Kadowaki S, Haga T, Takaesu H, Mitaku S: Identification of G protein-coupled receptor genes from the human genome sequence. FEBS Lett. 2002 Jun 5;520(1-3):97-101. [PubMed ]

1. Phosphatidylinositol-glycan biosynthesis class S protein

MAAAGAAATHLEVARGKRAALFFAAVAIVLGLPLWWKTTETYRASLPYSQISGLNALQLR
LMVPVTVVFTRESVPLDDQEKLPFTVVHEREIPLKYKMKIKCRFQKAYRRALDHEEEALS
SGSVQEAEAMLDEPQEQAEGSLTVYVISEHSSLLPQDMMSYIGPKRTAVVRGIMHREAFN
IIGRRIVQVAQAMSLTEDVLAAALADHLPEDKWSAEKRRPLKSSLGYEITFSLLNPDPKS
HDVYWDIEGAVRRYVQPFLNALGAAGNFSVDSQILYYAMLGVNPRFDSASSSYYLDMHSL
PHVINPVESRLGSSAASLYPVLNFLLYVPELAHSPLYIQDKDGAPVATNAFHSPRWGGIM
VYNVDSKTYNASVLPVRVEVDMVRVMEVFLAQLRLLFGIAQPQLPPKCLLSGPTSEGLMT
WELDRLLWARSVENLATATTTLTSLAQLLGKISNIVIKDDVASEVYKAVAAVQKSAEELA
SGHLASAFVASQEAVTSSELAFFDPSLLHLLYFPDDQKFAIYIPLFLPMAVPILLSLVKI
FLETRKSWRKPEKTD