1. Bicarbonate
2. Bicarbonate (HCO3-)
3. Bicarbonate anion
4. Bicarbonate ion
5. Bicarbonate ion (HCO31-)
6. Bicarbonate ions
7. carbonate
8. Carbonate (HCO31-)
9. Carbonate ion (HCO31-)
10. Carbonic acid
11. Hydrocarbonate(1-)
12. Hydrogen carbonate
13. Hydrogen carbonate (HCO3-)
14. Hydrogen carbonate anion
15. Hydrogen carbonate ion
16. Hydrogen carbonate ion (HCO3-)
17. Hydrogencarbonate
18. hydrogentrioxocarbonate
19. Monohydrogen carbonate

• Show PDF/HTML

• Cytoplasm
• Extracellular
• mitochondria

• Blood
• Cellular Cytoplasm
• Cerebrospinal Fluid

• 140350 (Hawkinsinuria)

1. Wikipedia

1. Bile salt-activated lipase precursor
2. Inositol polyphosphate 5-phosphatase OCRL-1
3. Lactotransferrin precursor
4. Serotransferrin precursor
5. Cystic fibrosis transmembrane conductance regulator
6. Electrogenic sodium bicarbonate cotransporter 1
7. Carbonic anhydrase 4 precursor
8. Sodium-driven chloride bicarbonate exchanger
9. Chloride anion exchanger
10. Sodium bicarbonate cotransporter 3
11. Testicular soluble adenylyl cyclase
12. Putative anion transporter
13. Anion transporter
14. Solute carrier family 4 member 5
15. Bestrophin-1
16. Bestrophin-2
17. Bestrophin-3
18. Bestrophin-4
19. Solute carrier family 26 member 10
20. Prestin
21. Sodium/hydrogen exchanger 10

1. BAL
2. Bile salt-stimulated lipase
3. BSSL
4. Carboxyl ester lipase
5. Sterol esterase
6. Cholesterol esterase
7. Pancreatic lysophospholipase

MGRLQLVVLGLTCCWAVASAAKLGAVYTEGGFVEGVNKKLGLLGDSVDIFKGIPFAAPTK
ALENPQPHPGWQGTLKAKNFKKRCLQATITQDSTYGDEDCLYLNIWVPQGRKQVSRDLPV
MIWIYGGAFLMGSGHGANFLNNYLYDGEEIATRGNVIVVTFNYRVGPLGFLSTGDANLPG
NYGLRDQHMAIAWVKRNIAAFGGDPNNITLFGESAGGASVSLQTLSPYNKGLIRRAISQS
GVALSPWVIQKNPLFWAKKVAEKVGCPVGDAARMAQCLKVTDPRALTLAYKVPLAGLEYP
MLHYVGFVPVIDGDFIPADPINLYANAADIDYIAGTNNMDGHIFASIDMPAINKGNKKVT
EEDFYKLVSEFTITKGLRGAKTTFDVYTESWAQDPSQENKKKTVVDFETDVLFLVPTEIA
LAQHRANAKSAKTYAYLFSHPSRMPVYPKWVGADHADDIQYVFGKPFATPTGYRPQDRTV
SKAMIAYWTNFAKTGDPNMGDSAVPTHWEPYTTENSGYLEITKKMGSSSMKRSLRTNFLR
YWTLTYLALPTVTDQEATPVPPTGDSEATPVPPTGDSETAPVPPTGDSGAPPVPPTGDSG
APPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVP
PTGDAGPPPVPPTGDSGAPPVPPTGDSGAPPVTPTGDSETAPVPPTGDSGAPPVPPTGDS
EAAPVPPTDDSKEAQMPAVIRF

• Bile Acid Biosynthesis (map00120 )

• A steryl ester + H2O = a sterol + a fatty acid

• COesterase (PF00135 )

• 1-20

ATGCTCACCATGGGGCGCCTGCAACTGGTTGTGTTGGGCCTCACCTGCTGCTGGGCAGTG
GCGAGTGCCGCGAAGCTGGGCGCCGTGTACACAGAAGGTGGGTTCGTGGAAGGCGTCAAT
AAGAAGCTCGGCCTCCTGGGTGACTCTGTGGACATCTTCAAGGGCATCCCCTTCGCAGCT
CCCACCAAGGCCCTGGAAAATCCTCAGCCACATCCTGGCTGGCAAGGGACCCTGAAGGCC
AAGAACTTCAAGAAGAGATGCCTGCAGGCCACCATCACCCAGGACAGCACCTACGGGGAT
GAAGACTGCCTGTACCTCAACATTTGGGTGCCCCAGGGCAGGAAGCAAGTCTCCCGGGAC
CTGCCCGTTATGATCTGGATCTATGGAGGCGCCTTCCTCATGGGGTCCGGCCATGGGGCC
AACTTCCTCAACAACTACCTGTATGACGGCGAGGAGATCGCCACACGCGGAAACGTCATC
GTGGTCACCTTCAACTACCGTGTCGGCCCCCTTGGGTTCCTCAGCACTGGGGACGCCAAT
CTGCCAGGTAACTATGGCCTTCGGGATCAGCACATGGCCATTGCTTGGGTGAAGAGGAAT
ATCGCGGCCTTCGGGGGGGACCCCAACAACATCACGCTCTTCGGGGAGTCTGCTGGAGGT
GCCAGCGTCTCTCTGCAGACCCTCTCCCCCTACAACAAGGGCCTCATCCGGCGAGCCATC
AGCCAGAGCGGCGTGGCCCTGAGTCCCTGGGTCATCCAGAAAAACCCACTCTTCTGGGCC
AAAAAGGTGGCTGAGAAGGTGGGTTGCCCTGTGGGTGATGCCGCCAGGATGGCCCAGTGT
CTGAAGGTTACTGATCCCCGAGCCCTGACGCTGGCCTATAAGGTGCCGCTGGCAGGCCTG
GAGTACCCCATGCTGCACTATGTGGGCTTCGTCCCTGTCATTGATGGAGACTTCATCCCC
GCTGACCCGATCAACCTGTACGCCAACGCCGCCGACATCGACTATATAGCAGGCACCAAC
AACATGGACGGCCACATCTTCGCCAGCATCGACATGCCTGCCATCAACAAGGGCAACAAG
AAAGTCACGGAGGAGGACTTCTACAAGCTGGTCAGTGAGTTCACAATCACCAAGGGGCTC
AGAGGCGCCAAGACGACCTTTGATGTCTACACCGAGTCCTGGGCCCAGGACCCATCCCAG
GAGAATAAGAAGAAGACTGTGGTGGACTTTGAGACCGATGTCCTCTTCCTGGTGCCCACC
GAGATTGCCCTAGCCCAGCACAGAGCCAATGCCAAGAGTGCCAAGACCTACGCCTACCTG
TTTTCCCATCCCTCTCGGATGCCCGTCTACCCCAAATGGGTGGGGGCCGACCATGCAGAT
GACATTCAGTACGTTTTCGGGAAGCCCTTCGCCACCCCCACGGGCTACCGGCCCCAAGAC
AGGACAGTCTCTAAGGCCATGATCGCCTACTGGACCAACTTTGCCAAAACAGGGGACCCC
AACATGGGCGACTCGGCTGTGCCCACACACTGGGAACCCTACACTACGGAAAACAGCGGC
TACCTGGAGATCACCAAGAAGATGGGCAGCAGCTCCATGAAGCGGAGCCTGAGAACCAAC
TTCCTGCGCTACTGGACCCTCACCTATCTGGCGCTGCCCACAGTGACCGACCAGGAGGCC
ACCCCTGTGCCCCCCACAGGGGACTCCGAGGCCACTCCCGTGCCCCCCACGGGTGACTCC
GAGACCGCCCCCGTGCCGCCCACGGGTGACTCCGGGGCCCCCCCCGTGCCGCCCACGGGT
GACTCCGGGGCCCCCCCCGTGCCGCCCACGGGTGACTCCGGGGCCCCCCCCGTGCCGCCC
ACGGGTGACTCCGGGGCCCCCCCCGTGCCGCCCACGGGTGACTCCGGGGCCCCCCCCGTG
CCGCCCACGGGTGACTCCGGGGCCCCCCCCGTGCCGCCCACGGGTGACTCCGGCGCCCCC
CCCGTGCCGCCCACGGGTGACGCCGGGCCCCCCCCCGTGCCGCCCACGGGTGACTCCGGC
GCCCCCCCCGTGCCGCCCACGGGTGACTCCGGGGCCCCCCCCGTGACCCCCACGGGTGAC
TCCGAGACCGCCCCCGTGCCGCCCACGGGTGACTCCGGGGCCCCCCCTGTGCCCCCCACG
GGTGACTCTGAGGCTGCCCCTGTGCCCCCCACAGATGACTCCAAGGAAGCTCAGATGCCT
GCAGTCATTAGGTTTTAG

1. Nilsson J, Blackberg L, Carlsson P, Enerback S, Hernell O, Bjursell G: cDNA cloning of human-milk bile-salt-stimulated lipase and evidence for its identity to pancreatic carboxylic ester hydrolase. Eur J Biochem. 1990 Sep 11;192(2):543-50. [PubMed ]
2. Hui DY, Kissel JA: Sequence identity between human pancreatic cholesterol esterase and bile salt-stimulated milk lipase. FEBS Lett. 1990 Dec 10;276(1-2):131-4. [PubMed ]
3. Baba T, Downs D, Jackson KW, Tang J, Wang CS: Structure of human milk bile salt activated lipase. Biochemistry. 1991 Jan 15;30(2):500-10. [PubMed ]
4. Lidberg U, Nilsson J, Stromberg K, Stenman G, Sahlin P, Enerback S, Bjursell G: Genomic organization, sequence analysis, and chromosomal localization of the human carboxyl ester lipase (CEL) gene and a CEL-like (CELL) gene. Genomics. 1992 Jul;13(3):630-40. [PubMed ]
5. Roudani S, Miralles F, Margotat A, Escribano MJ, Lombardo D: Bile salt-dependent lipase transcripts in human fetal tissues. Biochim Biophys Acta. 1995 Oct 17;1264(1):141-50. [PubMed ]
6. Christie DL, Cleverly DR, O'Connor CJ: Human milk bile-salt stimulated lipase. Sequence similarity with rat lysophospholipase and homology with the active site region of cholinesterases. FEBS Lett. 1991 Jan 28;278(2):190-4. [PubMed ]
7. Wang CS, Dashti A, Jackson KW, Yeh JC, Cummings RD, Tang J: Isolation and characterization of human milk bile salt-activated lipase C-tail fragment. Biochemistry. 1995 Aug 22;34(33):10639-44. [PubMed ]
8. Mechref Y, Chen P, Novotny MV: Structural characterization of the N-linked oligosaccharides in bile salt-stimulated lipase originated from human breast milk. Glycobiology. 1999 Mar;9(3):227-34. [PubMed ]
9. Terzyan S, Wang CS, Downs D, Hunter B, Zhang XC: Crystal structure of the catalytic domain of human bile salt activated lipase. Protein Sci. 2000 Sep;9(9):1783-90. [PubMed ]

1. Lowe oculocerebrorenal syndrome protein

MEPPLPVGAQPLATVEGMEMKGPLREPCALTLAQRNGQYELIIQLHEKEQHVQDIIPINS
HFRCVQEAEETLLIDIASNSGCKIRVQGDWIRERRFEIPDEEHCLKFLSAVLAAQKAQSQ
LLVPEQKDSSSWYQKLDTKDKPSVFSGLLGFEDNFSSMNLDKKINSQNQPTGIHREPPPP
PFSVNKMLPREKEASNKEQPKVTNTMRKLFVPNTQSGQREGLIKHILAKREKEYVNIQTF
RFFVGTWNVNGQSPDSGLEPWLNCDPNPPDIYCIGFQELDLSTEAFFYFESVKEQEWSMA
VERGLHSKAKYKKVQLVRLVGMMLLIFARKDQCRYIRDIATETVGTGIMGKMGNKGGVAV
RFVFHNTTFCIVNSHLAAHVEDFERRNQDYKDICARMSFVVPNQTLPQLNIMKHEVVIWL
GDLNYRLCMPDANEVKSLINKKDLQRLLKFDQLNIQRTQKKAFVDFNEGEIKFIPTYKYD
SKTDRWDSSGKCRVPAWCDRILWRGTNVNQLNYRSHMELKTSDHKPVSALFHIGVKVVDE
RRYRKVFEDSVRIMDRMENDFLPSLELSRREFVFENVKFRQLQKEKFQISNNGQVPCHFS
FIPKLNDSQYCKPWLRAEPFEGYLEPNETVDISLDVYVSKDSVTILNSGEDKIEDILVLH
LDRGKDYFLTISGNYLPSCFGTSLEALCRMKRPIREVPVTKLIDLEEDSFLEKEKSLLQM
VPLDEGASERPLQVPKEIWLLVDHLFKYACHQEDLFQTPGMQEELQQIIDCLDTSIPETI
PGSNHSVAEALLIFLEALPEPVICYELYQRCLDSAYDPRICRQVISQLPRCHRNVFRYLM
AFLRELLKFSEYNSVNANMIATLFTSLLLRPPPNLMARQTPSDRQRAIQFLLGFLLGSEE
D

• Inositol Metabolism (map00562 )
• Phosphatidylinositol signaling system (map04070 )

• 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate

• Exo_endo_phos (PF03372 )
• RhoGAP (PF00620 )

• None

• None

ATGAAGTTTTTTGTTTTTAAGAGCTTCCTTAGTGATTGTTATAGGAGCCTCCTAGACAAG
TCTCAGCTCCCAGCTCCCCGCTCCCGGCTCCCGGCGCCCGGCGCCCGGCGCGGAGCTGTT
CCTCAAACGACACGCAGCCGAGGTGGGTGGGTGTGGGGACGCGGGAGCCAGTGTCGTCGG
ATCGGCCCGCAGTCCGCTGTCCTGCTGAGCCCGGAGGCCGCCTGGATGGAGCCGCCGCTC
CCGGTCGGAGCCCAGCCGCTTGCCACTGTCGAGGGTATGGAGATGAAGGGTCCTCTCCGG
GAGCCCTGCGCCCTGACCCTAGCCCAGAGGAACGGGCAATATGAGTTAATAATCCAGTTG
CATGAGAAGGAACAGCATGTTCAAGATATCATTCCTATAAATAGCCACTTCAGATGTGTT
CAAGAAGCAGAAGAAACTCTTTTGATTGACATAGCTTCTAACAGTGGCTGCAAAATTCGG
GTTCAGGGGGACTGGATCAGAGAGCGCCGCTTTGAAATCCCTGATGAGGAACACTGTTTG
AAGTTCCTCTCAGCTGTCCTTGCTGCTCAGAAAGCTCAGTCACAGCTTCTTGTTCCAGAG
CAAAAGGACTCATCTAGCTGGTACCAGAAATTAGACACTAAGGACAAACCTTCTGTTTTT
TCAGGGCTTCTTGGATTTGAAGACAATTTTTCTTCTATGAATTTGGACAAGAAAATAAAT
TCACAAAATCAGCCTACTGGGATTCATCGGGAACCCCCACCTCCACCCTTTTCAGTGAAT
AAAATGCTTCCACGTGAAAAAGAAGCTTCTAACAAGGAGCAGCCCAAAGTGACCAACACC
ATGCGGAAGCTCTTTGTACCAAATACCCAATCTGGGCAGCGGGAGGGTCTCATCAAACAT
ATCCTGGCAAAGCGAGAGAAAGAATATGTCAACATTCAGACTTTCAGATTTTTTGTTGGA
ACTTGGAATGTGAATGGCCAGTCTCCAGATAGCGGGTTAGAACCTTGGCTGAACTGTGAT
CCCAATCCTCCTGATATCTACTGCATTGGATTCCAAGAACTGGACTTGAGCACAGAAGCC
TTCTTCTACTTTGAATCTGTGAAGGAACAAGAATGGTCCATGGCTGTAGAGAGAGGTTTG
CATTCCAAAGCCAAGTATAAGAAAGTTCAACTGGTGCGCCTTGTTGGGATGATGCTTCTT
ATATTTGCCAGAAAGGATCAGTGTCGATACATTCGTGATATTGCTACAGAAACAGTTGGA
ACTGGAATCATGGGGAAAATGGGAAACAAAGGTGGGGTAGCTGTGAGATTTGTATTTCAC
AACACCACCTTTTGCATTGTCAATTCCCATCTGGCTGCACACGTGGAGGACTTTGAGAGA
AGGAATCAAGATTATAAGGACATTTGTGCGAGAATGAGTTTTGTGGTCCCAAATCAGACC
CTCCCGCAGTTGAACATCATGAAACATGAGGTTGTCATTTGGTTGGGAGATTTGAATTAT
AGACTTTGCATGCCTGATGCCAATGAGGTGAAAAGTCTTATTAATAAGAAAGACCTTCAG
AGACTCTTGAAATTCGACCAGCTAAATATTCAGCGCACACAGAAAAAAGCTTTTGTTGAC
TTCAATGAAGGGGAAATCAAGTTCATCCCCACTTATAAGTATGACTCTAAAACAGACCGG
TGGGATTCCAGTGGGAAATGCCGGGTTCCAGCCTGGTGTGACCGAATTCTTTGGAGAGGA
ACAAATGTTAATCAGCTTAATTATCGGAGTCACATGGAACTGAAAACCAGCGACCACAAG
CCTGTTAGCGCCCTCTTCCATATTGGGGTGAAGGTTGTGGATGAACGAAGGTACCGGAAA
GTCTTTGAAGATAGTGTACGCATCATGGACAGAATGGAAAATGACTTCCTTCCTTCCTTA
GAACTCAGCAGGAGGGAGTTTGTGTTTGAAAATGTGAAGTTTCGGCAACTACAAAAGGAG
AAGTTCCAGATCAGCAACAATGGACAGGTTCCCTGCCATTTTTCTTTCATCCCTAAACTT
AATGACAGCCAGTACTGCAAGCCATGGCTTCGGGCTGAACCTTTTGAGGGCTACTTGGAG
CCAAATGAGACAGTGGACATTTCTCTTGATGTGTATGTCAGCAAAGACTCTGTAACCATC
CTGAACTCGGGAGAAGATAAGATTGAAGATATTCTCGTCCTTCACCTGGATCGAGGCAAA
GATTACTTCTTGACTATCAGTGGAAATTACCTCCCAAGTTGTTTTGGCACATCCTTAGAG
GCTCTGTGCCGTATGAAAAGACCAATCCGAGAAGTTCCTGTTACCAAACTCATAGACTTG
GAGAAATCCCTTCTGCAAATGGTTCCTTTGGATGAAGGTGCCAGTGAGAGACCCCTTCAG
GTTCCCAAGGAGATCTGGCTTCTAGTAGATCACCTATTCAAATACGCCTGTCACCAGGAG
GACCTGTTCCAGACCCCTGGAATGCAGGAAGAGCTCCAGCAGATCATTGATTGTCTGGAT
ACCAGCATTCCTGAGACAATCCCTGGCAGCAACCACTCTGTGGCTGAAGCACTGCTCATT
TTCTTGGAAGCCCTGCCAGAGCCAGTCATCTGTTACGAGCTGTATCAGCGATGTCTTGAC
TCTGCTTATGATCCCCGGATCTGCCGACAGGTGATCTCCCAGCTTCCGAGATGCCATAGA
AATGTTTTCCGTTACTTGATGGCATTCCTTCGAGAACTCTTAAAATTCTCTGAATACAAT
AGCGTCAATGCCAACATGATCGCTACTCTCTTCACTAGTCTTCTCCTGAGGCCTCCACCC
AACCTTATGGCAAGACAGACTCCAAGTGACCGCCAGCGTGCTATTCAGTTCCTTCTGGGC
TTTCTGCTTGGGAGCGAAGAAGACTAA

1. Attree O, Olivos IM, Okabe I, Bailey LC, Nelson DL, Lewis RA, McInnes RR, Nussbaum RL: The Lowe's oculocerebrorenal syndrome gene encodes a protein highly homologous to inositol polyphosphate-5-phosphatase. Nature. 1992 Jul 16;358(6383):239-42. [PubMed ]
2. Nussbaum RL, Orrison BM, Janne PA, Charnas L, Chinault AC: Physical mapping and genomic structure of the Lowe syndrome gene OCRL1. Hum Genet. 1997 Feb;99(2):145-50. [PubMed ]
3. Leahey AM, Charnas LR, Nussbaum RL: Nonsense mutations in the OCRL-1 gene in patients with the oculocerebrorenal syndrome of Lowe. Hum Mol Genet. 1993 Apr;2(4):461-3. [PubMed ]
4. Zhang X, Jefferson AB, Auethavekiat V, Majerus PW: The protein deficient in Lowe syndrome is a phosphatidylinositol-4,5-bisphosphate 5-phosphatase. Proc Natl Acad Sci U S A. 1995 May 23;92(11):4853-6. [PubMed ]
5. Zhang X, Hartz PA, Philip E, Racusen LC, Majerus PW: Cell lines from kidney proximal tubules of a patient with Lowe syndrome lack OCRL inositol polyphosphate 5-phosphatase and accumulate phosphatidylinositol 4,5-bisphosphate. J Biol Chem. 1998 Jan 16;273(3):1574-82. [PubMed ]
6. Lin T, Orrison BM, Leahey AM, Suchy SF, Bernard DJ, Lewis RA, Nussbaum RL: Spectrum of mutations in the OCRL1 gene in the Lowe oculocerebrorenal syndrome. Am J Hum Genet. 1997 Jun;60(6):1384-8. [PubMed ]
7. Lin T, Orrison BM, Suchy SF, Lewis RA, Nussbaum RL: Mutations are not uniformly distributed throughout the OCRL1 gene in Lowe syndrome patients. Mol Genet Metab. 1998 May;64(1):58-61. [PubMed ]
8. Kawano T, Indo Y, Nakazato H, Shimadzu M, Matsuda I: Oculocerebrorenal syndrome of Lowe: three mutations in the OCRL1 gene derived from three patients with different phenotypes. Am J Med Genet. 1998 Jun 5;77(5):348-55. [PubMed ]
9. Kubota T, Sakurai A, Arakawa K, Shimazu M, Wakui K, Furihata K, Fukushima Y: Identification of two novel mutations in the OCRL1 gene in Japanese families with Lowe syndrome. Clin Genet. 1998 Sep;54(3):199-202. [PubMed ]
10. Monnier N, Satre V, Lerouge E, Berthoin F, Lunardi J: OCRL1 mutation analysis in French Lowe syndrome patients: implications for molecular diagnosis strategy and genetic counseling. Hum Mutat. 2000;16(2):157-65. [PubMed ]
11. Roschinger W, Muntau AC, Rudolph G, Roscher AA, Kammerer S: Carrier assessment in families with lowe oculocerebrorenal syndrome: novel mutations in the OCRL1 gene and correlation of direct DNA diagnosis with ocular examination. Mol Genet Metab. 2000 Mar;69(3):213-22. [PubMed ]

1. Lactoferrin
2. Talalactoferrin alfa[Contains: Kaliocin-1
3. Lactoferroxin A
4. Lactoferroxin B
5. Lactoferroxin C]

MKLVFLVLLFLGALGLCLAGRRRSVQWCAVSQPEATKCFQWQRNMRKVRGPPVSCIKRDS
PIQCIQAIAENRADAVTLDGGFIYEAGLAPYKLRPVAAEVYGTERQPRTHYYAVAVVKKG
GSFQLNELQGLKSCHTGLRRTAGWNVPIGTLRPFLNWTGPPEPIEAAVARFFSASCVPGA
DKGQFPNLCRLCAGTGENKCAFSSQEPYFSYSGAFKCLRDGAGDVAFIRESTVFEDLSDE
AERDEYELLCPDNTRKPVDKFKDCHLARVPSHAVVARSVNGKEDAIWNLLRQAQEKFGKD
KSPKFQLFGSPSGQKDLLFKDSAIGFSRVPPRIDSGLYLGSGYFTAIQNLRKSEEEVAAR
RARVVWCAVGEQELRKCNQWSGLSEGSVTCSSASTTEDCIALVLKGEADAMSLDGGYVYT
AGKCGLVPVLAENYKSQQSSDPDPNCVDRPVEGYLAVAVVRRSDTSLTWNSVKGKKSCHT
AVDRTAGWNIPMGLLFNQTGSCKFDEYFSQSCAPGSDPRSNLCALCIGDEQGENKCVPNS
NERYYGYTGAFRCLAENAGDVAFVKDVTVLQNTDGNNNEAWAKDLKLADFALLCLDGKRK
PVTEARSCHLAMAPNHAVVSRMDKVERLKQVLLHQQAKFGRNGSDCPDKFCLFQSETKNL
LFNDNTECLARLHGKTTYEKYLGPQYVAGITNLKKCSTSPLLEACEFLRK

• Transferrin (PF00405 )

• 1-19

ATGAAACTTGTCTTCCTCGTCCTGCTGTTCCTCGGGGCCCTCGGACTGTGTCTGGCTGGC
CGTAGGAGAAGGAGTGTTCAGTGGTGCGCCGTATCCCAACCCGAGGCCACAAAATGCTTC
CAATGGCAAAGGAATATGAGAAAAGTGCGTGGCCCTCCTGTCAGCTGCATAAAGAGAGAC
TCCCCCATCCAGTGTATCCAGGCCATTGCGGAAAACAGGGCCGATGCTGTGACCCTTGAT
GGTGGTTTCATATACGAGGCAGGCCTGGCCCCCTACAAACTGCGACCTGTAGCGGCGGAA
GTCTACGGGACCGAAAGACAGCCACGAACTCACTATTATGCCGTGGCTGTGGTGAAGAAG
GGCGGCAGCTTTCAGCTGAACGAACTGCAAGGTCTGAAGTCCTGCCACACAGGCCTTCGC
AGGACCGCTGGATGGAATGTCCCTACAGGGACACTTCGTCCATTCTTGAATTGGACGGGT
CCACCTGAGCCCATTGAGGCAGCTGTGGCCAGGTTCTTCTCAGCCAGCTGTGTTCCCGGT
GCAGATAAAGGACAGTTCCCCAACCTGTGTCGCCTGTGTGCGGGGACAGGGGAAAACAAA
TGTGCCTTCTCCTCCCAGGAACCGTACTTCAGCTACTCTGGTGCCTTCAAGTGTCTGAGA
GACGGGGCTGGAGACGTGGCTTTTATCAGAGAGAGCACAGTGTTTGAGGACCTGTCAGAC
GAGGCTGAAAGGGACGAGTATGAGTTACTCTGCCCAGACAACACTCGGAAGCCAGTGGAC
AAGTTCAAAGACTGCCATCTGGCCCGGGTCCCTTCTCATGCCGTTGTGGCACGAAGTGTG
AATGGCAAGGAGGATGCCATCTGGAATCTTCTCCGCCAGGCACAGGAAAAGTTTGGAAAG
GACAAGTCACCGAAATTCCAGCTCTTTGGCTCCCCTAGTGGGCAGAAAGATCTGCTGTTC
AAGGACTCTGCCATTGGGTTTTCGAGGGTGCCCCCGAGGATAGATTCTGGGCTGTACCTT
GGCTCCGGCTACTTCACTGCCATCCAGAACTTGAGGAAAAGTGAGGAGGAAGTGGCTGCC
CGGCGTGCGCGGGTCGTGTGGTGTGCGGTGGGCGAGCAGGAGCTGCGCAAGTGTAACCAG
TGGAGTGGCTTGAGCGAAGGCAGCGTGACCTGCTCCTCGGCCTCCACCACAGAGGACTGC
ATCGCCCTGGTGCTGAAAGGAGAAGCTGATGCCATGAGTTTGGATGGAGGATATGTGTAC
ACTGCATGCAAATGTGGTTTGGTGCCTGTCCTGGCAGAGAACTACAAATCCCAACAAAGC
AGTGACCCTGATCCTAACTGTGTGGATAGACCTGTGGAAGGATATCTTGCTGTGGCGGTG
GTTAGGAGATCAGACACTAGCCTTACCTGGAACTCTGTGAAAGGCAAGAAGTCCTGCCAC
ACCGCCGTGGACAGGACTGCAGGCTGGAATATCCCCATGGGCCTGCTCTTCAACCAGACG
GGCTCCTGCAAATTTGATGAATATTTCAGTCAAAGCTGTGCCCCTGGGTCTGACCCGAGA
TCTAATCTCTGTGCTCTGTGTATTGGCGACGAGCAGGGTGAGAATAAGTGCGTGCCCAAC
AGCAACGAGAGATACTACGGCTACACTGGGGCTTTCCGGTGCCTGGCTGAGAATGCTGGA
GACGTTGCATTTGTGAAAGATGTCACTGTCTTGCAGAACACTGATGGAAATAACAATGAG
GCATGGGCTAAGGATTTGAAGCTGGCAGACTTTGCGCTGCTGTGCCTCGATGGCAAACGG
AAGCCTGTGACTGAGGCTAGAAGCTGCCATCTTGCCATGGCCCCGAATCATGCCGTGGTG
TCTCGGATGGATAAGGTGGAACGCCTGAAACAGGTGCTGCTCCACCAACAGGCTAAATTT
GGGAGAAATGGATCTGACTGCCCGGACAAGTTTTGCTTATTCCAGTCTGAAACCAAAAAC
CTTCTGTTCAATGACAACACTGAGTGTCTGGCCAGACTCCATGGCAAAACAACATATGAA
AAATATTTGGGACCACAGTATGTCGCAGGCATTACTAATCTGAAAAAGTGCTCAACCTCC
CCCCTCCTGGAAGCCTGTGAATTCCTCAGGAAGTAA

1. Rey MW, Woloshuk SL, deBoer HA, Pieper FR: Complete nucleotide sequence of human mammary gland lactoferrin. Nucleic Acids Res. 1990 Sep 11;18(17):5288. [PubMed ]
2. Teng CT, Liu Y, Yang N, Walmer D, Panella T: Differential molecular mechanism of the estrogen action that regulates lactoferrin gene in human and mouse. Mol Endocrinol. 1992 Nov;6(11):1969-81. [PubMed ]
3. Powell MJ, Ogden JE: Nucleotide sequence of human lactoferrin cDNA. Nucleic Acids Res. 1990 Jul 11;18(13):4013. [PubMed ]
4. Metz-Boutigue MH, Jolles J, Mazurier J, Schoentgen F, Legrand D, Spik G, Montreuil J, Jolles P: Human lactotransferrin: amino acid sequence and structural comparisons with other transferrins. Eur J Biochem. 1984 Dec 17;145(3):659-76. [PubMed ]
5. Metz-Boutigue MH, Mazurier J, Jolles J, Spik G, Montreuil J, Jolles P: The present state of the human lactotransferrin sequence. Study and alignment of the cyanogen bromide fragments and characterization of N- and C-terminal domains. Biochim Biophys Acta. 1981 Sep 29;670(2):243-54. [PubMed ]
6. Metz-Boutigue MH, Jolles J, Mazurier J, Spik G, Montreuil J, Jolles P: An 88 amino acid long C-terminal sequence of human lactotransferrin. FEBS Lett. 1982 Jun 1;142(1):107-10. [PubMed ]
7. Rado TA, Wei XP, Benz EJ Jr: Isolation of lactoferrin cDNA from a human myeloid library and expression of mRNA during normal and leukemic myelopoiesis. Blood. 1987 Oct;70(4):989-93. [PubMed ]
8. Tani F, Iio K, Chiba H, Yoshikawa M: Isolation and characterization of opioid antagonist peptides derived from human lactoferrin. Agric Biol Chem. 1990 Jul;54(7):1803-10. [PubMed ]
9. Viejo-Diaz M, Andres MT, Perez-Gil J, Sanchez M, Fierro JF: Potassium efflux induced by a new lactoferrin-derived peptide mimicking the effect of native human lactoferrin on the bacterial cytoplasmic membrane. Biochemistry (Mosc). 2003 Feb;68(2):217-27. [PubMed ]
10. Anderson BF, Baker HM, Norris GE, Rice DW, Baker EN: Structure of human lactoferrin: crystallographic structure analysis and refinement at 2.8 A resolution. J Mol Biol. 1989 Oct 20;209(4):711-34. [PubMed ]
11. Nicholson H, Anderson BF, Bland T, Shewry SC, Tweedie JW, Baker EN: Mutagenesis of the histidine ligand in human lactoferrin: iron binding properties and crystal structure of the histidine-253-->methionine mutant. Biochemistry. 1997 Jan 14;36(2):341-6. [PubMed ]
12. Sun XL, Baker HM, Shewry SC, Jameson GB, Baker EN: Structure of recombinant human lactoferrin expressed in Aspergillus awamori. Acta Crystallogr D Biol Crystallogr. 1999 Feb;55(Pt 2):403-7. [PubMed ]
13. Jameson GB, Anderson BF, Norris GE, Thomas DH, Baker EN: Structure of human apolactoferrin at 2.0 A resolution. Refinement and analysis of ligand-induced conformational change. Acta Crystallogr D Biol Crystallogr. 1998 Nov 1;54(Pt 6 Pt 2):1319-35. [PubMed ]
14. Klintworth GK, Sommer JR, Obrian G, Han L, Ahmed MN, Qumsiyeh MB, Lin PY, Basti S, Reddy MK, Kanai A, Hotta Y, Sugar J, Kumaramanickavel G, Munier F, Schorderet DF, El Matri L, Iwata F, Kaiser-Kupfer M, Nagata M, Nakayasu K, Hejtmancik JF, Teng CT: Familial subepithelial corneal amyloidosis (gelatinous drop-like corneal dystrophy): exclusion of linkage to lactoferrin gene. Mol Vis. 1998 Dec 31;4:31. [PubMed ]

1. Transferrin
2. Siderophilin
3. Beta-1-metal- binding globulin

MRLAVGALLVCAVLGLCLAVPDKTVRWCAVSEHEATKCQSFRDHMKSVIPSDGPSVACVK
KASYLDCIRAIAANEADAVTLDAGLVYDAYLAPNNLKPVVAEFYGSKEDPQTFYYAVAVV
KKDSGFQMNQLRGKKSCHTGLGRSAGWNIPIGLLYCDLPEPRKPLEKAVANFFSGSCAPC
ADGTDFPQLCQLCPGCGCSTLNQYFGYSGAFKCLKDGAGDVAFVKHSTIFENLANKADRD
QYELLCLDNTRKPVDEYKDCHLAQVPSHTVVARSMGGKEDLIWELLNQAQEHFGKDKSKE
FQLFSSPHGKDLLFKDSAHGFLKVPPRMDAKMYLGYEYVTAIRNLREGTCPEAPTDECKP
VKWCALSHHERLKCDEWSVNSVGKIECVSAETTEDCIAKIMNGEADAMSLDGGFVYIAGK
CGLVPVLAENYNKSDNCEDTPEAGYFAVAVVKKSASDLTWDNLKGKKSCHTAVGRTAGWN
IPMGLLYNKINHCRFDEFFSEGCAPGSKKDSSLCKLCMGSGLNLCEPNNKEGYYGYTGAF
RCLVEKGDVAFVKHQTVPQNTGGKNPDPWAKNLNEKDYELLCLDGTRKPVEEYANCHLAR
APNHAVVTRKDKEACVHKILRQQQHLFGSNVTDCSGNFCLFRSETKDLLFRDDTVCLAKL
HDRNTYEKYLGEEYVKAVGNLRKCSTSSLLEACTFRRP

• Transferrin (PF00405 )

• 1-19

ATGAGGCTCGCCGTGGGAGCCCTGCTGGTCTGCGCCGTCCTGGGGCTGTGTCTGGCTGTC
CCTGATAAAACTGTGAGATGGTGTGCAGTGTCGGAGCATGAGGCCACTAAGTGCCAGAGT
TTCCGCGACCATATGAAAAGCGTCATTCCATCCGATGGTCCCAGTGTTGCTTGTGTGAAG
AAAGCCTCCTACCTTGATTGCATCAGGGCCATTGCGGCAAACGAAGCGGATGCTGTGACA
CTGGATGCAGGTTTGGTGTATGATGCTTACTTGGCTCCCAATAACCTGAAGCCTGTGGTG
GCAGAGTTCTATGGGTCAAAAGAGGATCCACAGACTTTCTATTATGCTGTTGCTGTGGTG
AAGAAGGATAGTGGCTTCCAGATGAACCAGCTTCGAGGCAAGAAGTCCTGCCACACGGGT
CTAGGCAGGTCCGCTGGGTGGAACATCCCCATAGGCTTACTTTACTGTGACTTACCTGAG
CCACGTAAACCTCTTGAGAAAGCAGTGGCCAATTTCTTCTCGGGCAGCTGTGCCCCTTGT
GCGGATGGGACGGACTTCCCCCAGCTGTGTCAACTGTGTCCAGGGTGTGGCTGCTCCACC
CTTAACCAATACTTCGGCTACTCGGGAGCCTTCAAGTGTCTGAAGGATGGTGCTGGGGAT
GTGGCCTTTGTCAAGCACTCGACTATATTTGAGAACTTGGCAAACAAGGCTGACAGGGAC
CAGTATGAGCTGCTTTGCCTAGACAACACCCGGAAGCCGGTAGATGAATACAAGGACTGC
CACTTGGCCCAGGTCCCTTCTCATACCGTCGTGGCCCGAAGTATGGGCGGCAAGGAGGAC
TTGATCTGGGAGCTTCTCAACCAGGCCCAGGAACATTTTGGCAAAGACAAATCAAAAGAA
TTCCAACTATTCAGCTCTCCTCATGGGAAGGACCTGCTGTTTAAGGACTCTGCCCACGGG
TTTTTAAAAGTCCCCCCAAGGATGGATGCCAAGATGTACCTGGGCTATGAGTATGTCACT
GCCATCCGGAATCTACGGGAAGGCACATGCCCAGAAGCCCCAACAGATGAATGCAAGCCT
GTGAAGTGGTGTGCGCTGAGCCACCACGAGAGGCTCAAGTGTGATGAGTGGAGTGTTAAC
AGTGTAGGGAAAATAGAGTGTGTATCAGCAGAGACCACCGAAGACTGCATCGCCAAGATC
ATGAATGGAGAAGCTGATGCCATGAGCTTGGATGGAGGGTTTGTCTACATAGCGGGCAAG
TGTGGTCTGGTGCCTGTCTTGGCAGAAAACTACAATAAGAGCGATAATTGTGAGGATACA
CCAGAGGCAGGGTATTTTGCTGTAGCAGTGGTGAAGAAATCAGCTTCTGACCTCACCTGG
GACAATCTGAAAGGCAAGAAGTCCTGCCATACGGCAGTTGGCAGAACCGCTGGCTGGAAC
ATCCCCATGGGCCTGCTCTACAATAAGATCAACCACTGCAGATTTGATGAATTTTTCAGT
GAAGGTTGTGCCCCTGGGTCTAAGAAAGACTCCAGTCTCTGTAAGCTGTGTATGGGCTCA
GGCCTAAACCTGTGTGAACCCAACAACAAAGAGGGATACTACGGCTACACAGGCGCTTTC
AGGTGTCTGGTTGAGAAGGGAGATGTGGCCTTTGTGAAACACCAGACTGTCCCACAGAAC
ACTGGGGGAAAAAACCCTGATCCATGGGCTAAGAATCTGAATGAAAAAGACTATGAGTTG
CTGTGCCTTGATGGTACCAGGAAACCTGTGGAGGAGTATGCGAACTGCCACCTGGCCAGA
GCCCCGAATCACGCTGTGGTCACACGGAAAGATAAGGAAGCTTGCGTCCACAAGATATTA
CGTCAACAGCAGCACCTATTTGGAAGCAACGTAACTGACTGCTCGGGCAACTTTTGTTTG
TTCCGGTCGGAAACCAAGGACCTTCTGTTCAGAGATGACACAGTATGTTTGGCCAAACTT
CATGACAGAAACACATATGAAAAATACTTAGGAGAAGAATATGTCAAGGCTGTTGGTAAC
CTGAGAAAATGCTCCACCTCATCACTCCTGGAAGCCTGCACTTTCCGTAGACCTTAA

1. Yang F, Lum JB, McGill JR, Moore CM, Naylor SL, van Bragt PH, Baldwin WD, Bowman BH: Human transferrin: cDNA characterization and chromosomal localization. Proc Natl Acad Sci U S A. 1984 May;81(9):2752-6. [PubMed ]
2. Schaeffer E, Lucero MA, Jeltsch JM, Py MC, Levin MJ, Chambon P, Cohen GN, Zakin MM: Complete structure of the human transferrin gene. Comparison with analogous chicken gene and human pseudogene. Gene. 1987;56(1):109-16. [PubMed ]
3. Hershberger CL, Larson JL, Arnold B, Rosteck PR Jr, Williams P, DeHoff B, Dunn P, O'Neal KL, Riemen MW, Tice PA, et al.: A cloned gene for human transferrin. Ann N Y Acad Sci. 1991 Dec 27;646:140-54. [PubMed ]
4. Beutler E, Gelbart T, Lee P, Trevino R, Fernandez MA, Fairbanks VF: Molecular characterization of a case of atransferrinemia. Blood. 2000 Dec 15;96(13):4071-4. [PubMed ]
5. Adrian GS, Korinek BW, Bowman BH, Yang F: The human transferrin gene: 5' region contains conserved sequences which match the control elements regulated by heavy metals, glucocorticoids and acute phase reaction. Gene. 1986;49(2):167-75. [PubMed ]
6. Lucero MA, Schaeffer E, Cohen GN, Zakin MM: The 5' region of the human transferrin gene: structure and potential regulatory sites. Nucleic Acids Res. 1986 Nov 11;14(21):8692. [PubMed ]
7. MacGillivray RT, Mendez E, Shewale JG, Sinha SK, Lineback-Zins J, Brew K: The primary structure of human serum transferrin. The structures of seven cyanogen bromide fragments and the assembly of the complete structure. J Biol Chem. 1983 Mar 25;258(6):3543-53. [PubMed ]
8. de Arriba Zerpa GA, Saleh MC, Fernandez PM, Guillou F, Espinosa de los Monteros A, de Vellis J, Zakin MM, Baron B: Alternative splicing prevents transferrin secretion during differentiation of a human oligodendrocyte cell line. J Neurosci Res. 2000 Aug 15;61(4):388-95. [PubMed ]
9. Park I, Schaeffer E, Sidoli A, Baralle FE, Cohen GN, Zakin MM: Organization of the human transferrin gene: direct evidence that it originated by gene duplication. Proc Natl Acad Sci U S A. 1985 May;82(10):3149-53. [PubMed ]
10. Kovalyov LI, Shishkin SS, Efimochkin AS, Kovalyova MA, Ershova ES, Egorov TA, Musalyamov AK: The major protein expression profile and two-dimensional protein database of human heart. Electrophoresis. 1995 Jul;16(7):1160-9. [PubMed ]
11. Uzan G, Frain M, Park I, Besmond C, Maessen G, Trepat JS, Zakin MM, Kahn A: Molecular cloning and sequence analysis of cDNA for human transferrin. Biochem Biophys Res Commun. 1984 Feb 29;119(1):273-81. [PubMed ]
12. Namekata K, Oyama F, Imagawa M, Ihara Y: Human transferrin (Tf): a single mutation at codon 570 determines Tf C1 or Tf C2 variant. Hum Genet. 1997 Sep;100(3-4):457-8. [PubMed ]
13. Duguid JR, Bohmont CW, Liu NG, Tourtellotte WW: Changes in brain gene expression shared by scrapie and Alzheimer disease. Proc Natl Acad Sci U S A. 1989 Sep;86(18):7260-4. [PubMed ]
14. MacGillivray RT, Mendez E, Sinha SK, Sutton MR, Lineback-Zins J, Brew K: The complete amino acid sequence of human serum transferrin. Proc Natl Acad Sci U S A. 1982 Apr;79(8):2504-8. [PubMed ]
15. Woodworth RC, Mason AB, Funk WD, MacGillivray RT: Expression and initial characterization of five site-directed mutants of the N-terminal half-molecule of human transferrin. Biochemistry. 1991 Nov 12;30(45):10824-9. [PubMed ]
16. MacGillivray RT, Moore SA, Chen J, Anderson BF, Baker H, Luo Y, Bewley M, Smith CA, Murphy ME, Wang Y, Mason AB, Woodworth RC, Brayer GD, Baker EN: Two high-resolution crystal structures of the recombinant N-lobe of human transferrin reveal a structural change implicated in iron release. Biochemistry. 1998 Jun 2;37(22):7919-28. [PubMed ]
17. Jeffrey PD, Bewley MC, MacGillivray RT, Mason AB, Woodworth RC, Baker EN: Ligand-induced conformational change in transferrins: crystal structure of the open form of the N-terminal half-molecule of human transferrin. Biochemistry. 1998 Oct 6;37(40):13978-86. [PubMed ]
18. Bewley MC, Tam BM, Grewal J, He S, Shewry S, Murphy ME, Mason AB, Woodworth RC, Baker EN, MacGillivray RT: X-ray crystallography and mass spectroscopy reveal that the N-lobe of human transferrin expressed in Pichia pastoris is folded correctly but is glycosylated on serine-32. Biochemistry. 1999 Feb 23;38(8):2535-41. [PubMed ]
19. Evans P, Kemp J: Exon/intron structure of the human transferrin receptor gene. Gene. 1997 Oct 15;199(1-2):123-31. [PubMed ]
20. Pang H, Koda Y, Soejima M, Kimura H: Identification of a mutation (A1879G) of transferrin from cDNA prepared from peripheral blood cells. Ann Hum Genet. 1998 May;62(Pt 3):271-4. [PubMed ]
21. Lee PL, Halloran C, Trevino R, Felitti V, Beutler E: Human transferrin G277S mutation: a risk factor for iron deficiency anaemia. Br J Haematol. 2001 Nov;115(2):329-33. [PubMed ]
22. Douabin-Gicquel V, Soriano N, Ferran H, Wojcik F, Palierne E, Tamim S, Jovelin T, McKie AT, Le Gall JY, David V, Mosser J: Identification of 96 single nucleotide polymorphisms in eight genes involved in iron metabolism: efficiency of bioinformatic extraction compared with a systematic sequencing approach. Hum Genet. 2001 Oct;109(4):393-401. [PubMed ]

1. CFTR
2. cAMP- dependent chloride channel
3. ATP-binding cassette transporter sub- family C member 7

MQRSPLEKASVVSKLFFSWTRPILRKGYRQRLELSDIYQIPSVDSADNLSEKLEREWDRE
LASKKNPKLINALRRCFFWRFMFYGIFLYLGEVTKAVQPLLLGRIIASYDPDNKEERSIA
IYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYKKTLKLSSRVLDKISIGQL
VSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLIWELLQASAFCGLGFLIVLALFQAGL
GRMMMKYRDQRAGKISERLVITSEMIENIQSVKAYCWEEAMEKMIENLRQTELKLTRKAA
YVRYFNSSAFFFSGFFVVFLSVLPYALIKGIILRKIFTTISFCIVLRMAVTRQFPWAVQT
WYDSLGAINKIQDFLQKQEYKTLEYNLTTTEVVMENVTAFWEEGFGELFEKAKQNNNNRK
TSNGDDSLFFSNFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEG
KIKHSGRISFCSQFSWIMPGTIKENIIFGVSYDEYRYRSVIKACQLEEDISKFAEKDNIV
LGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTR
ILVTSKMEHLKKADKILILHEGSSYFYGTFSELQNLQPDFSSKLMGCDSFDQFSAERRNS
ILTETLHRFSLEGDAPVSWTETKKQSFKQTGEFGEKRKNSILNPINSIRKFSIVQKTPLQ
MNGIEEDSDEPLERRLSLVPDSEQGEAILPRISVISTGPTLQARRRQSVLNLMTHSVNQG
QNIHRKTTASTRKVSLAPQANLTELDIYSRRLSQETGLEISEEINEEDLKECFFDDMESI
PAVTTWNTYLRYITVHKSLIFVLIWCLVIFLAEVAASLVVLWLLGNTPLQDKGNSTHSRN
NSYAVIITSTSSYYVFYIYVGVADTLLAMGFFRGLPLVHTLITVSKILHHKMLHSVLQAP
MSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPYIFVATV
PVIVAFIMLRAYFLQTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHK
ALNLHTANWFLYLSTLRWFQMRIEMIFVIFFIAVTFISILTTGEGEGRVGIILTLAMNIM
STLQWAVNSSIDVDSLMRSVSRVFKFIDMPTEGKPTKSTKPYKNGQLSKVMIIENSHVKK
DDIWPSGGQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL
LNTEGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVAD
EVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVT
YQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSLFRQA
ISPSDRVKLFPHRNSSKCKSKPQIAALKEETEEEVQDTRL

• ABC_membrane (PF00664 )
• ABC_tran (PF00005 )

• None

• 81-103 118-138 195-215 221-241 308-328 331-350 860-880 912-932 991-1011 1014-1034 1103-1123 1129-1149

ATGCAGAGGTCGCCTCTGGAAAAGGCCAGCGTTGTCTCCAAACTTTTTTTCAGCTGGACC
AGACCAATTTTGAGGAAAGGATACAGACAGCGCCTGGAATTGTCAGACATATACCAAATC
CCTTCTGTTGATTCTGCTGACAATCTATCTGAAAAATTGGAAAGAGAATGGGATAGAGAG
CTGGCTTCAAAGAAAAATCCTAAACTCATTAATGCCCTTCGGCGATGTTTTTTCTGGAGA
TTTATGTTCTATGGAATCTTTTTATATTTAGGGGAAGTCACCAAAGCAGTACAGCCTCTC
TTACTGGGAAGAATCATAGCTTCCTATGACCCGGATAACAAGGAGGAACGCTCTATCGCG
ATTTATCTAGGCATAGGCTTATGCCTTCTCTTTATTGTGAGGACACTGCTCCTACACCCA
GCCATTTTTGGCCTTCATCACATTGGAATGCAGATGAGAATAGCTATGTTTAGTTTGATT
TATAAGAAGACTTTAAAGCTGTCAAGCCGTGTTCTAGATAAAATAAGTATTGGACAACTT
GTTAGTCTCCTTTCCAACAACCTGAACAAATTTGATGAAGGACTTGCATTGGCACATTTC
GTGTGGATCGCTCCTTTGCAAGTGGCACTCCTCATGGGGCTAATCTGGGAGTTGTTACAG
GCGTCTGCCTTCTGTGGACTTGGTTTCCTGATAGTCCTTGCCCTTTTTCAGGCTGGGCTA
GGGAGAATGATGATGAAGTACAGAGATCAGAGAGCTGGGAAGATCAGTGAAAGACTTGTG
ATTACCTCAGAAATGATTGAAAATATCCAATCTGTTAAGGCATACTGCTGGGAAGAAGCA
ATGGAAAAAATGATTGAAAACTTAAGACAAACAGAACTGAAACTGACTCGGAAGGCAGCC
TATGTGAGATACTTCAATAGCTCAGCCTTCTTCTTCTCAGGGTTCTTTGTGGTGTTTTTA
TCTGTGCTTCCCTATGCACTAATCAAAGGAATCATCCTCCGGAAAATATTCACCACCATC
TCATTCTGCATTGTTCTGCGCATGGCGGTCACTCGGCAATTTCCCTGGGCTGTACAAACA
TGGTATGACTCTCTTGGAGCAATAAACAAAATACAGGATTTCTTACAAAAGCAAGAATAT
AAGACATTGGAATATAACTTAACGACTACAGAAGTAGTGATGGAGAATGTAACAGCCTTC
TGGGAGGAGGGATTTGGGGAATTATTTGAGAAAGCAAAACAAAACAATAACAATAGAAAA
ACTTCTAATGGTGATGACAGCCTCTTCTTCAGTAATTTCTCACTTCTTGGTACTCCTGTC
CTGAAAGATATTAATTTCAAGATAGAAAGAGGACAGTTGTTGGCGGTTGCTGGATCCACT
GGAGCAGGCAAGACTTCACTTCTAATGATGATTATGGGAGAACTGGAGCCTTCAGAGGGT
AAAATTAAGCACAGTGGAAGAATTTCATTCTGTTCTCAGTTTTCCTGGATTATGCCTGGC
ACCATTAAAGAAAATATCATCTTTGGTGTTTCCTATGATGAATATAGATACAGAAGCGTC
ATCAAAGCATGCCAACTAGAAGAGGACATCTCCAAGTTTGCAGAGAAAGACAATATAGTT
CTTGGAGAAGGTGGAATCACACTGAGTGGAGGTCAACGAGCAAGAATTTCTTTAGCAAGA
GCAGTATACAAAGATGCTGATTTGTATTTATTAGACTCTCCTTTTGGATACCTAGATGTT
TTAACAGAAAAAGAAATATTTGAAAGCTGTGTCTGTAAACTGATGGCTAACAAAACTAGG
ATTTTGGTCACTTCTAAAATGGAACATTTAAAGAAAGCTGACAAAATATTAATTTTGAAT
GAAGGTAGCAGCTATTTTTATGGGACATTTTCAGAACTCCAAAATCTACAGCCAGACTTT
AGCTCAAAACTCATGGGATGTGATTCTTTCGACCAATTTAGTGCAGAAAGAAGAAATTCA
ATCCTAACTGAGACCTTACACCGTTTCTCATTAGAAGGAGATGCTCCTGTCTCCTGGACA
GAAACAAAAAAACAATCTTTTAAACAGACTGGAGAGTTTGGGGAAAAAAGGAAGAATTCT
ATTCTCAATCCAATCAACTCTATACGAAAATTTTCCATTGTGCAAAAGACTCCCTTACAA
ATGAATGGCATCGAAGAGGATTCTGATGAGCCTTTAGAGAGAAGGCTGTCCTTAGTACCA
GATTCTGAGCAGGGAGAGGCGATACTGCCTCGCATCAGCGTGATCAGCACTGGCCCCACG
CTTCAGGCACGAAGGAGGCAGTCTGTCCTGAACCTGATGACACACTCAGTTAACCAAGGT
CAGAACATTCACCGAAAGACAACAGCATCCACACGAAAAGTGTCACTGGCCCCTCAGGCA
AACTTGACTGAACTGGATATATATTCAAGAAGGTTATCTCAAGAAACTGGCTTGGAAATA
AGTGAAGAAATTAACGAAGAAGACTTAAAGGAGTGCCTTTTTGATGATATGGAGAGCATA
CCAGCAGTGACTACATGGAACACATACCTTCGATATATTACTGTCCACAAGAGCTTAATT
TTTGTGCTAATTTGGTGCTTAGTAATTTTTCTGGCAGAGGTGGCTGCTTCTTTGGTTGTG
CTGTGGCTCCTTGGAAACACTCCTCTTCAAGACAAAGGGAATAGTACTCATAGTAGAAAT
AACAGCTATGCAGTGATTATCACCAGCACCAGTTCGTATTATGTGTTTTACATTTACGTG
GGAGTAGCCGACACTTTGCTTGCTATGGGATTCTTCAGAGGTCTACCACTGGTGCATACT
CTAATCACAGTGTCGAAAATTTTACACCACAAAATGTTACATTCTGTTCTTCAAGCACCT
ATGTCAACCCTCAACACGTTGAAAGCAGGTGGGATTCTTAATAGATTCTCCAAAGATATA
GCAATTTTGGATGACCTTCTGCCTCTTACCATATTTGACTTCATCCAGTTGTTATTAATT
GTGATTGGAGCTATAGCAGTTGTCGCAGTTTTACAACCCTACATCTTTGTTGCAACAGTG
CCAGTGATAGTGGCTTTTATTATGTTGAGAGCATATTTCCTCCAAACCTCACAGCAACTC
AAACAACTGGAATCTGAAGGCAGGAGTCCAATTTTCACTCATCTTGTTACAAGCTTAAAA
GGACTATGGACACTTCGTGCCTTCGGACGGCAGCCTTACTTTGAAACTCTGTTCCACAAA
GCTCTGAATTTACATACTGCCAACTGGTTCTTGTACCTGTCAACACTGCGCTGGTTCCAA
ATGAGAATAGAAATGATTTTTGTCATCTTCTTCATTGCTGTTACCTTCATTTCCATTTTA
ACAACAGGAGAAGGAGAAGGAAGAGTTGGTATTATCCTGACTTTAGCCATGAATATCATG
AGTACATTGCAGTGGGCTGTAAACTCCAGCATAGATGTGGATAGCTTGATGCGATCTGTG
AGCCGAGTCTTTAAGTTCATTGACATGCCAACAGAAGGTAAACCTACCAAGTCAACCAAA
CCATACAAGAATGGCCAACTCTCGAAAGTTATGATTATTGAGAATTCACACGTGAAGAAA
GATGACATCTGGCCCTCAGGGGGCCAAATGACTGTCAAAGATCTCACAGCAAAATACACA
GAAGGTGGAAATGCCATATTAGAGAACATTTCCTTCTCAATAAGTCCTGGCCAGAGGGTG
GGCCTCTTGGGAAGAACTGGATCAGGGAAGAGTACTTTGTTATCAGCTTTTTTGAGACTA
CTGAACACTGAAGGAGAAATCCAGATCGATGGTGTGTCTTGGGATTCAATAACTTTGCAA
CAGTGGAGGAAAGCCTTTGGAGTGATACCACAGAAAGTATTTATTTTTTCTGGAACATTT
AGAAAAAACTTGGATCCCTATGAACAGTGGAGTGATCAAGAAATATGGAAAGTTGCAGAT
GAGGTTGGGCTCAGATCTGTGATAGAACAGTTTCCTGGGAAGCTTGACTTTGTCCTTGTG
GATGGGGGCTGTGTCCTAAGCCATGGCCACAAGCAGTTGATGTGCTTGGCTAGATCTGTT
CTCAGTAAGGCGAAGATCTTGCTGCTTGATGAACCCAGTGCTCATTTGGATCCAGTAACA
TACCAAATAATTAGAAGAACTCTAAAACAAGCATTTGCTGATTGCACAGTAATTCTCTGT
GAACACAGGATAGAAGCAATGCTGGAATGCCAACAATTTTTGGTCATAGAAGAGAACAAA
GTGCGGCAGTACGATTCCATCCAGAAACTGCTGAACGAGAGGAGCCTCTTCCGGCAAGCC
ATCAGCCCCTCCGACAGGGTGAAGCTCTTTCCCCACCGGAACTCAAGCAAGTGCAAGTCT
AAGCCCCAGATTGCTGCTCTGAAAGAGGAGACAGAAGAAGAGGTGCAAGATACAAGGCTT
TAG

1. Riordan JR, Rommens JM, Kerem B, Alon N, Rozmahel R, Grzelczak Z, Zielenski J, Lok S, Plavsic N, Chou JL, et al.: Identification of the cystic fibrosis gene: cloning and characterization of complementary DNA. Science. 1989 Sep 8;245(4922):1066-73. [PubMed ]
2. Zielenski J, Rozmahel R, Bozon D, Kerem B, Grzelczak Z, Riordan JR, Rommens J, Tsui LC: Genomic DNA sequence of the cystic fibrosis transmembrane conductance regulator (CFTR) gene. Genomics. 1991 May;10(1):214-28. [PubMed ]
3. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed ]
4. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed ]
5. Picciotto MR, Cohn JA, Bertuzzi G, Greengard P, Nairn AC: Phosphorylation of the cystic fibrosis transmembrane conductance regulator. J Biol Chem. 1992 Jun 25;267(18):12742-52. [PubMed ]
6. Neville DC, Rozanas CR, Price EM, Gruis DB, Verkman AS, Townsend RR: Evidence for phosphorylation of serine 753 in CFTR using a novel metal-ion affinity resin and matrix-assisted laser desorption mass spectrometry. Protein Sci. 1997 Nov;6(11):2436-45. [PubMed ]
7. Cheng J, Moyer BD, Milewski M, Loffing J, Ikeda M, Mickle JE, Cutting GR, Li M, Stanton BA, Guggino WB: A Golgi-associated PDZ domain protein modulates cystic fibrosis transmembrane regulator plasma membrane expression. J Biol Chem. 2002 Feb 1;277(5):3520-9. Epub 2001 Nov 13. [PubMed ]
8. McIntosh I, Cutting GR: Cystic fibrosis transmembrane conductance regulator and the etiology and pathogenesis of cystic fibrosis. FASEB J. 1992 Jul;6(10):2775-82. [PubMed ]
9. Hoedemaeker FJ, Davidson AR, Rose DR: A model for the nucleotide-binding domains of ABC transporters based on the large domain of aspartate aminotransferase. Proteins. 1998 Feb 15;30(3):275-86. [PubMed ]
10. Karthikeyan S, Leung T, Ladias JA: Structural basis of the Na+/H+ exchanger regulatory factor PDZ1 interaction with the carboxyl-terminal region of the cystic fibrosis transmembrane conductance regulator. J Biol Chem. 2001 Jun 8;276(23):19683-6. Epub 2001 Apr 13. [PubMed ]
11. Tsui LC: Mutations and sequence variations detected in the cystic fibrosis transmembrane conductance regulator (CFTR) gene: a report from the Cystic Fibrosis Genetic Analysis Consortium. Hum Mutat. 1992;1(3):197-203. [PubMed ]
12. Cutting GR, Kasch LM, Rosenstein BJ, Zielenski J, Tsui LC, Antonarakis SE, Kazazian HH Jr: A cluster of cystic fibrosis mutations in the first nucleotide-binding fold of the cystic fibrosis conductance regulator protein. Nature. 1990 Jul 26;346(6282):366-9. [PubMed ]
13. Kerem BS, Zielenski J, Markiewicz D, Bozon D, Gazit E, Yahav J, Kennedy D, Riordan JR, Collins FS, Rommens JM, et al.: Identification of mutations in regions corresponding to the two putative nucleotide (ATP)-binding folds of the cystic fibrosis gene. Proc Natl Acad Sci U S A. 1990 Nov;87(21):8447-51. [PubMed ]
14. White MB, Krueger LJ, Holsclaw DS Jr, Gerrard BC, Stewart C, Quittell L, Dolganov G, Baranov V, Ivaschenko T, Kapronov NI, et al.: Detection of three rare frameshift mutations in the cystic fibrosis gene in an African-American (CF444delA), an Italian (CF2522insC), and a Soviet (CF3821delT). Genomics. 1991 May;10(1):266-9. [PubMed ]
15. Jones CT, McIntosh I, Keston M, Ferguson A, Brock DJ: Three novel mutations in the cystic fibrosis gene detected by chemical cleavage: analysis of variant splicing and a nonsense mutation. Hum Mol Genet. 1992 Apr;1(1):11-7. [PubMed ]
16. Cheadle JP, Meredith AL, al-Jader LN: A new missense mutation (R1283M) in exon 20 of the cystic fibrosis transmembrane conductance regulator gene. Hum Mol Genet. 1992 May;1(2):123-5. [PubMed ]
17. Lissens W, Bonduelle M, Malfroot A, Dab I, Liebaers I: A serine to proline substitution (S1255P) in the second nucleotide binding fold of the cystic fibrosis gene. Hum Mol Genet. 1992 Sep;1(6):441-2. [PubMed ]
18. Shackleton S, Beards F, Harris A: Detection of novel and rare mutations in exon 4 of the cystic fibrosis gene by SSCP. Hum Mol Genet. 1992 Sep;1(6):439-40. [PubMed ]
19. Zielenski J, Fujiwara TM, Markiewicz D, Paradis AJ, Anacleto AI, Richards B, Schwartz RH, Klinger KW, Tsui LC, Morgan K: Identification of the M1101K mutation in the cystic fibrosis transmembrane conductance regulator (CFTR) gene and complete detection of cystic fibrosis mutations in the Hutterite population. Am J Hum Genet. 1993 Mar;52(3):609-15. [PubMed ]
20. Mercier B, Lissens W, Novelli G, Kalaydjieva L, De Arce M, Kapranov N, Klain NC, Lenoir G, Chauveau P, Lenaerts C, et al.: Identification of eight novel mutations in a collaborative analysis of a part of the second transmembrane domain of the CFTR gene. Genomics. 1993 Apr;16(1):296-7. [PubMed ]
21. Nunes V, Chillon M, Dork T, Tummler B, Casals T, Estivill X: A new missense mutation (E92K) in the first transmembrane domain of the CFTR gene causes a benign cystic fibrosis phenotype. Hum Mol Genet. 1993 Jan;2(1):79-80. [PubMed ]
22. Chillon M, Casals T, Nunes V, Gimenez J, Perez Ruiz E, Estivill X: Identification of a new missense mutation (P205S) in the first transmembrane domain of the CFTR gene associated with a mild cystic fibrosis phenotype. Hum Mol Genet. 1993 Oct;2(10):1741-2. [PubMed ]
23. Gasparini P, Marigo C, Bisceglia G, Nicolis E, Zelante L, Bombieri C, Borgo G, Pignatti PF, Cabrini G: Screening of 62 mutations in a cohort of cystic fibrosis patients from north eastern Italy: their incidence and clinical features of defined genotypes. Hum Mutat. 1993;2(5):389-94. [PubMed ]
24. Ghanem N, Costes B, Girodon E, Martin J, Fanen P, Goossens M: Identification of eight mutations and three sequence variations in the cystic fibrosis transmembrane conductance regulator (CFTR) gene. Genomics. 1994 May 15;21(2):434-6. [PubMed ]
25. Boteva K, Papageorgiou E, Georgiou C, Angastiniotis M, Middleton LT, Constantinou-Deltas CD: Novel cystic fibrosis mutation associated with mild disease in Cypriot patients. Hum Genet. 1994 May;93(5):529-32. [PubMed ]
26. Dork T, Mekus F, Schmidt K, Bosshammer J, Fislage R, Heuer T, Dziadek V, Neumann T, Kalin N, Wulbrand U, et al.: Detection of more than 50 different CFTR mutations in a large group of German cystic fibrosis patients. Hum Genet. 1994 Nov;94(5):533-42. [PubMed ]
27. Greil I, Wagner K, Rosenkranz W: A new missense mutation G1249E in exon 20 of the cystic fibrosis transmembrane conductance regulator (CFTR) gene. Hum Hered. 1994 Jul-Aug;44(4):238-40. [PubMed ]
28. Petreska L, Koceva S, Gordova-Muratovska A, Nestorov R, Efremov GD: Identification of two new mutations (711 +3A-->G and V1397E) in CF chromosomes of Albanian and Macedonian origin. Hum Mol Genet. 1994 Jun;3(6):999-1000. [PubMed ]
29. Schaedel C, Kristoffersson AC, Kornfalt R, Holmberg L: A novel cystic fibrosis mutation, Y109C, in the first transmembrane domain of CFTR. Hum Mol Genet. 1994 Jun;3(6):1001-2. [PubMed ]
30. Chillon M, Casals T, Gimenez J, Nunes V, Estivill X: Analysis of the CFTR gene in the Spanish population: SSCP-screening for 60 known mutations and identification of four new mutations (Q30X, A120T, 1812-1 G-->A, and 3667del4). Hum Mutat. 1994;3(3):223-30. [PubMed ]
31. Bienvenu T, Petitpretz P, Beldjord C, Kaplan JC: A missense mutation (F87L) in exon 3 of the cystic fibrosis transmembrane conductance regulator gene. Hum Mutat. 1994;3(4):395-6. [PubMed ]
32. Mercier B, Verlingue C, Lissens W, Silber SJ, Novelli G, Bonduelle M, Audrezet MP, Ferec C: Is congenital bilateral absence of vas deferens a primary form of cystic fibrosis? Analyses of the CFTR gene in 67 patients. Am J Hum Genet. 1995 Jan;56(1):272-7. [PubMed ]
33. Jezequel P, Dorval I, Fergelot P, Chauvel B, Le Treut A, Le Gall JY, Le Lannou D, Blayau M: Structural analysis of CFTR gene in congenital bilateral absence of vas deferens. Clin Chem. 1995 Jun;41(6 Pt 1):833-5. [PubMed ]
34. Brancolini V, Cremonesi L, Belloni E, Pappalardo E, Bordoni R, Seia M, Russo S, Padoan R, Giunta A, Ferrari M: Search for mutations in pancreatic sufficient cystic fibrosis Italian patients: detection of 90% of molecular defects and identification of three novel mutations. Hum Genet. 1995 Sep;96(3):312-8. [PubMed ]
35. Desgeorges M, Rodier M, Piot M, Demaille J, Claustres M: Four adult patients with the missense mutation L206W and a mild cystic fibrosis phenotype. Hum Genet. 1995 Dec;96(6):717-20. [PubMed ]
36. Zielenski J, Markiewicz D, Chen HS, Schappert K, Seller A, Durie P, Corey M, Tsui LC: Identification of six mutations (R31L, 441delA, 681delC, 1461ins4, W1089R, E1104X) in the cystic fibrosis transmembrane conductance regulator (CFTR) gene. Hum Mutat. 1995;5(1):43-7. [PubMed ]
37. Verlingue C, Kapranov NI, Mercier B, Ginter EK, Petrova NV, Audrezet MP, Ferec C: Complete screening of mutations in the coding sequence of the CFTR gene in a sample of CF patients from Russia: identification of three novel alleles. Hum Mutat. 1995;5(3):205-9. [PubMed ]
38. Romey MC, Desgeorges M, Ray P, Godard P, Demaille J, Claustres M: Novel missense mutation in the first transmembrane segment of the CFTR gene (Q98R) identified in a male adult. Hum Mutat. 1995;6(2):190-1. [PubMed ]
39. Leoni GB, Pitzalis S, Podda R, Zanda M, Silvetti M, Caocci L, Cao A, Rosatelli MC: A specific cystic fibrosis mutation (T3381) associated with the phenotype of isolated hypotonic dehydration. J Pediatr. 1995 Aug;127(2):281-3. [PubMed ]
40. Ferec C, Novelli G, Verlingue C, Quere I, Dallapiccola B, Audrezet MP, Mercier B: Identification of six novel CFTR mutations in a sample of Italian cystic fibrosis patients. Mol Cell Probes. 1995 Apr;9(2):135-7. [PubMed ]
41. Messaoud T, Verlingue C, Denamur E, Pascaud O, Quere I, Fattoum S, Elion J, Ferec C: Distribution of CFTR mutations in cystic fibrosis patients of Tunisian origin: identification of two novel mutations. Eur J Hum Genet. 1996;4(1):20-4. [PubMed ]
42. Nasr SZ, Strong TV, Mansoura MK, Dawson DC, Collins FS: Novel missense mutation (G314R) in a cystic fibrosis patient with hepatic failure. Hum Mutat. 1996;7(2):151-4. [PubMed ]
43. Petreska L, Plaseska D, Koceva S, Stavljenic-Rukavina A, Efremov GD: A novel mutation in exon 12 (Y569C) of the CFTR gene identified in a patient of Croatian origin. Hum Mutat. 1996;7(4):374-5. [PubMed ]
44. Bienvenu T, Chertkoff L, Beldjord C, Segal E, Carniglia L, Barreiro C, Kaplan JC: Identification of three novel mutations in the cystic fibrosis transmembrane conductance regulator gene in Argentinian CF patients. Hum Mutat. 1996;7(4):376-7. [PubMed ]
45. Hughes DJ, Hill AJ, Macek M Jr, Redmond AO, Nevin NC, Graham CA: Mutation characterization of CFTR gene in 206 Northern Irish CF families: thirty mutations, including two novel, account for approximately 94% of CF chromosomes. Hum Mutat. 1996;8(4):340-7. [PubMed ]
46. Zielenski J, Patrizio P, Markiewicz D, Asch RH, Tsui LC: Identification of two mutations (S50Y and 4173delC) in the CFTR gene from patients with congenital bilateral absence of vas deferens (CBAVD). Hum Mutat. 1997;9(2):183-4. [PubMed ]
47. Clavel C, Pennaforte F, Pigeon F, Verlingue C, Birembaut P, Ferec C: Identification of four novel mutations in the cystic fibrosis transmembrane conductance regulator gene: E664X, 2113delA, 306delTAGA, and delta M1140. Hum Mutat. 1997;9(4):368-9. [PubMed ]
48. Gouya L, Pascaud O, Munck A, Elion J, Denamur E: Novel mutation (A141D) in exon 4 of the CFTR gene identified in an Algerian patient. Hum Mutat. 1997;10(1):86-7. [PubMed ]
49. Casals T, Pacheco P, Barreto C, Gimenez J, Ramos MD, Pereira S, Pinheiro JA, Cobos N, Curvelo A, Vazquez C, Rocha H, Seculi JL, Perez E, Dapena J, Carrilho E, Duarte A, Palacio AM, Nunes V, Lavinha J, Estivill X: Missense mutation R1066C in the second transmembrane domain of CFTR causes a severe cystic fibrosis phenotype: study of 19 heterozygous and 2 homozygous patients. Hum Mutat. 1997;10(5):387-92. [PubMed ]
50. Shrimpton AE, Borowitz D, Swender P: Cystic fibrosis mutation frequencies in upstate New York. Hum Mutat. 1997;10(6):436-42. [PubMed ]
51. Friedman KJ, Leigh MW, Czarnecki P, Feldman GL: Cystic fibrosis transmembrane-conductance regulator mutations among African Americans. Am J Hum Genet. 1998 Jan;62(1):195-6. [PubMed ]
52. Onay T, Topaloglu O, Zielenski J, Gokgoz N, Kayserili H, Camcioglu Y, Cokugras H, Akcakaya N, Apak M, Tsui LC, Kirdar B: Analysis of the CFTR gene in Turkish cystic fibrosis patients: identification of three novel mutations (3172delAC, P1013L and M1028I). Hum Genet. 1998 Feb;102(2):224-30. [PubMed ]
53. Bombieri C, Benetazzo M, Saccomani A, Belpinati F, Gile LS, Luisetti M, Pignatti PF: Complete mutational screening of the CFTR gene in 120 patients with pulmonary disease. Hum Genet. 1998 Dec;103(6):718-22. [PubMed ]
54. Vankeerberghen A, Wei L, Jaspers M, Cassiman JJ, Nilius B, Cuppens H: Characterization of 19 disease-associated missense mutations in the regulatory domain of the cystic fibrosis transmembrane conductance regulator. Hum Mol Genet. 1998 Oct;7(11):1761-9. [PubMed ]
55. Malone G, Haworth A, Schwarz MJ, Cuppens H, Super M: Detection of five novel mutations of the cystic fibrosis transmembrane regulator (CFTR) gene in Pakistani patients with cystic fibrosis: Y569D, Q98X, 296+12(T>C), 1161delC and 621+2(T>C). Hum Mutat. 1998;11(2):152-7. [PubMed ]
56. Leoni GB, Pitzalis S, Tonelli R, Cao A: Identification of a novel mutation (S13F) in the CFTR gene in a CF patient of Sardinian origin. Hum Mutat. 1998;11(4):337. [PubMed ]
57. Feldmann D, Sardet A, Cougoureux E, Plouvier E, Fontaine JL, Tournier G, Aymard P: Identification of three novel mutations in the CFTR gene, R117P, deltaD192, and 3121-1G-->A in four French patients. Hum Mutat. 1998;Suppl 1:S78-80. [PubMed ]
58. Casals T, Ramos MD, Gimenez J, Nadal M, Nunes V, Estivill X: Paternal origin of a de novo novel CFTR mutation (L1065R) causing cystic fibrosis. Hum Mutat. 1998;Suppl 1:S99-102. [PubMed ]
59. Shackleton S, Harris A: A 2-amino acid insertion mutation (1243insACAAAA) in exon 7 of the CFTR gene. Hum Mutat. 1998;Suppl 1:S156-7. [PubMed ]
60. Picci L, Cameran M, Olante P, Zacchello F, Scarpa M: Identification of a D579G homozygote cystic fibrosis patient with pancreatic sufficiency and minor lung involvement. Mutations in brief no. 221. Online. Hum Mutat. 1999;13(2):173. [PubMed ]

1. Sodium bicarbonate cotransporter
2. Na(+/HCO3(-cotransporter
3. Solute carrier family 4 member 4
4. kNBC1

MEDEAVLDRGASFLKHVCDEEEVEGHHTIYIGVHVPKSYRRRRRHKRKTGHKEKKEKERI
SENYSDKSDIENADESSSSILKPLISPAAERIRFILGEEDDSPAPPQLFTELDELLAVDG
QEMEWKETARWIKFEEKVEQGGERWSKPHVATLSLHSLFELRTCMEKGSIMLDREASSLP
QLVEMIVDHQIETGLLKPELKDKVTYTLLRKHRHQTKKSNLRSLADIGKTVSSASRMFTN
PDNGSPAMTHRNLTSSSLNDISDKPEKDQLKNKFMKKLPRDAEASNVLVGEVDFLDTPFI
AFVRLQQAVMLGALTEVPVPTRFLFILLGPKGKAKSYHEIGRAIATLMSDEVFHDIAYKA
KDRHDLIAGIDEFLDEVIVLPPGEWDPAIRIEPPKSLPSSDKRKNMYSGGENVQMNGDTP
HDGGHGGGGHGDCEELQRTGRFCGGLIKDIKRKAPFFASDFYDALNIQALSAILFIYLAT
VTNAITFGGLLGDATDNMQGVLESFLGTAVSGAIFCLFAGQPLTILSSTGPVLVFERLLF
NFSKDNNFDYLEFRLWIGLWSAFLCLILVATDASFLVQYFTRFTEEGFSSLISFIFIYDA
FKKMIKLADYYPINSNFKVGYNTLFSCTCVPPDPANISISNDTTLAPEYLPTMSSTDMYH
NTTFDWAFLSKKECSKYGGNLVGNNCNFVPDITLMSFILFLGTYTSSMALKKFKTSPYFP
TTARKLISDFAIILSILIFCVIDALVGVDTPKLIVPSEFKPTSPNRGWFVPPFGENPWWV
CLAAAIPALLVTILIFMDQQITAVIVNRKEHKLKKGAGYHLDLFWVAILMVICSLMALPW
YVAATVISIAHIDSLKMETETSAPGEQPKFLGVREQRVTGTLVFILTGLSVFMAPILKFI
PMPVLYGVFLYMGVASLNGVQFMDRLKLLLMPLKHQPDFIYLRHVPLRRVHLFTFLQVLC
LALLWILKSTVAAIIFPVMILALVAVRKGMDYLFSQHDLSFLDDVIPEKDKKKKEDEKKK
KKKKGSLDSDNDDSDCPYSEKVPSIKIPMDIMEQQPFLSDSKPSDRERSPTFLERHTSC

• Band_3_cyto (PF07565 )
• HCO3_cotransp (PF00955 )

• 1-837

• 469-488 505-526 555-580 692-710 726-748 778-797 823-847 882-901 950-967 971-986

ATGTCCACTGAAAATGTGGAAGGGAAGCCCAGTAACCTTGGGGAGAGAGGAAGAGCCCGG
AGCTCCACTTTCCTCAGGGTTGTCCAGCCAATGTTTAACCACAGTATTTTCACTTCTGCA
GTCTCTCCTGCTGCAGAACGCATCCGATTCATCTTGGGAGAGGAGGATGACAGCCCAGCT
CCCCCTCAGCTCTTCACGGAACTGGATGAGCTGCTGGCCGTGGATGGGCAGGAGATGGAG
TGGAAGGAAACAGCCAGGTGGATCAAGTTTGAAGAAAAAGTGGAACAGGGTGGGGAAAGA
TGGAGCAAGCCCCATGTGGCCACATTGTCCCTTCATAGTTTATTTGAGCTGAGGACATGT
ATGGAGAAAGGATCCATCATGCTTGATCGGGAGGCTTCTTCTCTCCCACAGTTGGTGGAG
ATGATTGTTGACCATCAGATTGAGACAGGCCTATTGAAACCTGAACTTAAGGATAAGGTG
ACCTATACTTTGCTCCGGAAGCACCGGCATCAAACCAAGAAATCCAACCTTCGGTCCCTG
GCTGACATTGGGAAGACAGTCTCCAGTGCAAGTAGGATGTTTACCAACCCTGATAATGGT
AGCCCAGCCATGACCCATAGGAATCTGACTTCCTCCAGTCTGAATGACATTTCTGATAAA
CCGGAGAAGGACCAGCTGAAGAATAAGTTCATGAAAAAATTGCCACGTGATGCAGAAGCT
TCCAACGTGCTTGTTGGGGAGGTTGACTTTTTGGATACTCCTTTCATTGCCTTTGTTAGG
CTACAGCAGGCTGTCATGCTGGGTGCCCTGACTGAAGTTCCTGTGCCCACAAGGTTCTTG
TTCATTCTCTTAGGTCCTAAGGGGAAAGCCAAGTCCTACCACGAGATTGGCAGAGCCATT
GCCACCCTGATGTCTGATGAGGTGTTCCATGACATTGCTTATAAAGCAAAAGACAGGCAC
GACCTGATTGCTGGTATTGATGAGTTCCTAGATGAAGTCATCGTCCTTCCACCTGGGGAA
TGGGATCCAGCAATTAGGATAGAGCCTCCTAAGAGTCTTCCATCCTCTGACAAAAGAAAG
AATATGTACTCAGGTGGAGAGAATGTTCAGATGAATGGGGATACGCCCCATGATGGAGGT
CACGGAGGAGGAGGACATGGGGATTGTGAAGAATTGCAGCGAACTGGACGGTTCTGTGGT
GGACTAATTAAAGACATAAAGAGGAAAGCGCCATTTTTTGCCAGTGATTTTTATGATGCT
TTAAATATTCAAGCTCTTTCGGCAATTCTCTTCATTTATCTGGCAACTGTAACTAATGCT
ATCACTTTTGGAGGACTGCTTGGGGATGCCACTGACAACATGCAGGGCGTGTTGGAGAGT
TTCCTGGGCACTGCTGTCTCTGGAGCCATCTTTTGCCTTTTTGCTGGTCAACCACTCACT
ATTCTGAGCAGCACCGGACCTGTCCTAGTTTTTGAGAGGCTTCTATTTAATTTCAGCAAG
GACAATAATTTTGACTATTTGGAGTTTCGCCTTTGGATTGGCCTGTGGTCCGCCTTCCTA
TGTCTCATTTTGGTAGCCACTGATGCCAGCTTCTTGGTTCAATACTTCACACGTTTCACG
GAGGAGGGCTTTTCCTCTCTGATTAGCTTCATCTTTATCTATGATGCTTTCAAGAAGATG
ATCAAGCTTGCAGATTACTACCCCATCAACTCCAACTTCAAAGTGGGCTACAACACTCTC
TTTTCCTGTACCTGTGTGCCACCTGACCCAGCTAATATCTCAATATCTAATGACACCACA
CTGGCCCCAGAGTATTTGCCAACTATGTCTTCTACTGACATGTACCATAATACTACCTTT
GACTGGGCATTTTTGTCGAAGAAGGAGTGTTCAAAATACGGAGGAAACCTTGTCGGGAAC
AACTGTAATTTTGTTCCTGATATCACACTCATGTCTTTTATCCTCTTCTTGGGAACCTAC
ACCTCTTCCATGGCTCTGAAAAAATTCAAAACTAGTCCTTATTTTCCAACCACAGCAAGA
AAACTGATCAGTGATTTTGCCATTATCTTGTCCATTCTCATCTTTTGTGTAATAGATGCC
CTAGTAGGCGTGGACACCCCAAAACTAATTGTGCCAAGTGAGTTCAAGCCAACAAGTCCA
AACCGAGGTTGGTTCGTTCCACCGTTTGGAGAAAACCCCTGGTGGGTGTGCCTTGCTGCT
GCTATCCCGGCTTTGTTGGTCACTATACTGATTTTCATGGACCAACAAATTACAGCTGTG
ATTGTAAACAGGAAAGAACATAAACTCAAGAAAGGAGCAGGGTATCACTTGGATCTCTTT
TGGGTGGCCATCCTCATGGTTATATGCTCCCTCATGGCTCTTCCGTGGTATGTAGCTGCT
ACGGTCATCTCCATTGCTCACATCGACAGTTTGAAGATGGAGACAGAGACTTCTGCACCT
GGAGAACAACCAAAGTTTCTAGGAGTGAGGGAACAAAGAGTCACTGGAACCCTTGTGTTT
ATTCTGACTGGTCTGTCAGTCTTTATGGCTCCCATCTTGAAGTTTATACCCATGCCTGTA
CTCTATGGTGTGTTCCTGTATATGGGAGTAGCATCCCTTAATGGTGTGCAGTTCATGGAT
CGTCTGAAGCTGCTTCTGATGCCTCTGAAGCATCAGCCTGACTTCATCTACCTGCGTCAT
GTTCCTCTGCGCAGAGTCCACCTGTTCACTTTCCTGCAGGTGTTGTGTCTGGCCCTGCTT
TGGATCCTCAAGTCAACGGTGGCTGCTATCATTTTTCCAGTAATGATCTTGGCACTTGTA
GCTGTCAGAAAAGGCATGGACTACCTCTTCTCCCAGCATGACCTCAGCTTCCTGGATGAT
GTCATTCCAGAAAAGGACAAGAAAAAGAAGGAGGATGAGAAGAAAAAGAAAAAGAAGAAG
GGAAGTCTGGACAGTGACAATGATGATTCTGACTGCCCATACTCAGAAAAAGTTCCAAGT
ATTAAAATTCCAATGGACATCATGGAACAGCAACCTTTCCTAAGCGATAGCAAACCTTCT
GACAGAGAAAGATCACCAACATTCCTTGAACGCCACACATCATGCTGA

1. Burnham CE, Amlal H, Wang Z, Shull GE, Soleimani M: Cloning and functional expression of a human kidney Na+:HCO3- cotransporter. J Biol Chem. 1997 Aug 1;272(31):19111-4. [PubMed ]
2. Abuladze N, Lee I, Newman D, Hwang J, Boorer K, Pushkin A, Kurtz I: Molecular cloning, chromosomal localization, tissue distribution, and functional expression of the human pancreatic sodium bicarbonate cotransporter. J Biol Chem. 1998 Jul 10;273(28):17689-95. [PubMed ]
3. Choi I, Romero MF, Khandoudi N, Bril A, Boron WF: Cloning and characterization of a human electrogenic Na+-HCO-3 cotransporter isoform (hhNBC). Am J Physiol. 1999 Mar;276(3 Pt 1):C576-84. [PubMed ]
4. Sun XC, Bonanno JA: Identification and cloning of the Na/HCO(3-) cotransporter (NBC) in human corneal endothelium. Exp Eye Res. 2003 Sep;77(3):287-95. [PubMed ]
5. Park K, Hurley PT, Roussa E, Cooper GJ, Smith CP, Thevenod F, Steward MC, Case RM: Expression of a sodium bicarbonate cotransporter in human parotid salivary glands. Arch Oral Biol. 2002 Jan;47(1):1-9. [PubMed ]
6. Gross E, Pushkin A, Abuladze N, Fedotoff O, Kurtz I: Regulation of the sodium bicarbonate cotransporter kNBC1 function: role of Asp(986), Asp(988) and kNBC1-carbonic anhydrase II binding. J Physiol. 2002 Nov 1;544(Pt 3):679-85. [PubMed ]

1. Carbonic anhydrase IV
2. Carbonate dehydratase IV
3. CA-IV

MRMLLALLALSAARPSASAESHWCYEVQAESSNYPCLVPVKWGGNCQKDRQSPINIVTTK
AKVDKKLGRFFFSGYDKKQTWTVQNNGHSVMMLLENKASISGGGLPAPYQAKQLHLHWSD
LPYKGSEHSLDGEHFAMEMHIVHEKEKGTSRNVKEAQDPEDEIAVLAFLVEAGTQVNEGF
QPLVEALSNIPKPEMSTTMAESSLLDLLPKEEKLRHYFRYLGSLTTPTCDEKVVWTVFRE
PIQLHREQILAFSQKLYYDKEQTVSMKDNVRPLQQLGQRTVIKSGAPGRPLPWALPALLG
PMLACLLAGFLR

• Nitrogen Metabolism (map00910 )

• H2CO3 = CO2 + H2O

• Carb_anhydrase (PF00194 )

• 1-18

• 292-311

ATGCGGATGCTGCTGGCGCTCCTGGCCCTCTCCGCGGCGCGGCCATCGGCCAGTGCAGAG
TCACACTGGTGCTACGAGGTTCAAGCCGAGTCCTCCAACTACCCCTGCTTGGTGCCAGTC
AAGTGGGGTGGAAACTGCCAGAAGGACCGCCAGTCCCCCATCAACATCGTCACCACCAAG
GCAAAGGTGGACAAAAAACTGGGACGCTTCTTCTTCTCTGGCTACGATAAGAAGCAAACG
TGGACTGTCCAAAATAACGGGCACTCAGTGATGATGTTGCTGGAGAACAAGGCCAGCATT
TCTGGAGGAGGACTGCCTGCCCCATACCAGGCCAAACAGTTGCACCTGCACTGGTCCGAC
TTGCCATATAAGGGCTCGGAGCACAGCCTCGATGGGGAGCACTTTGCCATGGAGATGCAC
ATAGTACATGAGAAAGAGAAGGGGACATCGAGGAATGTGAAAGAGGCCCAGGACCCTGAA
GACGAAATTGCGGTGCTGGCCTTTCTGGTGGAGGCTGGAACCCAGGTGAACGAGGGCTTC
CAGCCACTGGTGGAGGCACTGTCTAATATCCCCAAACCTGAGATGAGCACTACGATGGCA
GAGAGCAGCCTGTTGGACCTGCTCCCCAAGGAGGAGAAACTGAGGCACTACTTCCGCTAC
CTGGGCTCACTCACCACACCGACCTGCGATGAGAAGGTCGTCTGGACTGTGTTCCGGGAG
CCCATTCAGCTTCACAGAGAACAGATCCTGGCATTCTCTCAGAAGCTGTACTACGACAAG
GAACAGACAGTGAGCATGAAGGACAATGTCAGGCCCCTGCAGCAGCTGGGGCAGCGCACG
GTGATAAAGTCCGGGGCCCCGGGTCGGCCGCTGCCCTGGGCCCTGCCTGCCCTGCTGGGC
CCCATGCTGGCCTGCCTGCTGGCCGGCTTCCTGCGATGA

1. Okuyama T, Sato S, Zhu XL, Waheed A, Sly WS: Human carbonic anhydrase IV: cDNA cloning, sequence comparison, and expression in COS cell membranes. Proc Natl Acad Sci U S A. 1992 Feb 15;89(4):1315-9. [PubMed ]
2. Okuyama T, Batanian JR, Sly WS: Genomic organization and localization of gene for human carbonic anhydrase IV to chromosome 17q. Genomics. 1993 Jun;16(3):678-84. [PubMed ]
3. Zhu XL, Sly WS: Carbonic anhydrase IV from human lung. Purification, characterization, and comparison with membrane carbonic anhydrase from human kidney. J Biol Chem. 1990 May 25;265(15):8795-801. [PubMed ]
4. Waheed A, Okuyama T, Heyduk T, Sly WS: Carbonic anhydrase IV: purification of a secretory form of the recombinant human enzyme and identification of the positions and importance of its disulfide bonds. Arch Biochem Biophys. 1996 Sep 15;333(2):432-8. [PubMed ]
5. Okuyama T, Waheed A, Kusumoto W, Zhu XL, Sly WS: Carbonic anhydrase IV: role of removal of C-terminal domain in glycosylphosphatidylinositol anchoring and realization of enzyme activity. Arch Biochem Biophys. 1995 Jul 10;320(2):315-22. [PubMed ]
6. Stams T, Nair SK, Okuyama T, Waheed A, Sly WS, Christianson DW: Crystal structure of the secretory form of membrane-associated human carbonic anhydrase IV at 2.8-A resolution. Proc Natl Acad Sci U S A. 1996 Nov 26;93(24):13589-94. [PubMed ]

1. Solute carrier family 4 member 10

MEIKDQGAQMEPLLPTRNDEEAVVDRGGTRSILKTHFEKEDLEGHRTLFIGVHVPLGGRK
SHRRHRHRGHKHRKRDRERDSGLEDGRESPSFDTPSQRVQFILGTEDDDEEHIPHDLFTE
LDEICWREGEDAEWRETARWLKFEEDVEDGGERWSKPYVATLSLHSLFELRSCILNGTVL
LDMHANTLEEIADMVLDQQVSSGQLNEDVRHRVHEALMKQHHHQNQKKLTNRIPIVRSFA
DIGKKQSEPNSMDKNAGQVVSPQSAPACVENKNDVSRENSTVDFSKGLGGQQKGHTSPCG
MKQRHEKGPPHQQEREVDLHFMKKIPPGAEASNILVGELEFLDRTVVAFVRLSPAVLLQG
LAEVPIPTRFLFILLGPLGKGQQYHEIGRSIATLMTDEVFHDVAYKAKDRNDLVSGIDEF
LDQVTVLPPGEWDPSIRIEPPKNVPSQEKRKIPAVPNGTAAHGEAEPHGGHSGPELQRTG
RIFGGLILDIKRKAPYFWSDFRDAFSLQCLASFLFLYCACMSPVITFGGLLGEATEGRIS
AIESLFGASMTGIAYSLFGGQPLTILGSTGPVLVFEKILFKFCKEYGLSYLSLRASIGLW
TATLCIILVATDASSLVCYITRFTEEAFASLICIIFIYEALEKLFELSEAYPINMHNDLE
LLTQYSCNCVEPHNPSNGTLKEWRESNISASDIIWENLTVSECKSLHGEYVGRACGHDHP
YVPDVLFWSVILFFSTVTLSATLKQFKTSRYFPTKVRSIVSDFAVFLTILCMVLIDYAIG
IPSPKLQVPSVFKPTRDDRGWFVTPLGPNPWWTVIAAIIPALLCTILIFMDQQITAVIIN
RKEHKLKKGCGYHLDLLMVAVMLGVCSIMGLPWFVAATVLSITHVNSLKLESECSAPGEQ
PKFLGIREQRVTGLMIFILMGSSVFMTSILKFIPMPVLYGVFLYMGASSLKGIQFFDRIK
LFWMPAKHQPDFIYLRHVPLRKVHLFTIIQMSCLGLLWIIKVSRAAIVFPMMVLALVFVR
KLMDLLFTKRELSWLDDLMPESKKKKLEDAEKEEEQSMLAMEDEGTVQLPLEGHYRDDPS
VINISDEMSKTALWRNLLITADNSKDKESSFPSKSSPS

• Band_3_cyto (PF07565 )
• HCO3_cotransp (PF00955 )

• 1-877

• 510-530 539-559 563-583 597-617 627-647 721-741 763-783 810-830 856-876 913-933 936-956 999-1019

ATGGAGATTAAAGACCAGGGAGCCCAAATGGAGCCGCTGCTGCCTACGAGAAATGATGAA
GAAGCAGTTGTGGATAGAGGTGGAACTCGTTCTATTCTCAAAACACACTTTGAGAAAGAA
GATTTAGAAGGTCATCGAACACTATTTATTGGAGTACATGTGCCCTTGGGAGGAAGAAAA
AGCCATCGACGTCACAGGCATCGTGGTCATAAACACAGAAAGAGAGACAGAGAAAGAGAT
TCAGGATTAGAGGATGGAAGGGAGTCACCTTCTTTTGACACCCCATCACAGAGGGTACAG
TTTATTCTTGGAACCGAGGATGATGACGAGGAACACATTCCTCATGACCTTTTCACAGAA
CTGGATGAGATTTGTTGGCGTGAAGGTGAGGACGCTGAGTGGCGAGAAACAGCCAGGTGG
TTGAAGTTTGAAGAAGATGTGGAAGATGGAGGAGAAAGGTGGAGCAAGCCTTATGTGGCT
ACTCTTTCATTGCACAGCTTGTTTGAATTGAGAAGTTGTATTCTGAATGGAACTGTGTTG
CTGGACATGCATGCCAACACTTTAGAAGAAATTGCAGATATGGTTCTTGACCAACAAGTG
AGCTCAGGTCAGCTGAATGAAGATGTACGCCATAGGGTCCATGAGGCATTGATGAAACAG
CATCATCATCAGAATCAGAAAAAACTCACCAACAGGATTCCCATTGTTCGTTCCTTTGCT
GATATTGGCAAGAAACAGTCAGAACCAAATTCCATGGACAAAAATGCAGGTCAGGTTGTT
TCTCCTCAGTCTGCTCCAGCCTGTGTTGAAAATAAAAATGATGTTAGCAGAGAAAACAGC
ACTGTTGACTTTAGCAAGGTTGATCTGCATTTTATGAAAAAGATTCCTCCAGGTGCTGAA
GCATCGAACATCTTACTGGGAGAACTGGAGTTCTTGGATCGAACAGTAGTTGCGTTTGTC
AGGTTGTCTCCAGCTGTATTGCTTCAAGGACTGGCTGAAGTCCCAATCCCAACCAGATTT
TTGTTCATTCTTCTGGGACCCCTGGGAAAGGGTCAACAGTACCATGAGATTGGCAGATCA
ATTGCAACCCTAATGACAGATGAGGTATTTCATGATGTTGCCTATAAAGCTAAAGATCGT
AATGACTTGGTATCAGGAATTGATGAGTTTCTGGATCAGGTTACTGTTCTCCCTCCTGGA
GAATGGGATCCAAGCATTCGAATAGAGCCTCCCAAAAATGTTCCTTCCCAGGAGAAGAGG
AAGATTCCTGCTGTACCAAATGGAACAGCAGCTCATGGGGAAGCAGAGCCCCACGGAGGA
CATAGTGGACCTGAACTCCAGCGAACTGGAAGGATTTTTGGGGGACTTATTTTAGATATC
AAAAGAAAAGCTCCATACTTCTGGAGTGACTTCAGAGATGCTTTCAGCCTGCAGTGCTTA
GCATCTTTTCTATTTCTCTACTGCGCGTGTATGTCTCCTGTCATCACGTTTGGAGGACTG
CTGGGAGAAGCAACTGAAGGGCGTATAAGTGCAATTGAATCTCTCTTTGGAGCATCCATG
ACCGGGATAGCCTATTCTCTCTTTGGTGGACAGCCTCTTACCATATTAGGCAGTACAGGA
CCAGTTTTGGTGTTTGAAAAGATTTTGTTTAAATTTTGCAAAGAATATGGGCTGTCATAC
CTATCTTTAAGAGCTAGCATTGGACTTTGGACTGCAACTCTATGTATCATACTTGTGGCC
ACAGATGCTAGTTCCCTTGTCTGCTACATCACTCGGTTTACTGAAGAAGCTTTTGCTTCC
CTGATTTGCATCATTTTCATTTATGAGGCCCTGGAGAAGTTGTTTGAACTCAGTGAAGCA
TATCCAATCAACATGCATAATGATCTGGAACTGCTGACACAATACTCGTGTAACTGTGTG
GAACCGCATAATCCCAGCAATGGCACATTGAAGGAATGGAGGGAATCCAATATTTCTGCC
TCTGACATAATTTGGGAGAACCTAACTGTGTCAGAATGCAAATCATTGCATGGAGAGTAT
GTTGGACGGGCCTGTGGCCATGATCACCCATATGTTCCAGATGTTCTATTTTGGTCTGTG
ATCCTGTTCTTTTCCACAGTTACTCTGTCAGCCACCCTGAAGCAGTTCAAGACTAGCAGA
TATTTTCCAACCAAGGTTCGATCCATAGTGAGTGACTTTGCTGTCTTTCTTACAATTCTG
TGTATGGTTTTAATTGACTATGCCATTGGGATCCCATCTCCAAAACTACAAGTACCAAGT
GTTTTCAAGCCCACTAGAGATGATCGTGGCTGGTTTGTTACGCCTTTAGGTCCAAACCCA
TGGTGGACAGTAATAGCTGCTATAATTCCAGCTCTGCTTTGTACTATTCTAATTTTCATG
GACCAACAGATTACAGCTGTCATCATCAACAGGAAAGAGCATAAGCTAAAGAAAGGTTGT
GGGTACCATCTGGACCTATTAATGGTGGCTGTCATGCTCGGTGTATGCTCCATCATGGGC
CTGCCATGGTTTGTGGCTGCCACAGTCCTCTCCATCACTCATGTCAATAGCCTAAAACTG
GAATCAGAATGCTCAGCTCCAGGAGAACAACCCAAATTTCTCGGCATTCGGGAGCAAAGG
GTTACTGGGCTTATGATTTTTATTCTTATGGGTTCATCAGTCTTTATGACCAGTATTCTG
AAGTTTATTCCCATGCCAGTGCTATATGGAGTGTTTCTTTATATGGGTGCTTCATCTCTA
AAGGGAATTCAGTTCTTTGATAGGATAAAGCTCTTCTGGATGCCGGCAAAACATCAACCA
GATTTTATATACCTAAGGCACGTACCGCTTCGAAAAGTGCATCTCTTCACAATTATTCAG
ATGAGTTGCCTTGGCCTTTTGTGGATAATAAAAGTTTCAAGAGCTGCTATTGTCTCTCCC
ATGATGGTGTTATCCCTGGTTTTTGTAAGAAAGTTGATGGACTTGTTGTTCACGAAACGG
GAACTCTGCTGGTTGGATGATTTGATGCCTGAGAGTAAGAAAAAGAAACTGGAATATGCT
GAAAAAGAAGAAGAACAATGTGTGCTACCTATGGAAGATGAGGGCACAGTACAACTCCCA
TTGGAAGGGCACTATAGAGATGATCCATCTGTGATCAATATATCTGATGAAATGTCAAAG
ACTGCCTTGTGGAGGAACCTTCTGATTACTGCCGATAACTCAAAAGATAAGGAGTCAAGC
TTTCCTTCCAAAAGCTCCCCTTCCTAA

1. Wang CZ, Yano H, Nagashima K, Seino S: The Na+-driven Cl-/HCO3- exchanger. Cloning, tissue distribution, and functional characterization. J Biol Chem. 2000 Nov 10;275(45):35486-90. [PubMed ]

1. Protein DRA
2. Down-regulated in adenoma
3. Solute carrier family 26 member 3

MIEPFGNQYIVARPVYSTNAFEENHKKTGRHHKTFLDHLKVCCSCSPQKAKRIVLSLFPI
ASWLPAYRLKEWLLSDIVSGISTGIVAVLQGLAFALLVDIPPVYGLYASFFPAIIYLFFG
TSRHISVGPFPILSMMVGLAVSGAVSKAVPDRNATTLGLPNNSNNSSLLDDERVRVAAAA
SVTVLSGIIQLAFGILRIGFVVIYLSESLISGFTTAAAVHVLVSQLKFIFQLTVPSHTDP
VSIFKVLYSVFSQIEKTNIADLVTALIVLLVVSIVKEINQRFKDKLPVPIPIEFIMTVIA
AGVSYGCDFKNRFKVAVVGDMNPGFQPPITPDVETFQNTVGDCFGIAMVAFAVAFSVASV
YSLKYDYPLDGNQELIALGLGNIVCGVFRGFAGSTALSRSAVQESTGGKTQIAGLIGAII
VLIVVLAIGFLLAPLQKSVLAALALGNLKGMLMQFAEIGRLWRKDKYDCLIWIMTFIFTI
VLGLGLGLAASVAFQLLTIVFRTQFPKCSTLANIGRTNIYKNKKDYYDMYEPEGVKIFRC
PSPIYFANIGFFRRKLIDAVGFSPLRILRKRNKALRKIRKLQKQGLLQVTPKGFICTVDT
IKDSDEELDNNQIEVLDQPINTTDLPFHIDWNDDLPLNIEVPKISLHSLILDFSAVSFLD
VSSVRGLKSILQEFIRIKVDVYIVGTDDDFIEKLNRYEFFDGEVKSSIFFLTIHDAVLHI
LMKKDYSTSKFNPSQEKDGKIDFTINTNGGLRNRVYEVPVETKF

• STAS (PF01740 )
• Sulfate_transp (PF00916 )

• 1-491

• 77-97 100-120 125-145 176-196 198-218 259-279 286-306 343-363 375-395 412-432 439-459 470-490 644-664 702-722

ATGATTGAACCCTTTGGGAATCAGTATATTGTGGCCAGGCCAGTGTATTCTACAAATGCT
TTTGAGGAAAATCATAAAAAGACAGGAAGACATCATAAGACATTTCTGGATCATCTCAAA
GTGTGTTGTAGCTGTTCCCCACAAAAGGCCAAGAGAATTGTCCTCTCTTTGTTCCCCATA
GCATCTTGGTTGCCAGCATACCGGCTTAAAGAATGGTTGCTCAGTGATATTGTTTCTGGT
ATCAGCACAGGGATTGTGGCCGTACTACAAGGTTTAGCATTTGCTCTGCTGGTCGACATT
CCCCCAGTCTATGGGTTGTATGCATCCTTTTTCCCAGCCATAATCTACCTTTTCTTCGGC
ACTTCCAGACACATATCCGTGGGTCCGTTTCCGATTCTGAGTATGATGGTGGGACTAGCA
GTTTCAGGAGCAGTTTCAAAAGCAGTCCCAGATCGCAATGCAACTACTTTGGGATTGCCT
AACAACTCGAATAATTCTTCACTACTGGATGACGAGAGGGTGAGGGTGGCGGCGGCGGCA
TCAGTCACAGTGCTTTCTGGAATCATCCAGTTGGCTTTTGGGATTCTGCGGATTGGATTT
GTAGTGATATACCTGTCTGAGTCCCTCATCAGTGGCTTCACTACTGCTGCTGCTGTTCAT
GTTTTGGTTTCCCAACTCAAATTCATTTTTCAGTTGACAGTCCCGTCACACACTGATCCA
GTTTCAATTTTCAAAGTACTATACTCTGTATTCTCACAAATAGAGAAGACTAATATTGCA
GACCTGGTGACAGCTCTGATTGTCCTTTTGGTTGTATCCATTGTTAAAGAAATAAATCAG
CGCTTCAAAGACAAACTTCCAGTGCCCATTCCAATCGAATTCATTATGACCGTGATTGCA
GCAGGTGTATCCTACGGCTGTGACTTTAAAAACAGGTTTAAAGTGGCTGTGGTTGGGGAC
ATGAATCCTGGATTTCAGCCCCCTATTACACCTGACGTGGAGACTTTCCAAAACACCGTA
GGAGATTGCTTCGGCATCGCAATGGTTGCATTTGCAGTGGCCTTTTCAGTTGCCAGCGTC
TATTCCCTCAAATACGATTATCCACTTGATGGCAATCAGGAGTTAATAGCCTTGGGACTG
GGTAACATAGTCTGTGGAGTATTCAGAGGATTTGCTGGGAGTACTGCCCTCTCCAGATCA
GCAGTTCAGGAGAGCACAGGAGGCAAAACACAGATTGCTGGGCTTATTGGTGCCATCATC
GTGCTGATTGTCGTTCTAGCCATTGGATTTCTCCTGGCGCCTCTACAAAAGTCCGTCCTG
GCAGCTTTAGCATTGGGAAACTTAAAGGGAATGCTGATGCAGTTTGCTGAAATAGGCAGA
TTGTGGCGAAAGGACAAATATGATTGTTTAATTTGGATCATGACCTTCATCTTCACCATT
GTCCTGGGACTCGGGTTAGGCCTGGCAGCTAGTGTGGCATTTCAACTGCTAACCATCGTG
TTCAGGACCCAATTTCCAAAATGCAGCACGCTGGCTAATATTGGAAGAACCAACATCTAT
AAGAATAAAAAAGATTATTATGATATGTATGAGCCAGAAGGAGTGAAAATTTTCAGATGT
CCATCTCCTATCTACTTTGCAAACATTGGTTTCTTTAGGCGGAAACTTATCGATGCTGTT
GGCTTTAGTCCACTTCGAATTCTACGCAAGCGCAACAAAGCTTTGAGGAAAATCCGAAAA
CTGCAGAAGCAAGGCTTGCTACAAGTGACACCAAAAGGATTTATATGTACTGTTGACACC
ATAAAAGATTCTGACGAAGAGCTGGACAACAATCAGATAGAAGTACTGGACCAGCCAATC
AATACCACAGACCTGCCTTTCCACATTGACTGGAATGATGATCTTCCTCTCAACATTGAG
GTCCCCAAAATCAGCCTCCACAGCCTCATTCTCGACTTTTCAGCAGTGTCCTTTCTTGAT
GTTTCTTCAGTGAGGGGCCTTAAATCGATTTTGCAAGAATTTATCAGGATCAAGGTAGAT
GTGTATATCGTTGGAACTGATGATGACTTCATTGAGAAGCTTAACCGGTATGAATTTTTT
GATGGTGAAGTGAAAAGCTCAATATTTTTCTTAACAATCCATGATGCTGTTTTGCATATT
TTGATGAAGAAAGATTACAGTACTTCAAAGTTTAATCCCAGTCAGGAAAAAGATGGAAAA
ATTGATTTTACCATAAATACAAATGGAGGATTACGTAATCGGGTATATGAGGTGCCAGTT
GAAACAAAATTCTAA

1. Schweinfest CW, Henderson KW, Suster S, Kondoh N, Papas TS: Identification of a colon mucosa gene that is down-regulated in colon adenomas and adenocarcinomas. Proc Natl Acad Sci U S A. 1993 May 1;90(9):4166-70. [PubMed ]
2. Sandal NN, Marcker KA: Similarities between a soybean nodulin, Neurospora crassa sulphate permease II and a putative human tumour suppressor. Trends Biochem Sci. 1994 Jan;19(1):19. [PubMed ]
3. Hoglund P, Haila S, Socha J, Tomaszewski L, Saarialho-Kere U, Karjalainen-Lindsberg ML, Airola K, Holmberg C, de la Chapelle A, Kere J: Mutations of the Down-regulated in adenoma (DRA) gene cause congenital chloride diarrhoea. Nat Genet. 1996 Nov;14(3):316-9. [PubMed ]
4. Hoglund P, Haila S, Gustavson KH, Taipale M, Hannula K, Popinska K, Holmberg C, Socha J, de la Chapelle A, Kere J: Clustering of private mutations in the congenital chloride diarrhea/down-regulated in adenoma gene. Hum Mutat. 1998;11(4):321-7. [PubMed ]
5. Hoglund P, Sormaala M, Haila S, Socha J, Rajaram U, Scheurlen W, Sinaasappel M, de Jonge H, Holmberg C, Yoshikawa H, Kere J: Identification of seven novel mutations including the first two genomic rearrangements in SLC26A3 mutated in congenital chloride diarrhea. Hum Mutat. 2001 Sep;18(3):233-42. [PubMed ]

1. Sodium bicarbonate cotransporter 2
2. Sodium bicarbonate cotransporter 2b
3. Bicarbonate transporter
4. Solute carrier family 4 member 7

MERFRLEKKLPGPDEEAVVDLGKTSSTVNTKFEKEELESHRAVYIGVHVPFSKESRRRHR
HRGHKHHHRRRKDKESDKEDGRESPSYDTPSQRVQFILGTEDDDEEHIPHDLFTEMDELC
YRDGEEYEWKETARWLKFEEDVEDGGDRWSKPYVATLSLHSLFELRSCILNGTVMLDMRA
STLDEIADMVLDNMIASGQLDESIRENVREALLKRHHHQNEKRFTSRIPLVRSFADIGKK
HSDPHLLERNGEGLSASRHSLRTGLSASNLSLRGESPLSLLLGHLLPSSRAGTPAGSRCT
TPVPTPQNSPPSSPSISRLTSRSSQKSQRQAPELLVSPASDDIPTVVIHPPEEDLEAALK
GEEQKNEENVDLTPGILASPQSAPGNLDNSKSGEIKGNGSGGSRENSTVDFSKVDMNFMR
KIPTGAEASNVLVGEVDFLERPIIAFVRLAPAVLLTGLTEVPVPTRFLFLLLGPAGKAPQ
YHEIGRSIATLMTDEIFHDVAYKAKDRNDLLSGIDEFLDQVTVLPPGEWDPSIRIEPPKS
VPSQEKRKIPVFHNGSTPTLGETPKEAAHHAGPELQRTGRLFGGLILDIKRKAPFFLSDF
KDALSLQCLASILFLYCACMSPVITFGGLLGEATEGRISAIESLFGASLTGIAYSLFAGQ
PLTILGSTGPVLVFEKILYKFCRDYQLSYLSLRTSIGLWTSFLCIVLVATDASSLVCYIT
RFTEEAFAALICIIFIYEALEKLFDLGETYAFNMHNNLDKLTSYSCVCTEPPNPSNETLA
QWKKDNITAHNISWRNLTVSECKKLRGVFLGSACGHHGPYIPDVLFWCVILFFTTFFLSS
FLKQFKTKRYFPTKVRSTISDFAVFLTIVIMVTIDYLVGVPSPKLHVPEKFEPTHPERGW
IISPLGDNPWWTLLIAAIPALLCTILIFMDQQITAVIINRKEHKLKKGAGYHLDLLMVGV
MLGVCSVMGLPWFVAATVLSISHVNSLKVESECSAPGEQPKFLGIREQRVTGLMIFILMG
LSVFMTSVLKFIPMPVLYGVFLYMGVSSLKGIQLFDRIKLFGMPAKHQPDLIYLRYVPLW
KVHIFTVIQLTCLVLLWVIKVSAAAVVFPMMVLALVFVRKLMDLCFTKRELSWLDDLMPE
SKKKKEDDKKKKEKEEAERMLQDDDDTVHLPFEGGSLLQIPVKALKYSPDKPVSVKISFE
DEPRKKYVDAETSL

• Band_3_cyto (PF07565 )
• HCO3_cotransp (PF00955 )

• 1-1104

• 609-629 638-658 696-716 726-746 818-838 862-882 909-929 955-975 1012-1032 1035-1055 1093-1113

ATGGCTGTAACACAGTTCATCCATTTCCGTGAAGAGATCATGGGGAATATGTTCTTCATC
ATCATCTTCAGTACCAAGGATAAACTGTGTTACAGAGATGGAGAAGAATATGAATGGAAA
GAAACTGCTAGATGGCTGAAATTTGAAGAGGATGTTGAAGATGGCGGTGACCGATGGAGT
AAACCTTATGTGGCAACTCTCTCTTTGCACAGTCTTTTTGAACTAAGGAGTTGCATCCTC
AATGGAACAGTCATGCTGGATATGAGAGCAAGCACTCTAGATGAAATAGCAGATATGGTA
TTAGACAACATGATAGCTTCTGGCCAATTAGACGAGTCCATACGAGAGAATGTCAGAGAA
GCTCTTCTGAAGAGACATCATCATCAGAATGAGAAAAGATTCACCAGTCGGATTCCTCTT
GTTCGATCTTTTGCAGATATAGGCAAGAAACATTCTGACCCTCACTTGCTTGAAAGGAAT
GGTATTTTGGCCTCTCCCCAGTCTGCTCCTGGAAACTTGGACAATAGTAAAAGTGGAGAA
ATTAAAGGTAATGGAAGTGGTGGAAGCAGAGAAAATAGTACTGTTGACTTCAGCAAGGTT
GATATGAATTTCATGAGAAAAATTCCTACGGGTGCTGAGGCATCCAACGTCCTGGTGGGC
GAAGTAGACTTTTTGGAAAGGCCAATAATTGCATTTGTGAGACTGGCTCCTGCTGTCCTC
CTTACAGGGTTGACTGAGGTCCCTGTTCCAACCAGGTTTTTGTTTTTGTTATTGGGTCCA
GCGGGCAAGGCACCACAGTACCATGAAATTGGACGATCAATAGCCACTCTCATGACAGAT
GAGATTTTCCATGATGTAGCTTATAAAGCAAAAGACAGAAATGACCTCTTATCTGGAATT
GATGAATTTTTAGATCAAGTAACTGTCCTACCTCCAGGAGAGTGGGATCCTTCTATACGC
ATAGAACCACCAAAAAGTGTCCCTTCTCAGGAAAAGAGAAAGATTCCTGTGTTTCACAAT
GGATCTACCCCCACACTGGGTGAGACTCCTAAAGAGGCCGCTCATCATGCTGGGCCTGAG
CTACAGAGGACTGGACGGCTTTTTGGTGGGTTGATACTTGACATCAAAAGGAAAGCACCT
TTTTTCTTGAGTGACTTCAAGGATGCATTAAGCCTGCAGTGCCTGGCCTCGATTCTTTTC
CTATACTGTGCCTGTATGTCTCCTGTAATCACTTTTGGAGGGCTGCTTGGAGAAGCTACA
GAAGGCAGAATAAGTGCAATAGAGTCTCTTTTTGGAGCATCATTAACTGGGATTGCCTAT
TCATTGTTTGCTGGGCAACCTCTAACAATATTGGGGAGCACAGGTCCAGTTCTAGTGTTT
GAAAAAATTTTATATAAATTCTGCAGAGATTATCAACTTTCTTATCTGTCTTTAAGAACC
AGTATTGGTCTGTGGACTTCTTTTTTGTGCATTGTTTTGGTTGCAACAGATGCAAGCAGC
CTTGTGTGTTATATTACTCGATTTACAGAAGAGGCTTTTGCAGCCCTTATTTGCATCATA
TTCATCTACGAGGCTTTGGAGAAGCTCTTTGATTTAGGAGAAACATATGCATTTAATATG
CACAACAACTTAGATAAACTGACCAGCTACTCATGTGTATGTACTGAACCTCCAAACCCC
AGCAATGAAACTCTAGCACAATGGAAGAAAGATAATATAACAGCACACAATATTTCCTGG
AGAAATCTTACTGTTTCTGAATGTAAAAAACTTCGTGGTGTATTCTTGGGGTCAGCTTGT
GGTCATCATGGACCTTATATTCCAGATGTGCTCTTTTGGTGTGTCATCTTGTTTTTCACA
ACATTTTTTCTGTCTTCATTCCTCAAGCAATTTAAGACCAAGCGTTACTTTCCTACCAAG
GTGCGATCGACAATCAGTGATTTTGCTGTATTTCTCACAATAGTAATAATGGTTACAATT
GACTACCTTGTAGGAGTTCCATCTCCTAAACTTCATGTTCCTGAAAAATTTGAGCCTACT
CATCCAGAGAGAGGGTGGATCATAAGCCCACTGGGAGATAATCCTTGGTGGACCTTATTA
ATAGCTGCTATTCCTGCTTTGCTTTGTACCATTCTCATCTTTATGGATCAACAAATCACA
GCTGTAATTATAAACAGAAAGGAACACAAATTGAAGAAAGGAGCTGGCTATCACCTTGAT
TTGCTCATGGTTGGCGTTATGTTGGGAGTTTGCTCTGTCATGGGACTTCCATGGTTTGTG
GCTGCAACAGTGTTGTCAATAAGTCATGTCAACAGCTTAAAAGTTGAATCTGAATGTTCT
GCTCCAGGGGAACAACCCAAGTTTTTGGGAATTCGTGAACAGCGGGTTACAGGGCTAATG
ATTTTTATTCTAATGGGCCTCTCTGTGTTCATGACTTCAGTCCTAAAGTTTATTCCAATG
CCTGTTCTGTATGGTGTTTTCCTTTATATGGGAGTTTCCTCATTAAAAGGAATCCAGTTA
TTTGACCGGATAAAATTATTTGGAATGCCTGCTAAGCATCAGCCTGATTTGATATACCTC
CGGTATGTGCCGCTCTGGAAGGTCCATATTTTCACAGTCATTCAGCTTACTTGCTTGGTC
CTTTTATGGGTGATAAAAGTTTCAGCTGCTGCAGTGGTTTTTCCCATGATGGTTCTTGCA
TTAGTGTTTGTGCGCAAACTCATGGACCTGTGTTTCACGAAGAGAGAACTTAGTTGGCTT
GATGATCTTATGCCAGAAAGTAAGAAAAAGAAAGAAGATGACAAAAAGAAAAAAGAGAAA
GAGGAAGCTGAACGGATGCTTCAAGACGATGATGATACTGTGCACCTTCCATTTGAAGGG
GGAAGTCTCTTGCAAATTCCAGTCAAGGCCCTAAAATATAGTGGTGATCCCTCAATTGGT
AACATATCAGATGAAATGGCCAAAACTGCACAGTGGAAGGCACTTTCCATGAATACTGAG
AATGCCAAAGTAACCAGATCTAACATGAGTCCTGATAAACCTGTGAGTGTGAAATAA

1. Pushkin A, Abuladze N, Lee I, Newman D, Hwang J, Kurtz I: Cloning, tissue distribution, genomic organization, and functional characterization of NBC3, a new member of the sodium bicarbonate cotransporter family. J Biol Chem. 1999 Jun 4;274(23):16569-75. [PubMed ]

MNTPKEEFQDWPIVRIAAHLPDLIVYGHFSPERPFMDYFDGVLMFVDISGFTAMTEKFSS
AMYMDRGAEQLVEILNYHISAIVEKVLIFGGDILKFAGDALLALWRVERKQLKNIITVVI
KCSLEIHGLFETQEWEEGLDIRVKIGLAAGHISMLVFGDETHSHFLVIGQAVDDVRLAQN
MAQMNDVILSPNCWQLCDRSMIEIESVPDQRAVKVNFLKPPPNFNFDEFFTKCTTFMHYY
PSGEHKNLLRLACTLKPDPELEMSLQKYVMESILKQIDNKQLQGYLSELRPVTIVFVNLM
FEDQDKAEEIGPAIQDAYMHITSVLKIFQGQINKVFMFDKGCSFLCVFGFPGEKVPDELT
HALECAMDIFDFCSQVHKIQTVSIGVASGIVFCGIVGHTVRHEYTVIGQKVNLAARMMMY
YPGIVTCDSVTYNGSNLPAYFFKELPKKVMKGVADSGPLYQYWGRTEKVMFGMACLICNR
KEDYPLLGRNKEINYFMYTMKKFLISNSSQVLMYEGLPGYGKSQILMKIEYLAQGKNHRI
IAISLNKISFHQTFYTIQMFMANVLGLDTCKHYKERQTNLRNKVMTLLDEKFYCLLNDIF
HVQFPISREISRMSTLKKQKQLEILFMKILKLIVKEERIIFIIDEAQFVDSTSWRFMEKL
IRTLPIFIIMSLCPFVNIPCAAARAVIKNRNTTYIVIGAVQPNDISNKICLDLNVSCISK
ELDSYLGEGSCGIPFYCEELLKNLEHHEVLVFQQTESEEKTNRTWNNLFKYSIKLTEKLN
MVTLHSDKESEEVCHLTSGVRLKNLSPPTSLKEISLIQLDSMRLSHQMLVRCAAIIGLTF
TTELLFEILPCWNMKMMIKTLATLVESNIFYCFRNGKELQKALKQNDPSFEVHYRSLSLK
PSEGMDHGEEEQLRELENEVIECHRIRFCNPMMQKTAYELWLKDQRKAMHLKCARFLEED
AHRCDHCRGRDFIPYHHFTVNIRLNALDMDAIKKMAMSHGFKTEEKLILSNSEIPETSAF
FPENRSPEEIREKILNFFDHVLTKMKTSDEDIIPLESCQCEEILEIVILPLAHHFLALGE
NDKALYYFLEIASAYLIFCDNYMAYMYLNEGQKLLKTLKKDKSWSQTFESATFYSLKGEV
CFNMGQIVLAKKMLRKALKLLNRIFPYNLISLFLHIHVEKNRHFHYVNRQAQESPPPGKK
RLAQLYRQTVCLSLLWRIYSYSYLFHCKYYAHLAVMMQMNTALETQNCFQIIKAYLDYSL
YHHLAGYKGVWFKYEVMAMEHIFNLPLKGEGIEIVAYVAETLVFNKLIMGHLDLAIELGS
RALQMWALLQNPNRHYQSLCRLSRCLLLNSRYPQLIQVPGRLWELSVTQEHIFSKAFFYF
VCLDILLYSGFVYRTFEECLEFIHQYENNRILKFHSGLLLGLYSSVAIWYARLQEWDNFY
KFSNRAKNLLPRRTMTLTYYDGISRYMEGQVLHLQKQIKEQSENAQASGEELLKNLENLV
AQNTTGPVFCPRLYHLMAYVCILMGDGQKCGLFLNTALRLSETQGNILEKCWLNMNKESW
YSTSELKEDQWLQTILSLPSWEKIVAGRVNIQDLQKNKFLMRANTVDNHF

• ATP --> cAMP + Diphosphate

• Guanylate_cyc (PF00211 )

• None

• None

1. Solute carrier family 26, member 9, isoform CRA_b
2. Solute carrier family 26, member 9

MSQPRPRYVVDRAAYSLTLFDDEFEKKDRTYPVGEKLRNAFRCSSAKIKAVVFGLLPVLS
WLPKYKIKDYIIPDLLGGLSGGSIQVPQGMAFALLANLPAVNGLYSSFFPLLTYFFLGGV
HQMVPGTFAVISILVGNICLQLAPESKFQVFNNATNESYVDTAAMEAERLHVSATLACLT
AIIQMGLGFMQFGFVAIYLSESFIRGFMTAAGLQILISVLKYIFGLTIPSYTGPGSIVFT
FIDICKNLPHTNIASLIFALISGAFLVLVKELNARYMHKIRFPIPTEMIVVVVATAISGG
CKMPKKYHMQIVGEIQRGFPTPVSPVVSQWKDMIGTAFSLAIVSYVINLAMGRTLANKHG
YDVDSNQEMIALGCSNFFGSFFKIHVICCALSVTLAVDGAGGKSQVASLCVSLVVMITML
VLGIYLYPLPKSVLGALIAVNLKNSLKQLTDPYYLWRKSKLDCCIWVVSFLSSFFLSLPY
GVAVGVAFSVLVVVFQTQFRNGYALAQVMDTDIYVNPKTYNRAQDIQGIKIITYCSPLYF
ANSEIFRQKVIAKTGMDPQKVLLAKQKYLKKQEKRRMRPTQQRRSLFMKTKTVSLQELQQ
DFENAPPTDPNNNQTPANGTSVSYITFSPDSSSPAQSEPPASAEAPGEPSDMLASVPPFV
TFHTLILDMSGVSFVDLMGIKALAKLSSTYGKIGVKVFLVNIHAQVYNDISHGGVFEDGS
LECKHVFPSIHDAVLFAQANARDVTPGHNFQGAPGDAELSLYDSEEDIRSYWDLEQEMFG
SMFHAETLTAL

• (2)Bicarbonate[c] + Sulfate[e] --> (2)Bicarbonate[e] + Sulfate[c]

• STAS (PF01740 )
• Sulfate_transp (PF00916 )

• None

• None

1. Lohi H, Kujala M, Makela S, Lehtonen E, Kestila M, Saarialho-Kere U, Markovich D, Kere J: Functional characterization of three novel tissue-specific anion exchangers SLC26A7, -A8, and -A9. J Biol Chem. 2002 Apr 19;277(16):14246-54. Epub 2002 Feb 7. [PubMed ]

MTGAKRKKKSMLWSKMHTPQCEDIIQWCRRRLPILDWAPHYNLKENLLPDTVSGIMLAVQ
QVTQGLAFAVLSSVHPVFGLYGSLFPAIIYAIFGMGHHVATGTFALTSLISANAVERIVP
QNMQNLTTQSNASVLGLSDFEMQRIHVAAAVSFLGGVIQVAMFVLQLGSATFVVTEPVIS
AMTTGAATHVVTSQVKYLLGMKMPYISGPLGFFYIYAYVFENIKSVRLEALLLSLLSIVV
LVLVKELNEQFKRKIKVVLPVDLVLIIAASFACYCTNMENTYGLEVVGHIPQGIPSPRAP
PMNILSAVITEAFGVALVGYVASLALAQGSAKKFKYSIDDNQEFLAHGLSNIVSSFFFCI
PSAAAMGRTAGLYSTGAKTQVACLISCIFVLIVIYAIGPLLYWLPMCVLASIIVVGLKGM
LIQFRDLKKYWNVDKIDWGIWVSTYVFTICFAANVGLLFGVVCTIAIVIGRFPRAMTVSI
KNMKEMEFKVKTEMDSETLQQVKIISINNPLVFLNAKKFYTDLMNMIQKENACNQPLDDI
SKCEQNTLLNSLSNGNCNEEASQSCPNEKCYLILDCSGFTFFDYSGVSMLVEVYMDCKGR
SVDVLLAHCTASLIKAMTYYGNLDSEKPIFFESVSAAISHIHSNKNLSKLSDHSEV

• (2)Bicarbonate[c] + Sulfate[e] --> (2)Bicarbonate[e] + Sulfate[c]

• STAS (PF01740 )
• Sulfate_transp (PF00916 )

• None

• None

1. Vincourt JB, Jullien D, Kossida S, Amalric F, Girard JP: Molecular cloning of SLC26A7, a novel member of the SLC26 sulfate/anion transporter family, from high endothelial venules and kidney. Genomics. 2002 Feb;79(2):249-56. [PubMed ]

1. Sodium bicarbonate cotransporter 4

MKVKEEKAGVGKLDHTNHRRRFPDQKECPPIHIGLPVPTYPQRKTDQKGHLSGLQKVHWG
LRPDQPQQELTGPGSGASSQDSSMDLISRTRSPAAEQLQDILGEEDEAPNPTLFTEMDTL
QHDGDQMEWKESARWIKFEEKVEEGGERWSKPHVSTLSLHSLFELRTCLQTGTVLLDLDS
GSLPQIIDDVIEKQIEDGLLRPELRERVSYVLLRRHRHQTKKPIHRSLADIGKSVSTTNR
SPARSPGAGPSLHHSTEDLRMRQSANYGRLCHAQSRSMNDISLTPNTDQRKNKFMKKIPK
DSEASNVLVGEVDFLDQPFIAFVRLIQSAMLGGVTEVPVPTRFLFILLGPSGRAKSYNEI
GRAIATLMVDDLFSDVAYKARNREDLIAGIDEFLDEVIVLPPGEWDPNIRIEPPKKVPSA
DKRKSVFSLAELGQMNGSVGGGGGAPGGGNGGGGGGGSGGGAGSGGAGGTSSGDDGEMPA
MHEIGEELIWTGRFFGGLCLDIKRKLPWFPSDFYDGFHIQSISAILFIYLGCITNAITFG
GLLGDATDNYQGVMESFLGTAMAGSLFCLFSGQPLIILSSTGPILIFEKLLFDFSKGNGL
DYMEFRLWIGLHSAVQCLILVATDASFIIKYITRFTEEGFSTLISFIFIYDAIKKMIGAF
KYYPINMDFKPNFITTYKCECVAPDTVNTTVFNASAPLAPDTNASLYNLLNLTALDWSLL
SKKECLSYGGRLLGNSCKFIPDLALMSFILFFGTYSMTLTLKKFKFSRYFPTKVRALVAD
FSIVFSILMFCGIDACFGLETPKLHVPSVIKPPRPDRGWFVAPFGKNPWWVYPASILPAL
LVTILIFMDQQITAVIVNRKENKLKKAAGYHLDLFWVGILMALCSFMGLPWYVAATVISI
AHIDSLKMETETSAPGEQPQFLGVREQRVTGIIVFILTGISVFLAPILKCIPLPVLYGVF
LYMGVASLNGIQMGTGGSEFKIQKKLTPFWERCKLFLMPAKHQPDHAFLRHVPLRRIHLF
TLVQILCLAVLWILKSTVAAIIFPVMILGLIIVRRLLDFIFSQHDLAWIDNILPEKEKKE
TDKKRKRKKGAHEDCDEEPQFPPPSVIKIPMESVQSDPQNGIHCIARKRSSSWSYSL

• (2)Bicarbonate[e] + Sodium[e] <==> (2)Bicarbonate[c] + Sodium[c]

• Band_3_cyto (PF07565 )
• HCO3_cotransp (PF00955 )

• None

• None

1. Pushkin A, Abuladze N, Newman D, Lee I, Xu G, Kurtz I: Two C-terminal variants of NBC4, a new member of the sodium bicarbonate cotransporter family: cloning, characterization, and localization. IUBMB Life. 2000 Jul;50(1):13-9. [PubMed ]

1. Vitelliform macular dystrophy protein 2
2. TU15B

MTITYTSQVANARLGSFSRLLLCWRGSIYKLLYGEFLIFLLCYYIIRFIYRLALTEEQQL
MFEKLTLYCDSYIQLIPISFVLGFYVTLVVTRWWNQYENLPWPDRLMSLVSGFVEGKDEQ
GRLLRRTLIRYANLGNVLILRSVSTAVYKRFPSAQHLVQAGFMTPAEHKQLEKLSLPHNM
FWVPWVWFANLSMKAWLGGRIRDPILLQSLLNEMNTLRTQCGHLYAYDWISIPLVYTQVV
TVAVYSFFLTCLVGRQFLNPAKAYPGHELDLVVPVFTFLQFFFYVGWLKVAEQLINPFGE
DDDDFETNWIVDRNLQVSLLAVDEMHQDLPRMEPDMYWNKPEPQPPYTAASAQFRRASFM
GSTFNISLNKEEMEFQPNQEDEEDAHAGIIGRFLGLQSHDHHPPRANSRTKLLWPKRESL
LHEGLPKNHKAAKQNVRGQEDNKAWKLKAVDAFKSAPLYQRPGYYSAPQTPLSPTPMFFP
LEPSAPSKLHSVTGIDTKDKSLKTVSSGAKKSFELLSESDGALMEHPEVSQVRRKTVEFN
LTDMPEIPENHLKEPLEQSPTNIHTTLKDHMDPYWALENRDEAHS

• Bestrophin (PF01062 )

• None

• 26-46 71-91 179-199 271-291

ATGACCATCACTTACACAAGCCAAGTGGCTAATGCCCGCTTAGGCTCCTTCTCCCGCCTG
CTGCTGTGCTGGCGGGGCAGCATCTACAAGCTGCTATATGGCGAGTTCTTAATCTTCCTG
CTCTGCTACTACATCATCCGCTTTATTTATAGGCTGGCCCTCACGGAAGAACAACAGCTG
ATGTTTGAGAAACTGACTCTGTATTGCGACAGCTACATCCAGCTCATCCCCATTTCCTTC
GTGCTGGGCTTCTACGTGACGCTGGTCGTGACCCGCTGGTGGAACCAGTACGAGAACCTG
CCGTGGCCCGACCGCCTCATGAGCCTGGTGTCGGGCTTCGTCGAAGGCAAGGACGAGCAA
GGCCGGCTGCTGCGGCGCACGCTCATCCGCTACGCCAACCTGGGCAACGTGCTCATCCTG
CGCAGCGTCAGCACCGCAGTCTACAAGCGCTTCCCCAGCGCCCAGCACCTGGTGCAAGCA
GGCTTTATGACTCCGGCAGAACACAAGCAGTTGGAGAAACTGAGCCTACCACACAACATG
TTCTGGGTGCCCTGGGTGTGGTTTGCCAACCTGTCAATGAAGGCGTGGCTTGGAGGTCGA
ATCCGGGACCCTATCCTGCTCCAGAGCCTGCTGAACGAGATGAACACCTTGCGTACTCAG
TGTGGACACCTGTATGCCTACGACTGGATTAGTATCCCACTGGTGTATACACAGGTGGTG
ACTGTGGCGGTGTACAGCTTCTTCCTGACTTGTCTAGTTGGGCGGCAGTTTCTGAACCCA
GCCAAGGCCTACCCTGGCCATGAGCTGGACCTCGTTGTGCCCGTCTTCACGTTCCTGCAG
TTCTTCTTCTATGTTGGCTGGCTGAAGGTGGCAGAGCAGCTCATCAACCCCTTTGGAGAG
GATGATGATGATTTTGAGACCAACTGGATTGTCGACAGGAATTTGCAGGTGTCCCTGTTG
GCTGTGGATGAGATGCACCAGGACCTGCCTCGGATGGAGCCGGACATGTACTGGAATAAG
CCCGAGCCACAGCCCCCCTACACAGCTGCTTCCGCCCAGTTCCGTCGAGCCTCCTTTATG
GGCTCCACCTTCAACATCAGCCTGAACAAAGAGGAGATGGAGTTCCAGCCCAATCAGGAG
GACGAGGAGGATGCTCACGCTGGCATCATTGGCCGCTTCCTAGGCCTGCAGTCCCATGAT
CACCATCCTCCCAGGGCAAACTCAAGGACCAAACTACTGTGGCCCAAGAGGGAATCCCTT
CTCCACGAGGGCCTGCCCAAAAACCACAAGGCAGCCAAACAGAACGTTAGGGGCCAGGAA
GACAACAAGGCCTGGAAGCTTAAGGCTGTGGACGCCTTCAAGTCTGCCCCACTGTATCAG
AGGCCAGGCTACTACAGTGCCCCACAGACACCCCTCAGCCCCACTCCCATGTTCTTCCCC
CTAGAACCATCAGCGCCGTCAAAGCTTCACAGTGTCACAGGCATAGACACCAAAGACAAA
AGCTTAAAGACTGTGAGTTCTGGGGCCAAGAAAAGTTTTGAATTGCTCTCAGAGAGCGAT
GGGGCCTTGATGGAGCACCCAGAAGTATCTCAAGTGAGGAGGAAAACTGTGGAGTTTAAC
CTGACGGATATGCCAGAGATCCCCGAAAATCACCTCAAAGAACCTTTGGAACAATCACCA
ACCAACATACACACTACACTCAAAGATCACATGGATCCTTATTGGGCCTTGGAAAACAGG
GATGAAGCACATTCCTAA

1. Marquardt A, Stohr H, Passmore LA, Kramer F, Rivera A, Weber BH: Mutations in a novel gene, VMD2, encoding a protein of unknown properties cause juvenile-onset vitelliform macular dystrophy (Best's disease). Hum Mol Genet. 1998 Sep;7(9):1517-25. [PubMed ]
2. Petrukhin K, Koisti MJ, Bakall B, Li W, Xie G, Marknell T, Sandgren O, Forsman K, Holmgren G, Andreasson S, Vujic M, Bergen AA, McGarty-Dugan V, Figueroa D, Austin CP, Metzker ML, Caskey CT, Wadelius C: Identification of the gene responsible for Best macular dystrophy. Nat Genet. 1998 Jul;19(3):241-7. [PubMed ]
3. Tsunenari T, Sun H, Williams J, Cahill H, Smallwood P, Yau KW, Nathans J: Structure-function analysis of the bestrophin family of anion channels. J Biol Chem. 2003 Oct 17;278(42):41114-25. Epub 2003 Aug 7. [PubMed ]
4. Sun H, Tsunenari T, Yau KW, Nathans J: The vitelliform macular dystrophy protein defines a new family of chloride channels. Proc Natl Acad Sci U S A. 2002 Mar 19;99(6):4008-13. [PubMed ]
5. Caldwell GM, Kakuk LE, Griesinger IB, Simpson SA, Nowak NJ, Small KW, Maumenee IH, Rosenfeld PJ, Sieving PA, Shows TB, Ayyagari R: Bestrophin gene mutations in patients with Best vitelliform macular dystrophy. Genomics. 1999 May 15;58(1):98-101. [PubMed ]
6. Bakall B, Marknell T, Ingvast S, Koisti MJ, Sandgren O, Li W, Bergen AA, Andreasson S, Rosenberg T, Petrukhin K, Wadelius C: The mutation spectrum of the bestrophin protein--functional implications. Hum Genet. 1999 May;104(5):383-9. [PubMed ]
7. Allikmets R, Seddon JM, Bernstein PS, Hutchinson A, Atkinson A, Sharma S, Gerrard B, Li W, Metzker ML, Wadelius C, Caskey CT, Dean M, Petrukhin K: Evaluation of the Best disease gene in patients with age-related macular degeneration and other maculopathies. Hum Genet. 1999 Jun;104(6):449-53. [PubMed ]
8. Lotery AJ, Namperumalsamy P, Jacobson SG, Weleber RG, Fishman GA, Musarella MA, Hoyt CS, Heon E, Levin A, Jan J, Lam B, Carr RE, Franklin A, Radha S, Andorf JL, Sheffield VC, Stone EM: Mutation analysis of 3 genes in patients with Leber congenital amaurosis. Arch Ophthalmol. 2000 Apr;118(4):538-43. [PubMed ]
9. Marchant D, Gogat K, Boutboul S, Pequignot M, Sternberg C, Dureau P, Roche O, Uteza Y, Hache JC, Puech B, Puech V, Dumur V, Mouillon M, Munier FL, Schorderet DF, Marsac C, Dufier JL, Abitbol M: Identification of novel VMD2 gene mutations in patients with best vitelliform macular dystrophy. Hum Mutat. 2001 Mar;17(3):235. [PubMed ]

1. Vitelliform macular dystrophy 2-like protein 1

MTVTYTARVANARFGGFSQLLLLWRGSIYKLLWRELLCFLGFYMALSAAYRFVLTEGQKR
YFEKLVIYCDQYASLIPVSFVLGFYVTLVVNRWWSQYLCMPLPDALMCVVAGTVHGRDDR
GRLYRRTLMRYAGLSAVLILRSVSTAVFKRFPTIDHVVEAGFMTREERKKFENLNSSYNK
YWVPCVWFSNLAAQARREGRIRDNSALKLLLEELNVFRGKCGMLFHYDWISVPLVYTQVV
TIALYSYFLACLIGRQFLDPAQGYKDHDLDLCVPIFTLLQFFFYAGWLKVAEQLINPFGE
DDDDFETNFLIDRNFQVSMLAVDEMYDDLAVLEKDLYWDAAEARAPYTAATVFQLRQPSF
QGSTFDITLAKEDMQFQRLDGLDGPMGEAPGDFLQRLLPAGAGMVAGGPLGRRLSFLLRK
NSCVSEASTGASCSCAVVPEGAAPECSCGDPLLDPGLPEPEAPPPAGPEPLTLIPGPVEP
FSIVTMPGPRGPAPPWLPSPIGEEEENLA

• Bestrophin (PF01062 )

• None

• 26-46 71-91 179-199 271-291

ATGACCGTCACCTACACAGCCCGAGTGGCGAACGCCCGCTTCGGTGGCTTCTCCCAGCTG
CTGCTACTGTGGCGTGGGAGCATCTACAAACTCCTGTGGCGAGAGCTGCTCTGCTTCCTT
GGGTTCTACATGGCGCTGAGTGCTGCCTACCGCTTTGTGCTGACCGAAGGGCAGAAGCGC
TACTTCGAGAAGCTTGTGATTTATTGTGACCAGTATGCCAGCCTCATCCCTGTCTCCTTC
GTGCTTGGCTTTTATGTGACGCTGGTGGTGAACCGCTGGTGGAGCCAGTACCTATGCATG
CCGCTGCCCGACGCGCTCATGTGCGTGGTGGCGGGCACCGTGCACGGACGCGACGACCGC
GGCCGCCTCTACCGGCGCACACTCATGCGCTACGCAGGGCTCTCGGCCGTGCTCATCCTG
CGCTCCGTCAGCACCGCGGTGTTCAAGCGCTTCCCCACCATAGACCACGTGGTGGAGGCT
GGGTTTATGACCCGCGAGGAGCGCAAGAAGTTTGAAAACCTGAACTCATCCTACAACAAG
TACTGGGTGCCCTGCGTCTGGTTCTCCAACCTGGCGGCACAGGCCCGACGCGAGGGCCGC
ATCCGCGACAACAGCGCCCTTAAGCTGCTGCTCGAGGAGCTGAATGTTTTTCGGGGCAAA
TGTGGAATGCTCTTTCACTATGACTGGATTAGCGTACCCCTCGTGTACACGCAGGTGGTG
ACCATCGCACTGTACAGCTACTTCCTGGCTTGCCTCATTGGTCGCCAGTTCCTGGACCCG
GCTCAGGGTTACAAAGACCACGACCTAGACCTGTGTGTGCCCATCTTCACCCTCTTGCAG
TTCTTCTTCTACGCCGGCTGGCTCAAGGTAGCTGAGCAGCTCATCAACCCCTTCGGAGAG
GACGATGATGACTTTGAGACCAACTTTCTGATCGATAGAAACTTCCAGGTGTCCATGCTG
GCAGTGGACGAGATGTATGATGACCTGGCTGTGCTGGAGAAGGACTTGTACTGGGATGCA
GCCGAGGCTCGCGCCCCATACACAGCGGCTACTGTCTTCCAGCTGCGGCAGCCTTCCTTC
CAGGGCTCCACCTTTGACATCACGCTGGCCAAAGAAGACATGCAGTTCCAGCGGCTGGAC
GGCTTGGATGGACCGATGGGAGAGGCGCCCGGCGACTTCCTGCAGCGCCTCCTGCCGGCG
GGCGCGGGCATGGTCGCGGGAGGCCCGCTGGGCCGGCGCCTGTCCTTTCTACTCCGCAAG
AACAGCTGCGTGTCGGAGGCGTCTACTGGGGCCAGCTGCTCATGCGCGGTTGTCCCCGAA
GGCGCGGCCCCGGAGTGCAGCTGCGGGGACCCGCTGCTCGACCCCGGCCTGCCGGAGCCC
GAGGCCCCGCCCCCTGCGGGTCCCGAACCGCTTACCCTCATCCCTGGGCCTGTCGAGCCC
TTCAGCATCGTGACCATGCCCGGGCCCCGGGGTCCGGCGCCACCCTGGCTGCCCAGCCCT
ATTGGCGAGGAGGAGGAGAATCTGGCCTGA

1. Stohr H, Marquardt A, Nanda I, Schmid M, Weber BH: Three novel human VMD2-like genes are members of the evolutionary highly conserved RFP-TM family. Eur J Hum Genet. 2002 Apr;10(4):281-4. [PubMed ]
2. Tsunenari T, Sun H, Williams J, Cahill H, Smallwood P, Yau KW, Nathans J: Structure-function analysis of the bestrophin family of anion channels. J Biol Chem. 2003 Oct 17;278(42):41114-25. Epub 2003 Aug 7. [PubMed ]
3. Sun H, Tsunenari T, Yau KW, Nathans J: The vitelliform macular dystrophy protein defines a new family of chloride channels. Proc Natl Acad Sci U S A. 2002 Mar 19;99(6):4008-13. [PubMed ]

1. Vitelliform macular dystrophy 2-like protein 3

MTVTYSSKVANATFFGFHRLLLKWRGSIYKLLYREFIVFAVLYTAISLVYRLLLTGVQKR
YFEKLSIYCDRYAEQIPVTFVLGFYVTLVVNRWWNQFVNLPWPDRLMFLISSSVHGSDEH
GRLLRRTLMRYVNLTSLLIFRSVSTAVYKRFPTMDHVVEAGFMTTDERKLFNHLKSPHLK
YWVPFIWFGNLATKARNEGRIRDSVDLQSLMTEMNRYRSWCSLLFGYDWVGIPLVYTQVV
TLAVYTFFFACLIGRQFLDPTKGYAGHDLDLYIPIFTLLQFFFYAGWLKVAEQLINPFGE
DDDDFETNWCIDRNLQVSLLAVDEMHMSLPKMKKDIYWDDSAARPPYTLAAADYCIPSFL
GSTVQMGLSGSDFPDEEWLWDYEKHGHRHSMIRRVKRFLSAHEHPSSPRRRSYRRQTSDS
SMFLPRDDLSPARDLLDVPSRNPPRASPTWKKSCFPEGSPTLHFSMGELSTIRETSQTST
LQSLTPQSSVRTSPIKMPLVPEVLITAAEAPVPTSGGYHHDSATSILSSEFTGVQPSKTE
QQQGPMGSILSPSEKETPPGGPSPQTVSASAEENIFNCEEDPGDTFLKRWSLPGFLGSSH
TSLGNLSPDPMSSQPALLIDTETSSEISGINIVAGSRVSSDMLYLMENLDTKETDIIELN
KETEESPK

• Bestrophin (PF01062 )

• None

• 26-46 71-91 179-199 271-291

ATGACTGTCACTTACTCCAGTAAAGTAGCAAATGCAACTTTTTTTGGATTTCATAGGTTA
CTCCTCAAGTGGAGAGGCAGCATCTACAAACTACTGTACAGGGAATTTATTGTTTTTGCT
GTTCTTTATACAGCAATAAGTTTGGTGTACAGATTGTTACTTACAGGAGTCCAAAAACGT
TACTTTGAAAAATTATCAATTTACTGTGACAGATATGCTGAACAAATTCCAGTAACCTTT
GTGCTTGGGTTTTATGTTACTCTGGTAGTGAACCGATGGTGGAACCAGTTTGTGAATTTG
CCCTGGCCAGACAGGCTAATGTTCCTCATCTCTAGCAGTGTTCACGGAAGCGACGAGCAC
GGGCGCCTGCTTAGAAGGACGCTGATGCGCTACGTCAATCTCACCTCCCTGCTCATCTTT
CGCTCGGTGAGCACTGCTGTGTACAAAAGATTTCCCACAATGGACCACGTGGTTGAAGCA
GGTTTTATGACAACAGATGAAAGGAAATTATTCAACCACCTCAAGTCTCCTCATCTGAAA
TATTGGGTTCCATTCATCTGGTTTGGAAATCTTGCAACTAAAGCCCGGAATGAAGGTAGA
ATCAGAGACAGTGTTGATCTGCAATCATTGATGACTGAAATGAATCGATACCGCTCTTGG
TGCAGCCTCTTATTCGGTTATGACTGGGTTGGGATTCCGCTGGTTTACACCCAGGTTGTC
ACTCTTGCTGTCTATACCTTCTTCTTTGCGTGCCTGATTGGACGCCAGTTTTTGGATCCC
ACCAAAGGCTACGCAGGGCATGACTTGGATCTTTACATTCCCATCTTCACCCTCCTACAA
TTCTTCTTCTATGCAGGATGGCTTAAGGTAGCAGAGCAGCTTATCAACCCTTTTGGAGAA
GATGATGATGATTTTGAAACTAACTGGTGCATTGACAGAAATTTGCAGGTCTCTCTTTTA
GCTGTGGACGAAATGCACATGAGCTTACCCAAGATGAAGAAGGACATTTACTGGGACGAT
TCTGCTGCTCGCCCACCATACACATTGGCAGCTGCTGACTACTGCATACCCTCATTTCTG
GGGTCAACAGTCCAGATGGGGAAACAGATGCCTAAGAATGAGTGGAAGATGGAAGATATA
AAAATCCCACTCCCTCAGCCTCAATTCCAGTGTGCTAAGAGTGATCCTGGTGGTTAA

1. Stohr H, Marquardt A, Nanda I, Schmid M, Weber BH: Three novel human VMD2-like genes are members of the evolutionary highly conserved RFP-TM family. Eur J Hum Genet. 2002 Apr;10(4):281-4. [PubMed ]
2. Tsunenari T, Sun H, Williams J, Cahill H, Smallwood P, Yau KW, Nathans J: Structure-function analysis of the bestrophin family of anion channels. J Biol Chem. 2003 Oct 17;278(42):41114-25. Epub 2003 Aug 7. [PubMed ]

1. Vitelliform macular dystrophy 2-like protein 2

MTVSYTLKVAEARFGGFSGLLLRWRGSIYKLLYKEFLLFGALYAVLSITYRLLLTQEQRY
VYAQVARYCNRSADLIPLSFVLGFYVTLVVNRWWSQYTSIPLPDQLMCVISASVHGVDQR
GRLLRRTLIRYANLASVLVLRSVSTRVLKRFPTMEHVVDAGFMSQEERKKFESLKSDFNK
YWVPCVWFTNLAAQARRDGRIRDDIALCLLLEELNKYRAKCSMLFHYDWISIPLVYTQVV
TIAVYSFFALSLVGRQFVEPEAGAAKPQKLLKPGQEPAPALGDPDMYVPLTTLLQFFFYA
GWLKVAEQIINPFGEDDDDFETNQLIDRNLQVSLLSVDEMYQNLPPAEKDQYWDEDQPQP
PYTVATAAESLRPSFLGSTFNLRMSDDPEQSLQVEASPGSGRPAPAAQTPLLGRFLGVGA
PSPAISLRNFGRVRGTPRPPHLLRFRAEEGGDPEAAARIEEESAESGDEALEP

• Bestrophin (PF01062 )

• None

• 26-46 71-91 179-199 286-306

ATGACGGTTTCATACACTCTCAAAGTGGCGGAGGCCCGCTTCGGAGGTTTCTCTGGCCTG
CTTCTCCGCTGGAGGGGAAGCATCTACAAGCTCCTCTACAAGGAATTCCTCCTCTTTGGG
GCCTTGTACGCTGTGCTTAGCATCACCTACCGGCTGCTGCTGACCCAGGAGCAGAGGTAC
GTGTATGCTCAGGTGGCCCGGTACTGCAACCGCTCAGCAGACCTCATTCCCTTGTCCTTT
GTATTGGGTTTCTATGTGACTCTCGTGGTGAACCGCTGGTGGTCCCAGTACACAAGCATC
CCGCTGCCAGACCAGCTGATGTGCGTCATCTCGGCTAGCGTGCACGGCGTGGACCAGCGG
GGCCGCCTGCTGCGCCGCACCCTCATCCGCTACGCGAACCTGGCGTCCGTGCTGGTGCTG
CGCTCGGTCAGCACCCGCGTGCTTAAGCGCTTCCCCACCATGGAGCACGTGGTGGACGCA
GGTTTCATGTCCCAGGAAGAGAGGAAAAAGTTTGAGAGCCTGAAATCCGACTTCAACAAG
TACTGGGTCCCCTGCGTCTGGTTCACCAACCTGGCGGCCCAGGCCCGGAGGGACGGGCGA
ATACGTGACGATATCGCTCTCTGTCTACTTTTGGAAGAGCTGAACAAGTACCGAGCCAAG
TGCAGCATGCTATTCCACTATGACTGGATCAGCATCCCCCTCGTCTACACCCAAGTGGTG
ACCATAGCCGTCTACTCTTTCTTTGCCCTCTCCCTGGTTGGCCGCCAGTTTGTGGAGCCA
GAGGCAGGGGCTGCCAAACCTCAGAAGCTTCTGAAGCCAGGCCAGGAGCCAGCCCCAGCC
CTGGGAGACCCGGACATGTACGTGCCTCTCACCACTCTGCTGCAGTTCTTCTTCTATGCT
GGCTGGCTCAAGGTGGCTGAACAGATCATCAACCCATTTGGTGAGGATGATGACGACTTT
GAGACAAATCAGCTCATAGACCGCAACTTGCAGGTGTCCCTGCTATCCGTGGACGAAATG
TACCAGAACCTTCCCCCCGCTGAGAAGGACCAGTACTGGGATGAGGACCAGCCGCAGCCA
CCCTACACTGTGGCCACGGCGGCCGAGTCTCTGCGGCCCTCATTCCTGGGCTCCACCTTC
AACCTGCGCATGAGCGACGACCCTGAGCAGAGCCTGCAGGTGGAGGCGTCCCCCGGATCT
GGTCGGCCCGCGCCCGCCGCGCAGACCCCGTTGCTCGGCCGCTTCCTGGGCGTAGGGGCG
CCCTCCCCGGCCATCAGCCTCCGGAACTTCGGCCGCGTGCGAGGCACCCCCCGCCCCCCG
CATCTGCTGCGCTTCCGGGCGGAGGAGGGCGGCGACCCCGAGGCCGCAGCCCGCATCGAG
GAGGAATCGGCGGAGTCCGGGGACGAGGCCCTGGAGCCCTGA

1. Stohr H, Marquardt A, Nanda I, Schmid M, Weber BH: Three novel human VMD2-like genes are members of the evolutionary highly conserved RFP-TM family. Eur J Hum Genet. 2002 Apr;10(4):281-4. [PubMed ]
2. Tsunenari T, Sun H, Williams J, Cahill H, Smallwood P, Yau KW, Nathans J: Structure-function analysis of the bestrophin family of anion channels. J Biol Chem. 2003 Oct 17;278(42):41114-25. Epub 2003 Aug 7. [PubMed ]

MRLDLASLMSAPKSLGSAFKSWRLDKAPSPQHTFPSTSIPGMAFALLASVPPVFGLYTSF
FPVLIYSLLGTGRHLSTGTFAILSLMTGSAVERLVPEPLVGNLSGIEKEQLDAQRVGVAA
AVAFGSGALMLGMFVLQLGVLSTFLSEPVVKALTSGAALHVLLSQLPSLLGLSLPRQIGC
FSLFKTLASLLTALPRSSPAELTISALSLALLVPVKELNVRFRDRLPTPIPGEVVLVLLA
SVLCFTSSVDTRYQVQIVGLLPGGFPQPLLPNLAELPRILADSLPIALVSFAVSASLASI
HADKYSYTIDSNQEFLAHGASNLISSLFSCFPNSATLATTNLLVDAGGKTQLAGLFSCTV
VLSVLLWLGPFFYYLPKAVLACINISSMRQVFCQMQELPQLWHISRVDFLLQVPGLCILS
YPTPLYFGTRGQFRCNLEWHLGLGEGEKETSKPDGPMVAVAEPVRVVVLDFSGVTFADAA
GAREVVQVRERLASRCRDARIRLLLAQCNALVQGTLTRVGLLDRVTPDQLFVSVQDAAAY
ALGSLLRGSSTRSGSQEALGCGK

• STAS (PF01740 )
• Sulfate_transp (PF00916 )

• None

• None

ATGAGGCTTGATTTAGCATCCTTGATGTCAGCTCCTAAGAGTCTGGGAAGTGCATTTAAG
TCCTGGAGGTTGGACAAGGCCCCCTCCCCACAGCACACCTTTCCATCCACTTCTATCCCA
GGCATGGCTTTTGCTCTCCTGGCCTCCGTGCCCCCGGTGTTTGGACTCTACACTTCTTTC
TTCCCCGTCCTCATCTACAGCTTGCTAGGTACTGGGAGACACCTGTCCACAGGAACTTTC
GCCATACTCAGCCTCATGACAGGCTCGGCCGTCGAGCGGCTGGTGCCGGAACCCCTCGTG
GGGAATCTGAGCGGAATCGAGAAGGAGCAGCTGGACGCTCAACGGGTTGGGGTAGCCGCG
GCCGTGGCCTTCGGGAGCGGGGCGTTGATGCTGGGGATGTTCGTGCTGCAGCTCGGCGTC
TTGTCCACCTTTTTGTCCGAGCCTGTGGTCAAGGCGCTGACCAGCGGGGCCGCGCTGCAC
GTGCTCTTGTCCCAGCTGCCGAGCCTCTTGGGGTTGTCCCTCCCGCGCCAGATCGGCTGC
TTCTCTCTCTTCAAGACGCTGGCCTCCTTGCTGACTGCGCTGCCTCGGAGCAGTCCGGCC
GAACTGACCATCTCCGCGCTCAGCCTGGCGCTGCTCGTGCCGGTCAAGGAATTGAACGTG
AGATTCCGAGACCGGCTACCCACGCCGATCCCGGGGGAAGTCGTCTTGGTGCTTCTGGCC
TCCGTGCTCTGCTTCACCTCTTCTGTGGACACAAGATACCAAGTCCAGATAGTGGGGCTG
TTGCCTGGAGGATTTCCCCAACCCCTCCTCCCCAACCTGGCTGAGCTGCCCAGGATTCTG
GCTGACTCGCTGCCCATTGCACTGGTTAGTTTTGCGGTGTCTGCCTCCCTGGCCTCCATC
CATGCAGACAAGTATAGCTACACTATTGACTCCAACCAGGAGTTCCTGGCACATGGTGCC
TCCAACCTCATCTCCTCCCTCTTCTCTTGCTTTCCCAACTCGGCTACGCTGGCCACCACC
AATCTACTGGTGGATGCTGGTGGGAAAACACAGCTGGCAGGCCTCTTCTCCTGCACAGTG
GTCCTGTCGGTGCTGCTGTGGCTGGGGCCCTTCTTTTACTATCTGCCCAAGGCTGTCCTG
GCTTGCATCAACATCTCCAGCATGCGCCAGGTGTTCTGCCAGATGCAGGAACTTCCACAA
CTATGGCACATCAGCCGAGTGGACTTTCTCCTCCAGGTCCCGGGGCTCTGCATCCTGAGC
TATCCAACACCACTGTACTTTGGGACCCGTGGGCAGTTTCGCTGCAACCTGGAGTGGCAC
CTGGGGCTCGGAGAAGGAGAAAAGGAGACTTCAAAGCCAGATGGCCCAATGGTTGCAGTT
GCTGAGCCTGTCAGGGTGGTGGTCCTAGACTTCAGTGGTGTCACCTTTGCAGATGCTGCT
GGGGCCAGAGAAGTGGTGCAGGTGAGGGAGAGGCTGGCCAGCCGATGTCGAGATGCTAGG
ATCCGCCTCCTCCTGGCTCAGTGTAATGCCTTGGTGCAGGGGACACTGACCCGGGTAGGA
CTCCTGGACAGGGTGACTCCAGATCAGCTGTTTGTGAGTGTGCAGGATGCAGCTGCTTAT
GCCCTGGGGAGCCTGTTAAGGGGCAGTAGCACCAGGAGCGGGAGCCAGGAGGCACTGGGC
TGCGGCAAGTGA

1. Solute carrier family 26 member 5

MDHAEENEILAATQRYYVERPIFSHPVLQERLHTKDKVPDSIADKLKQAFTCTPKKIRNI
IYMFLPITKWLPAYKFKEYVLGDLVSGISTGVLQLPQGLAFAMLAAVPPIFGLYSSFYPV
IMYCFLGTSRHISIGPFAVISLMIGGVAVRLVPDDIVIPGGVNATNGTEARDALRVKVAM
SVTLLSGIIQFCLGVCRFGFVAIYLTEPLVRGFTTAAAVHVFTSMLKYLFGVKTKRYSGI
FSVVYSTVAVLQNVKNLNVCSLGVGLMVFGLLLGGKEFNERFKEKLPAPIPLEFFAVVMG
TGISAGFNLKESYNVDVVGTLPLGLLPPANPDTSLFHLVYVDAIAIAIVGFSVTISMAKT
LANKHGYQVDGNQELIALGLCNSIGSLFQTFSISCSLSRSLVQEGTGGKTQLAGCLASLM
ILLVILATGFLFESLPQAVLSAIVIVNLKGMFMQFSDLPFFWRTSKIELTIWLTTFVSSL
FLGLDYGLITAVIIALLTVIYRTQSPSYKVLGKLPETDVYIDIDAYEEVKEIPGIKIFQI
NAPIYYANSDLYSNALKRKTGVNPAVIMGARRKAMRKYAKEVGNANMANATVVKADAEVD
GEDATKPEEEDGEVKYPPIVIKSTFPEEMQRFMPPGDNVHTVILDFTQVNFIDSVGVKTL
AGIVKEYGDVGIYVYLAGCSAQVVNDLTRNRFFENPALWELLFHSIHDAVLGSQLREALA
EQEASAPPSQEDLEPNATPATPEA

• STAS (PF01740 )
• Sulfate_transp (PF00916 )

• None

• 80-100 103-123 132-152 184-204 212-232 254-274 287-307 335-355 375-395 412-432 442-462 480-500

ATGGATCATGCTGAAGAAAATGAAATCCTTGCAGCAACCCAGAGGTACTATGTGGAAAGG
CCTATCTTTAGTCATCCGGTCCTCCAGGAAAGACTACACACAAAGGACAAGGTTCCTGAT
TCCATTGCGGATAAGCTGAAACAGGCATTCACATGTACTCCTAAAAAAATAAGAAATATC
ATTTATATGTTCCTACCCATAACTAAATGGCTGCCAGCATACAAATTCAAGGAATATGTG
TTGGGTGACTTGGTCTCAGGCATAAGCACAGGGGTGCTTCAGCTTCCTCAAGGCTTAGCC
TTTGCAATGCTGGCAGCTGTGCCTCCAATATTTGGCCTGTACTCTTCATTTTACCCTGTT
ATCATGTATTGTTTTCTTGGAACCTCCAGACACATATCCATAGGTCCTTTTGCTGTTATT
AGCCTGATGATTGGTGGTGTAGCTGTTCGATTAGTACCAGATGATATAGTCATTCCAGGA
GGAGTAAATGCAACCAATGGCACAGAGGCCAGAGATGCCTTGAGAGTGAAAGTCGCCATG
TCTGTGACCTTACTTTCAGGAATCATTCAGTTTTGCCTAGGTGTCTGTAGGTTTGGATTT
GTGGCCATATATCTCACAGAGCCTCTGGTCCGTGGGTTTACCACCGCAGCAGCTGTGCAT
GTCTTCACCTCCATGTTAAAATATCTGTTTGGAGTTAAAACAAAGCGGTACAGTGGAATC
TTTTCCGTGGTGTATAGTACAGTTGCTGTGTTGCAGAATGTTAAAAACCTCAACGTGTGT
TCCCTAGGCGTCGGGCTGATGGTTTTTGGTTTGCTGTTGGGTGGCAAGGAGTTTAATGAG
AGATTTAAAGAGAAATTGCCGGCGCCTATTCCTTTAGAGTTCTTTGCGGTCGTAATGGGA
ACTGGCATTTCAGCTGGGTTTAACTTGAAAGAATCATACAATGTGGATGTCGTTGGAACA
CTTCCTCTAGGGCTGCTACCTCCAGCCAATCCGGACACCAGCCTCTTCCACCTTGTGTAC
GTAGATGCCATTGCCATAGCCATCGTTGGATTTTCAGTGACCATCTCCATGGCCAAGACC
TTAGCAAATAAACATGGCTACCAGGTTGACGGCAATCAGGAGCTCATTGCCCTGGGACTG
TGCAATTCCATTGGCTCACTCTTCCAGACCTTTTCAATTTCATGCTCCTTGTCTCGAAGC
CTTGTTCAGGAGGGAACCGGTGGGAAGACACAGCTTGCAGGTTGTTTGGCCTCATTAATG
ATTCTGCTGGTCATATTAGCAACTGGATTCCTCTTTGAATCATTGCCCCAGGCTGTGCTG
TCGGCCATTGTGATTGTCAACCTGAAGGGAATGTTTATGCAGTTCTCAGATCTCCCCTTT
TTCTGGAGAACCAGCAAAATAGAGCTGACCATCTGGCTTACCACTTTTGTGTCCTCCTTG
TTCCTGGGATTGGACTATGGTTTGATCACTGCTGTGATCATTGCTCTGCTGACTGTGATT
TACAGAACACAGAGTCCAAGCTACAAAGTCCTTGGAAAGCTTCCTGAAACTGATGTGTAT
ATTGATATAGACGCATATGAGGAGGTGAAAGAAATTCCTGGAATAAAAATATTTCAAATA
AATGCACCAATTTACTATGCAAATAGCGACTTGTATAGCAATGCATTAAAACGAAAGACT
GGAGTGAACCCAGCAGTCATCATGGGAGCAAGGAGAAAGGCCATGCGGAAGTACGCTAAG
GAAGTCGGAAATGCAAATATGGCCAACGCAACTGTTGTCAAAGCAGATGCAGAAGTAGAT
GGAGAGGATGCTACCAAGCCTGAAGAAGAGGATGGTGAAGTAAAATATCCCCCAATAGTG
ATCAAAAGCACATTTCCTGAGGAAATGCAAAGATTTATGCCCCCAGGGGATAACGTCCAC
ACTGTCATTTTGGATTTCACTCAAGTCAATTTTATTGATTCTGTTGGAGTGAAAACTCTG
GCAGGGATTGTAAAAGAATATGGAGACGTCGGTATATATGTATACTTAGCAGGATGCAGT
GCACAAGTTGTGAATGACCTCACTCGGAATAGATTTTTTGAAAATCCTGCCCTATGGGAG
CTGCTGTTCCACAGCATTCATGATGCAGTTTTAGGCAGCCAACTTAGAGAGGCACTTGCT
GAACAGGAAGCCTCGGCTCCCCCTTCCCAGGAGGACTTGGAGCCCAATGCCACTCCTGCC
ACTCCTGAGGCATAG

1. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed ]

1. Na(+/H(+exchanger 10
2. Sperm-specific Na(+/H(+exchanger
3. sNHE
4. Solute carrier family 10 member 10

MAGIFKEFFFSTEDLPEVILTLSLISSIGAFLNRHLEDFPIPVPVILFLLGCSFEVLSFT
SSQVQRYANAIQWMSPDLFFRIFTPVVFFTTAFDMDTYMLQKLFWQILLISIPGFLVNYI
LVLWHLASVNQLLLKPTQWLLFSAILVSSDPMLTAAAIRDLGLSRSLISLINGESLMTSV
ISLITFTSIMDFDQRLQSKRNHTLAEEIVGGICSYIIASFLFGILSSKLIQFWMSTVFGD
DVNHISLIFSILYLIFYICELVGMSGIFTLAIVGLLLNSTSFKAAIEETLLLEFWTFLSR
IAFLMVFTFFGLLIPAHTYLYIEFVDIYYSLNIYLTLIVLRFLTLLLISPVLSRVGHEFS
WRWIFIMVCSEMKGMPNINMALLLAYSDLYFGSDKEKSQILFHGVLVCLITLVVNRFILP
VAVTILGLRDATSTKYKSVCCTFQHFQELTKSAASALKFDKDLANADWNMIEKAITLENP
YMLNEEETTEHQKVKCPHCNKEIDEIFNTEAMELANRRLLSAQIASYQRQYRNEILSQSA
VQVLVGAAESFGEKKGKCMSLDTIKNYSESQKTVTFARKLLLNWVYNTRKEKEGPSKYFF
FRICHTIVFTEEFEHVGYLVILMNIFPFIISWISQLNVIYHSELKHTNYCFLTLYILEAL
LKIAAMRKDFFSHAWNIFELAITLIGILHVILIEIDTIKYIFNETEVIVFIKVVQFFRIL
RIFKLIAPKLLQIIDKRMSHQKTFWYGILKGYVQGEADIMTIIDQITSSKQIKQMLLKQV
IRNMEHAIKELGYLEYDHPEIAVTVKTKEEINVMLNMATEILKAFGLKGIISKTEGAGIN
KLIMAKKKEVLDSQSIIRPLTVEEVLYHIPWLDKNKDYINFIQEKAKVVTFDCGNDIFEE
GDEPKGIYIIISGMVKLEKSKPGLGIDQMVESKEKDFPIIDTDYMLSGEIIGEINCLTNE
PMKYSATCKTVVETCFIPKTHLYDAFEQCSPLIKQKMWLKLGLAITARKIREHLSYEDWN
YNMQLKLSNIYVVDIPMSTKTDIYDENLIYVILIHGAVEDCLLRKTYRAPFLIPITCHQI
QSIEDFTKVVIIQTPINMKTFRRNIRKFVPKHKSYLTPGLIGSVGTLEEGIQEERNVKED
GAHSAATARSPQPCSLLGTKFNCKESPRINLRKVRKE

• cNMP_binding (PF00027 )
• Ion_trans (PF00520 )

• 1-353

• 8-28 39-59 73-93 103-123 138-158 167-187 204-224 248-268 301-321 333-353 364-384 405-425 613-633 646-666 675-695 707-727

ATGGCTGGAATATTTAAGGAGTTTTTTTTCAGTACTGAGGACCTCCCTGAAGTCATTCTA
ACATTGTCTTTGATCAGCTCCATTGGAGCATTTTTGAACCGGCACTTGGAAGACTTTCCA
ATTCCTGTCCCTGTGATATTATTTTTACTTGGATGCAGTTTTGAAGTATTAAGCTTTACA
TCTTCACAGGTCCAAAGATACGCAAACGCCATACAATGGATAAGTCCAGACTTATTTTTT
CGTATATTTACACCAGTAGTTTTCTTTACTACTGCATTTGACATGGATACGTACATGCTT
CAAAAGTTATTTTGGCAGATACTTTTAATTTCAATTCCCGGCTTTTTGGTTAATTATATC
TTAGTTCTTTGGCATCTGGCATCTGTAAATCAATTACTTTTGAAGCCTACCCAATGGTTA
TTATTTTCAGCTATCCTTGTGAGTTCAGATCCCATGCTAACCGCAGCTGCTGTAAGAGAC
CTTGGGCTTTCTAGAAGCCTCATCAGTTTAATTAATGGAGAAAGTCTGATGACCTCTGTT
ATATCATTAATTACATTTACTAGTATTATGGATTTTGACCAAAGACTACAAAGTAAAAGA
AACCATACCTTAGCTGAAGAGATCGTGGGTGGAATTTGTTCATATATTATAGCAAGTTTC
TTGTTTGGAATTCTAAGTTCAAAACTGATTCAATTTTGGATGTCAACTGTTTTTGGTGAT
GATGTCAATCATATAAGTCTCATCTTTTCAATTCTGTATCTCATCTTTTATATTTGTGAG
TTAGTTGGAATGTCAGGAATATTTACTCTGGCCATTGTGGGACTTCTTTTAAATTCTACA
AGTTTTAAAGCAGCAGTTGAAGAAACACTTCTTCTTGAATTCTGGACTTTTCTATCACGT
ATTGCTTTTCTCATGGTGTTTACTTTCTTTGGACTTCTAATTCCTGCACATACATATTTG
TATATAGAATTTGTTGATATATACTATTCATTAAATATCTACTTAACATTGATTGTTTTA
AGATTTCTGACCCTTCTTTTAATGAGCCCTGTTTTGTCTCGAGTTGGTCATGAGTTCAGT
TGGCGCTGGGTATTCATAATGGTCTGTAGTGAAATGAAAGGGATGCCTAATATAAACATG
GCCCTTCTGCTTGCCTACTCTGATCTTTATTTTGGATCTGACAAAGAAAAATCTCAAATA
TTATTTCATGGAGTGTTAGTATGCCTAATAACCCTTGTTGTCAATAGATTTATTTTGCCA
GTGGCAGTTGCTATACTAGGTCTTCGTGATGCCACATCAACAAAATATAAATCGGTTTGT
TGCACATTTCAACACTTTCAAGAGCTAACCAAGTCTGCAGCCTCTGCCCTTAAATTTGAC
AAAGATCTTGCTAATGCTGATTGGAACATGATTGAGAAAGCAATTACACTTGAAAACCCA
TACATGTTGAACGAAGAAGAAACAACAGAACATCAGAAGGTGAAATGTCCACACTGTAAC
AAGGAAATAGATGAGATCTTTAACACTGAAGCAATGGAGCTGGCCAACAGGCGTCTCTTG
TCAGCACAAATAGCAAGCTACCAGAGACAATACAGGAATGAGATTCTGTCCCAGAGTGCT
GTCCAGGTGTTGGTTGGTGCAGCAGAAAGTTTTGGTGAGAAGAAGGGAAAATGTATGAGT
CTTGATACAATAAAGAATTATTCTGAAAGCCAAAAAACAGTTACCTTTGCTAGAAAACTA
CTACTTAATTGGGTGTATAATACCAGAAAGGAAAAAGAGGGCCCATCAAAATACTTCTTT
TTTCGTATATGCCATACAATAGTATTTACTGAGGAATTTGAACATGTTGGATACCTTGTG
ATATTAATGAATATATTTCCCTTTATAATCTCTTGGATATCCCAGTTAAATGTAATCTAC
CACAGCGAATTAAAACACACTAACTACTGTTTTCTTACACTTTATATTCTAGAGGCACTA
CTTAAGATAGCAGCAATGAGGAAGGACTTTTTTTCACATGCCTGGAACATATTCGAGTTA
GCAATTACATTAATTGGCATCTTACATGTAATACTTATTGAAATAGACACCATTAAGTAT
ATTTTTAATGAGATTGAAGTAATAGTCTTTATAAAAGTTGTTCAATTTTTTCGTATACTA
CGCATTTTCAAGCTCATAGCACCAAAGTTGCTGAAAATAATAGATAAAAGAATGAGTCAT
CAGAAGACCTTTTGGTATGGAATACTAAAAGGCTATGTCCAAGGCGAAGCAGACATAATG
ACCATAATTGATCAGATTACAATTTCTAAACAGATTAAACAGATGTTATTAAAGCAAGTG
ATAAGGAATATGGACCATGCTACAAAAGAGCTAGGCTACTTAGAGTATGATCACCCAGAA
ATTGCTGTCACTGTGAAAACAAAGGAAGAAATTAATGTTATGCTCAATATGGCTACAGAA
ATTCTTAAGGCTTTCAGCTTAAAAGGAATTATTAGTAAAACTGAAGGTGCTGGAATTAAT
AAGTTAATCATGGCCAAAAAGAAAGAGGTGCTTGATTCTCAATCTATTATCAGGCCTCTT
ACTGTTGAAGAAGTTCTATATCATATTCCGTGGCTAGATAAAAACAAAGATTATATAAAC
TTCATTCAGGAAAAAGCCAAAGTTGTAACATTTGATTGTGGAAATGATATATTTGAAGAA
GGTGATGAGCCCAAAGGAATCTATATCATTATTTCAGGCATGGTAAAGCTTGAAAAATCA
AAGCCAGGTTTAGGGATTGATCAAATGGTGGAGTCAAAGGAGAAAGATTTTCCGATAATT
GACACAGACTATATGCTCAGTGGAGAAATAATAGGAGAGATAAACTGCTTAACTAATGAA
CCTATGAAATATTCTGCCACCTGCAAAACTGTAGTGGAGACATGTTTTATTCCCAAAACT
CACTTGTATGATGCTTTTGAGCAATGCTCTCCTCTCATTAAACAAAAAATGTGGCTAAAA
CTTGGACTCGCTATTACAGCCAGAAAAATCAGAGAACACTTATCTTATGAGGATTGGAAC
TACAATATGCAACTAAAGCTCTCTAATATTTATGTAGTAGATATACCAATGAGTACCAAA
ACTGATATTTATGATGAAAATCTAATCTATGTTATCCTCATACATGGAGCTGTAGAAGAT
TGTCTGTTACGAAAAACTTATAGAGCACCTTTCTTAATTCCTATAACATGCCATCAGATA
CAAAGTATTGAAGATTTCACAAAAGTAGTGATTATTCAAACTCCGATTAACATGAAAACA
TTCAGAAGGAATATTAGAAAGTTTGTTCCTAAACATAAAAGTTATCTTACACCAGGATTA
ATAGGTTCAGTTGGAACATTGGAAGAAGGCATTCAAGAAGAAAGAAATGTTAAGGAGGAT
GGAGCACACAGTGCCGCCACTGCCAGGAGTCCCCAGCCTTGCTCCCTGCTGGGGACAAAG
TTCAACTGTAAGGAGTCCCCTAGAATAAACCTAAGGAAAGTCAGGAAAGAGTAA

1. Oduru S, Campbell JL, Karri S, Hendry WJ, Khan SA, Williams SC: Gene discovery in the hamster: a comparative genomics approach for gene annotation by sequencing of hamster testis cDNAs. BMC Genomics. 2003 Jun 3;4(1):22. [PubMed ]