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2.A.31.1.1
Anion exchanger (HCO3-:Cl- antiporter; also called Band 3, transports a variety of inorganic and organic anions. Anionic phospholipids are ''flipped'' from one monolayer to the other in erythrocytes and the nephron). Mutations cause Southeast Asian ovalocytosis (SAO) hereditary spherocytosis and distal renal tubular acidosis (dRTA) with impaired acid secretion in humans (Chu et al., 2010; Kittanakom et al., 2008; Toye et al., 2008). Activated by glycophorin A (Stewart et al., 2011). Kanadaptin (SLC4a1; Q9BWU0) has been reported to interact with kidney AE1 (Chen et al. 1998), but Kittanakom et al. 2005 could not detect this interaction. Hübner et al. 2002, 2003 reported nuclear and mitochondrial targetting of kanadaptin.  Some point mutations allow the normally electroneutral anion exchanger to catalyze Na+ and K+ conductance or induce a cation leak in the still functional anion exchanger. A structural model of the AE1 membrane spanning domain, based on the structure of Uracil-proton symporter, suggests that there is a unique transport site comprising TMSs 3-5 and 8 that may function in anion exchange and cation leak (Barneaud-Rocca et al. 2013). The spectrin-actin-based cytoskeletal network is attached to the plasma membrane through interactions with ankyrin, which binds to both spectrin and a beta-hairpin loop in the cytoplasmic domain of band 3 (Stefanovic et al. 2007). A detailed transport mechanism has been proposed: It involves an elevator-like motion of the substrate-binding domain relative to the nearly stationary dimerization domain and to the membrane plane (Ficici et al. 2017). The structure-function relationships of band 3 have been reviewed (Abbas et al. 2018).

Accession Number:P02730
Protein Name:B3AT aka SLC4A1 aka AE1 aka EPB3 aka DI
Length:911
Molecular Weight:101792.00
Species:Homo sapiens (Human) [9606]
Number of TMSs:14
Location1 / Topology2 / Orientation3: Membrane1 / Multi-pass membrane protein2
Substrate anions, phospholipids

Cross database links:

Genevestigator: P02730 P02730
eggNOG: prNOG12370 NOG268067
HEGENOM: HBG355640
RefSeq: NP_000333.1   
Entrez Gene ID: 6521   
Pfam: PF07565    PF00955   
OMIM: 109270  gene+phenotype
110500  phenotype
112010  phenotype
112050  phenotype
130600  phenotype
179800  phenotype
601550  phenotype
601551  phenotype
611590  phenotype
612653  phenotype
KEGG: hsa:6521    hsa:6521   

Gene Ontology

GO:0016323 C:basolateral plasma membrane
GO:0030863 C:cortical cytoskeleton
GO:0005887 C:integral to plasma membrane
GO:0030506 F:ankyrin binding
GO:0005452 F:inorganic anion exchanger activity
GO:0043495 F:protein anchor
GO:0042803 F:protein homodimerization activity
GO:0006820 P:anion transport
GO:0006873 P:cellular ion homeostasis
GO:0030018 C:Z disc
GO:0015301 F:anion:anion antiporter activity
GO:0015108 F:chloride transmembrane transporter activity
GO:0015701 P:bicarbonate transport

References (117)

[1] “The complete amino acid sequence of the human erythrocyte membrane anion-transport protein deduced from the cDNA sequence.”  Tanner M.J.A.et.al.   3223947
[2] “Cloning and characterization of band 3, the human erythrocyte anion-exchange protein (AE1).”  Lux S.E.et.al.   2594752
[3] “Recessive distal renal tubular acidosis in Sarawak caused by AE1 mutations.”  Choo K.E.et.al.   16252102
[4] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”  The MGC Project Teamet.al.   15489334
[5] “Primary structure of the cytoplasmic domain of human erythrocyte protein band 3. Comparison with its sequence in the mouse.”  Yannoukakos D.et.al.   2790053
[6] “Amino acid sequence of the N alpha-terminal 201 residues of human erythrocyte membrane band 3.”  Kaul R.K.et.al.   6345535
[7] “Orientation of the band 3 polypeptide from human erythrocyte membranes. Identification of NH2-terminal sequence and site of carbohydrate attachment.”  Drickamer L.K.et.al.   701248
[8] “Anion exchanger 1 in human kidney and oncocytoma differs from erythroid AE1 in its NH2 terminus.”  Kollert-Jons A.et.al.   7506871
[9] “The human erythrocyte anion-transport protein. Partial amino acid sequence, conformation and a possible molecular mechanism for anion exchange.”  Brock C.J.et.al.   6615451
[10] “Anion-proton cotransport through the human red blood cell band 3 protein. Role of glutamate 681.”  Jennings M.L.et.al.   1352774
[11] “Band 3 Chur: a variant associated with band 3-deficient hereditary spherocytosis and substitution in a highly conserved position of transmembrane segment 11.”  Maillet P.et.al.   8547122
[12] “Localization of the pyridoxal phosphate binding site at the COOH-terminal region of erythrocyte band 3 protein.”  Kawano Y.et.al.   3372523
[13] “Phosphorylation sites in human erythrocyte band 3 protein.”  Yannoukakos D.et.al.   1998697
[14] “Palmitoylation of cysteine 69 from the COOH-terminal of band 3 protein in the human erythrocyte membrane. Acylation occurs in the middle of the consensus sequence of F--I-IICLAVL found in band 3 protein and G2 protein of Rift Valley fever virus.”  Okubo K.et.al.   1885574
[15] “Sequential phosphorylation of protein band 3 by Syk and Lyn tyrosine kinases in intact human erythrocytes: identification of primary and secondary phosphorylation sites.”  Brunati A.M.et.al.   10942405
[16] “Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.”  Rikova K.et.al.   18083107
[17] “Two-dimensional structure of the membrane domain of human band 3, the anion transport protein of the erythrocyte membrane.”  Wang D.N.et.al.   8508760
[18] “Three-dimensional map of the dimeric membrane domain of the human erythrocyte anion exchanger, Band 3.”  Wang D.N.et.al.   8045253
[19] “The solution structures of the first and second transmembrane-spanning segments of band 3.”  Gargaro A.R.et.al.   8168533
[20] “Solution structure of a band 3 peptide inhibitor bound to aldolase: a proposed mechanism for regulating binding by tyrosine phosphorylation.”  Schneider M.L.et.al.   8527430
[21] “Insights into tyrosine phosphorylation control of protein-protein association from the NMR structure of a band 3 peptide inhibitor bound to glyceraldehyde-3-phosphate dehydrogenase.”  Eisenmesser E.Z.et.al.   9454576
[22] “Studies on the structure of a transmembrane region and a cytoplasmic loop of the human red cell anion exchanger.”  Chambers E.J.et.al.   9765907
[23] “NMR solution structure of a cytoplasmic surface loop of the human red cell anion transporter, band 3.”  Askin D.et.al.   9709005
[24] “Human erythrocyte band 3 polymorphism (band 3 Memphis): characterization of the structural modification (Lys 56-->Glu) by protein chemistry methods.”  Yannoukakos D.et.al.   1678289
[25] “Deletion in erythrocyte band 3 gene in malaria-resistant Southeast Asian ovalocytosis.”  Jarolim P.et.al.   1722314
[26] “Band 3 Tuscaloosa: Pro-327-->Arg substitution in the cytoplasmic domain of erythrocyte band 3 protein associated with spherocytic hemolytic anemia and partial deficiency of protein 4.2.”  Jarolim P.et.al.   1378323
[27] “Basis of unique red cell membrane properties in hereditary ovalocytosis.”  Schofield A.E.et.al.   1538405
[28] “Band 3 HT, a human red-cell variant associated with acanthocytosis and increased anion transport, carries the mutation Pro-868-->Leu in the membrane domain of band 3.”  Bruce L.J.et.al.   8343110
[29] “Human erythrocyte protein 4.2 deficiency associated with hemolytic anemia and a homozygous 40 glutamic acid-->lysine substitution in the cytoplasmic domain of band 3 (band 3Montefiore).”  Rybicki A.C.et.al.   8471774
[30] “Band 3 Memphis variant II. Altered stilbene disulfonate binding and the Diego (Dia) blood group antigen are associated with the human erythrocyte band 3 mutation Pro-854-->Leu.”  Bruce L.J.et.al.   8206915
[31] “Changes in the blood group Wright antigens are associated with a mutation at amino acid 658 in human erythrocyte band 3: a site of interaction between band 3 and glycophorin A under certain conditions.”  Bruce L.J.et.al.   7812009
[32] “Mutations of conserved arginines in the membrane domain of erythroid band 3 lead to a decrease in membrane-associated band 3 and to the phenotype of hereditary spherocytosis.”  Jarolim P.et.al.   7530501
[33] “Characterization of 13 novel band 3 gene defects in hereditary spherocytosis with band 3 deficiency.”  Jarolim P.et.al.   8943874
[34] “Ankyrin-1 mutations are a major cause of dominant and recessive hereditary spherocytosis.”  Eber S.W.et.al.   8640229
[35] “Modulation of clinical expression and band 3 deficiency in hereditary spherocytosis.”  Alloisio N.et.al.   9207478
[36] “Novel band 3 variants (bands 3 Foggia, Napoli I and Napoli II) associated with hereditary spherocytosis and band 3 deficiency: status of the D38A polymorphism within the EPB3 locus.”  Miraglia del Giudice E.et.al.   9012689
[37] “Heterogenous band 3 deficiency in hereditary spherocytosis related to different band 3 gene defects.”  Dhermy D.et.al.   9233560
[38] “Familial distal renal tubular acidosis is associated with mutations in the red cell anion exchanger (Band 3, AE1) gene.”  Bruce L.J.et.al.   9312167
[39] “Blood group antigens Rb(a), Tr(a), and Wd(a) are located in the third ectoplasmic loop of erythroid band 3.”  Jarolim P.et.al.   9191821
[40] “Band 3 Tokyo: Thr837-->Ala837 substitution in erythrocyte band 3 protein associated with spherocytic hemolysis.”  Iwase S.et.al.   9973643
[41] “Characterization of seven low incidence blood group antigens carried by erythrocyte band 3 protein.”  Jarolim P.et.al.   9845551
[42] “Novel AE1 mutations in recessive distal renal tubular acidosis: loss-of-function is rescued by glycophorin A.”  Tanphaichitr V.S.et.al.   9854053
[43] “Mutations in the chloride-bicarbonate exchanger gene AE1 cause autosomal dominant but not autosomal recessive distal renal tubular acidosis.”  Karet F.E.et.al.   9600966
[44] “A Gly565-->Ala substitution in human erythroid band 3 accounts for the Wu blood group polymorphism.”  Zelinski T.et.al.   9709782
[45] “Arginine 490 is a hot spot for mutation in the band 3 gene in hereditary spherocytosis.”  Lima P.R.M.et.al.   10580570
[46] “Band 3 mutations, renal tubular acidosis and South-East Asian ovalocytosis in Malaysia and Papua New Guinea: loss of up to 95% band 3 transport in red cells.”  Bruce L.J.et.al.   10926824
[47] “Severe hereditary spherocytosis and distal renal tubular acidosis associated with the total absence of band 3.”  Ribeiro M.L.et.al.   10942416
[48] “Characteristic features of the genotype and phenotype of hereditary spherocytosis in the Japanese population.”  Yawata Y.et.al.   10745622
[49] “Trafficking and folding defects in hereditary spherocytosis mutants of the human red cell anion exchanger.”  Quilty J.A.et.al.   11208088
[50] “Amino acid substitutions in human erythroid protein band 3 account for the low-incidence antigens NFLD and BOW.”  McManus K.et.al.   10738034
[51] “An amino acid substitution in the putative second extracellular loop of RBC band 3 accounts for the Froese blood group polymorphism.”  McManus K.et.al.   11061863
[52] “Distinctive Swann blood group genotypes: molecular investigations.”  Zelinski T.et.al.   11155072
[53] “Band 3 Cape Town (E90K) causes severe hereditary spherocytosis in combination with band 3 Prague III.”  Bracher N.A.et.al.   11380459
[54] “Novel compound heterozygous SLC4A1 mutations in Thai patients with autosomal recessive distal renal tubular acidosis.”  Sritippayawan S.et.al.   15211439
[55] “A novel missense mutation in AE1 causing autosomal dominant distal renal tubular acidosis retains normal transport function but is mistargeted in polarized epithelial cells.”  Rungroj N.et.al.   14734552
[56] “Band 3Tambau: a de novo mutation in the AE1 gene associated with hereditary spherocytosis. Implications for anion exchange and insertion into the red blood cell membrane.”  Lima P.R.M.et.al.   15813913
[57] “Monovalent cation leaks in human red cells caused by single amino-acid substitutions in the transport domain of the band 3 chloride-bicarbonate exchanger, AE1.”  Bruce L.J.et.al.   16227998
[58] “The complete amino acid sequence of the human erythrocyte membrane anion-transport protein deduced from the cDNA sequence.”  Tanner M.J.A.et.al.   3223947
[59] “Cloning and characterization of band 3, the human erythrocyte anion-exchange protein (AE1).”  Lux S.E.et.al.   2594752
[60] “Recessive distal renal tubular acidosis in Sarawak caused by AE1 mutations.”  Choo K.E.et.al.   16252102
[61] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”  The MGC Project Teamet.al.   15489334
[62] “Primary structure of the cytoplasmic domain of human erythrocyte protein band 3. Comparison with its sequence in the mouse.”  Yannoukakos D.et.al.   2790053
[63] “Amino acid sequence of the N alpha-terminal 201 residues of human erythrocyte membrane band 3.”  Kaul R.K.et.al.   6345535
[64] “Orientation of the band 3 polypeptide from human erythrocyte membranes. Identification of NH2-terminal sequence and site of carbohydrate attachment.”  Drickamer L.K.et.al.   701248
[65] “Anion exchanger 1 in human kidney and oncocytoma differs from erythroid AE1 in its NH2 terminus.”  Kollert-Jons A.et.al.   7506871
[66] “A structural study of the membrane domain of band 3 by tryptic digestion. Conformational change of band 3 in situ induced by alkali treatment.”  Kang D.et.al.   1527044
[67] “The human erythrocyte anion-transport protein. Partial amino acid sequence, conformation and a possible molecular mechanism for anion exchange.”  Brock C.J.et.al.   6615451
[68] “Anion-proton cotransport through the human red blood cell band 3 protein. Role of glutamate 681.”  Jennings M.L.et.al.   1352774
[69] “Band 3 Chur: a variant associated with band 3-deficient hereditary spherocytosis and substitution in a highly conserved position of transmembrane segment 11.”  Maillet P.et.al.   8547122
[70] “Localization of the pyridoxal phosphate binding site at the COOH-terminal region of erythrocyte band 3 protein.”  Kawano Y.et.al.   3372523
[71] “Phosphorylation sites in human erythrocyte band 3 protein.”  Yannoukakos D.et.al.   1998697
[72] “Palmitoylation of cysteine 69 from the COOH-terminal of band 3 protein in the human erythrocyte membrane. Acylation occurs in the middle of the consensus sequence of F--I-IICLAVL found in band 3 protein and G2 protein of Rift Valley fever virus.”  Okubo K.et.al.   1885574
[73] “The ANK repeats of erythrocyte ankyrin form two distinct but cooperative binding sites for the erythrocyte anion exchanger.”  Michaely P.et.al.   7665627
[74] “Sequential phosphorylation of protein band 3 by Syk and Lyn tyrosine kinases in intact human erythrocytes: identification of primary and secondary phosphorylation sites.”  Brunati A.M.et.al.   10942405
[75] “Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.”  Rikova K.et.al.   18083107
[76] “Initial characterization of the human central proteome.”  Burkard T.R.et.al.   21269460
[77] “Two-dimensional structure of the membrane domain of human band 3, the anion transport protein of the erythrocyte membrane.”  Wang D.N.et.al.   8508760
[78] “Three-dimensional map of the dimeric membrane domain of the human erythrocyte anion exchanger, Band 3.”  Wang D.N.et.al.   8045253
[79] “The solution structures of the first and second transmembrane-spanning segments of band 3.”  Gargaro A.R.et.al.   8168533
[80] “Solution structure of a band 3 peptide inhibitor bound to aldolase: a proposed mechanism for regulating binding by tyrosine phosphorylation.”  Schneider M.L.et.al.   8527430
[81] “Insights into tyrosine phosphorylation control of protein-protein association from the NMR structure of a band 3 peptide inhibitor bound to glyceraldehyde-3-phosphate dehydrogenase.”  Eisenmesser E.Z.et.al.   9454576
[82] “Studies on the structure of a transmembrane region and a cytoplasmic loop of the human red cell anion exchanger.”  Chambers E.J.et.al.   9765907
[83] “NMR solution structure of a cytoplasmic surface loop of the human red cell anion transporter, band 3.”  Askin D.et.al.   9709005
[84] “Human erythrocyte band 3 polymorphism (band 3 Memphis): characterization of the structural modification (Lys 56-->Glu) by protein chemistry methods.”  Yannoukakos D.et.al.   1678289
[85] “Deletion in erythrocyte band 3 gene in malaria-resistant Southeast Asian ovalocytosis.”  Jarolim P.et.al.   1722314
[86] “Band 3 Tuscaloosa: Pro-327-->Arg substitution in the cytoplasmic domain of erythrocyte band 3 protein associated with spherocytic hemolytic anemia and partial deficiency of protein 4.2.”  Jarolim P.et.al.   1378323
[87] “Basis of unique red cell membrane properties in hereditary ovalocytosis.”  Schofield A.E.et.al.   1538405
[88] “Band 3 HT, a human red-cell variant associated with acanthocytosis and increased anion transport, carries the mutation Pro-868-->Leu in the membrane domain of band 3.”  Bruce L.J.et.al.   8343110
[89] “Human erythrocyte protein 4.2 deficiency associated with hemolytic anemia and a homozygous 40 glutamic acid-->lysine substitution in the cytoplasmic domain of band 3 (band 3Montefiore).”  Rybicki A.C.et.al.   8471774
[90] “Band 3 Memphis variant II. Altered stilbene disulfonate binding and the Diego (Dia) blood group antigen are associated with the human erythrocyte band 3 mutation Pro-854-->Leu.”  Bruce L.J.et.al.   8206915
[91] “Changes in the blood group Wright antigens are associated with a mutation at amino acid 658 in human erythrocyte band 3: a site of interaction between band 3 and glycophorin A under certain conditions.”  Bruce L.J.et.al.   7812009
[92] “Mutations of conserved arginines in the membrane domain of erythroid band 3 lead to a decrease in membrane-associated band 3 and to the phenotype of hereditary spherocytosis.”  Jarolim P.et.al.   7530501
[93] “Characterization of 13 novel band 3 gene defects in hereditary spherocytosis with band 3 deficiency.”  Jarolim P.et.al.   8943874
[94] “Ankyrin-1 mutations are a major cause of dominant and recessive hereditary spherocytosis.”  Eber S.W.et.al.   8640229
[95] “Modulation of clinical expression and band 3 deficiency in hereditary spherocytosis.”  Alloisio N.et.al.   9207478
[96] “Novel band 3 variants (bands 3 Foggia, Napoli I and Napoli II) associated with hereditary spherocytosis and band 3 deficiency: status of the D38A polymorphism within the EPB3 locus.”  Miraglia del Giudice E.et.al.   9012689
[97] “Heterogenous band 3 deficiency in hereditary spherocytosis related to different band 3 gene defects.”  Dhermy D.et.al.   9233560
[98] “Familial distal renal tubular acidosis is associated with mutations in the red cell anion exchanger (Band 3, AE1) gene.”  Bruce L.J.et.al.   9312167
[99] “Blood group antigens Rb(a), Tr(a), and Wd(a) are located in the third ectoplasmic loop of erythroid band 3.”  Jarolim P.et.al.   9191821
[100] “Band 3 Tokyo: Thr837-->Ala837 substitution in erythrocyte band 3 protein associated with spherocytic hemolysis.”  Iwase S.et.al.   9973643
[101] “Characterization of seven low incidence blood group antigens carried by erythrocyte band 3 protein.”  Jarolim P.et.al.   9845551
[102] “Novel AE1 mutations in recessive distal renal tubular acidosis: loss-of-function is rescued by glycophorin A.”  Tanphaichitr V.S.et.al.   9854053
[103] “Mutations in the chloride-bicarbonate exchanger gene AE1 cause autosomal dominant but not autosomal recessive distal renal tubular acidosis.”  Karet F.E.et.al.   9600966
[104] “A Gly565-->Ala substitution in human erythroid band 3 accounts for the Wu blood group polymorphism.”  Zelinski T.et.al.   9709782
[105] “Arginine 490 is a hot spot for mutation in the band 3 gene in hereditary spherocytosis.”  Lima P.R.M.et.al.   10580570
[106] “Band 3 mutations, renal tubular acidosis and South-East Asian ovalocytosis in Malaysia and Papua New Guinea: loss of up to 95% band 3 transport in red cells.”  Bruce L.J.et.al.   10926824
[107] “Severe hereditary spherocytosis and distal renal tubular acidosis associated with the total absence of band 3.”  Ribeiro M.L.et.al.   10942416
[108] “Characteristic features of the genotype and phenotype of hereditary spherocytosis in the Japanese population.”  Yawata Y.et.al.   10745622
[109] “Trafficking and folding defects in hereditary spherocytosis mutants of the human red cell anion exchanger.”  Quilty J.A.et.al.   11208088
[110] “Amino acid substitutions in human erythroid protein band 3 account for the low-incidence antigens NFLD and BOW.”  McManus K.et.al.   10738034
[111] “An amino acid substitution in the putative second extracellular loop of RBC band 3 accounts for the Froese blood group polymorphism.”  McManus K.et.al.   11061863
[112] “Distinctive Swann blood group genotypes: molecular investigations.”  Zelinski T.et.al.   11155072
[113] “Band 3 Cape Town (E90K) causes severe hereditary spherocytosis in combination with band 3 Prague III.”  Bracher N.A.et.al.   11380459
[114] “Novel compound heterozygous SLC4A1 mutations in Thai patients with autosomal recessive distal renal tubular acidosis.”  Sritippayawan S.et.al.   15211439
[115] “A novel missense mutation in AE1 causing autosomal dominant distal renal tubular acidosis retains normal transport function but is mistargeted in polarized epithelial cells.”  Rungroj N.et.al.   14734552
[116] “Band 3Tambau: a de novo mutation in the AE1 gene associated with hereditary spherocytosis. Implications for anion exchange and insertion into the red blood cell membrane.”  Lima P.R.M.et.al.   15813913
[117] “Monovalent cation leaks in human red cells caused by single amino-acid substitutions in the transport domain of the band 3 chloride-bicarbonate exchanger, AE1.”  Bruce L.J.et.al.   16227998
Structure:
1BH7   1BNX   1BTQ   1BTR   1BTS   1BTT   1BZK   1HYN   2BTA   2BTB   [...more]

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MEELQDDYED MMEENLEQEE YEDPDIPESQ MEEPAAHDTE ATATDYHTTS HPGTHKVYVE 
61:	LQELVMDEKN QELRWMEAAR WVQLEENLGE NGAWGRPHLS HLTFWSLLEL RRVFTKGTVL 
121:	LDLQETSLAG VANQLLDRFI FEDQIRPQDR EELLRALLLK HSHAGELEAL GGVKPAVLTR 
181:	SGDPSQPLLP QHSSLETQLF CEQGDGGTEG HSPSGILEKI PPDSEATLVL VGRADFLEQP 
241:	VLGFVRLQEA AELEAVELPV PIRFLFVLLG PEAPHIDYTQ LGRAAATLMS ERVFRIDAYM 
301:	AQSRGELLHS LEGFLDCSLV LPPTDAPSEQ ALLSLVPVQR ELLRRRYQSS PAKPDSSFYK 
361:	GLDLNGGPDD PLQQTGQLFG GLVRDIRRRY PYYLSDITDA FSPQVLAAVI FIYFAALSPA 
421:	ITFGGLLGEK TRNQMGVSEL LISTAVQGIL FALLGAQPLL VVGFSGPLLV FEEAFFSFCE 
481:	TNGLEYIVGR VWIGFWLILL VVLVVAFEGS FLVRFISRYT QEIFSFLISL IFIYETFSKL 
541:	IKIFQDHPLQ KTYNYNVLMV PKPQGPLPNT ALLSLVLMAG TFFFAMMLRK FKNSSYFPGK 
601:	LRRVIGDFGV PISILIMVLV DFFIQDTYTQ KLSVPDGFKV SNSSARGWVI HPLGLRSEFP 
661:	IWMMFASALP ALLVFILIFL ESQITTLIVS KPERKMVKGS GFHLDLLLVV GMGGVAALFG 
721:	MPWLSATTVR SVTHANALTV MGKASTPGAA AQIQEVKEQR ISGLLVAVLV GLSILMEPIL 
781:	SRIPLAVLFG IFLYMGVTSL SGIQLFDRIL LLFKPPKYHP DVPYVKRVKT WRMHLFTGIQ 
841:	IICLAVLWVV KSTPASLALP FVLILTVPLR RVLLPLIFRN VELQCLDADD AKATFDEEEG 
901:	RDEYDEVAMP V