[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Blood; PubMed=3223947 [NCBI, ExPASy, EBI, Israel, Japan] Tanner M.J.A., Martin P.G., High S.; "The complete amino acid sequence of the human erythrocyte membrane anion-transport protein deduced from the cDNA sequence."; Biochem. J. 256:703-712(1988).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1073/pnas.86.23.9089; PubMed=2594752 [NCBI, ExPASy, EBI, Israel, Japan] Lux S.E., John K.M., Kopito R.R., Lodish H.F.; "Cloning and characterization of band 3, the human erythrocyte anion-exchange protein (AE1)."; Proc. Natl. Acad. Sci. U.S.A. 86:9089-9093(1989).
[3]	NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-38. DOI=10.1007/s00467-005-2061-z; PubMed=16252102 [NCBI, ExPASy, EBI, Israel, Japan] Choo K.E., Nicoli T.K., Bruce L.J., Tanner M.J., Ruiz-Linares A., Wrong O.M.; "Recessive distal renal tubular acidosis in Sarawak caused by AE1 mutations."; Pediatr. Nephrol. 21:212-217(2006).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-38; GLU-56; LYS-508 AND ILE-862. SeattleSNPs variation discovery resource; Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Cerebellum; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[6]	PROTEIN SEQUENCE OF 1-199; 220-292 AND 347-370. DOI=10.1016/0167-4838(89)90116-7; PubMed=2790053 [NCBI, ExPASy, EBI, Israel, Japan] Yannoukakos D., Vasseur C., Blouquit Y., Bursaux E., Wajcman H.; "Primary structure of the cytoplasmic domain of human erythrocyte protein band 3. Comparison with its sequence in the mouse."; Biochim. Biophys. Acta 998:43-49(1989).
[7]	PROTEIN SEQUENCE OF 1-201. PubMed=6345535 [NCBI, ExPASy, EBI, Israel, Japan] Kaul R.K., Murthy S.N.P., Reddy A.G., Steck T.L., Kohler H.; "Amino acid sequence of the N alpha-terminal 201 residues of human erythrocyte membrane band 3."; J. Biol. Chem. 258:7981-7990(1983).
[8]	PROTEIN SEQUENCE OF 1-3. PubMed=701248 [NCBI, ExPASy, EBI, Israel, Japan] Drickamer L.K.; "Orientation of the band 3 polypeptide from human erythrocyte membranes. Identification of NH2-terminal sequence and site of carbohydrate attachment."; J. Biol. Chem. 253:7242-7248(1978).
[9]	NUCLEOTIDE SEQUENCE [MRNA] OF 66-180. PubMed=7506871 [NCBI, ExPASy, EBI, Israel, Japan] Kollert-Jons A., Wagner S., Hubner S., Appelhans H., Drenckhahn D.; "Anion exchanger 1 in human kidney and oncocytoma differs from erythroid AE1 in its NH2 terminus."; Am. J. Physiol. 265:F813-F821(1993).
[10]	PROTEIN SEQUENCE OF 559-630. PubMed=6615451 [NCBI, ExPASy, EBI, Israel, Japan] Brock C.J., Tanner M.J.A., Kempf C.; "The human erythrocyte anion-transport protein. Partial amino acid sequence, conformation and a possible molecular mechanism for anion exchange."; Biochem. J. 213:577-586(1983).
[11]	PROTEIN SEQUENCE OF 665-688, AND ROLE OF GLU-681. PubMed=1352774 [NCBI, ExPASy, EBI, Israel, Japan] Jennings M.L., Smith J.S.; "Anion-proton cotransport through the human red blood cell band 3 protein. Role of glutamate 681."; J. Biol. Chem. 267:13964-13971(1992).
[12]	NUCLEOTIDE SEQUENCE [MRNA] OF 757-778, AND VARIANT HS ASP-771. DOI=10.1111/j.1365-2141.1995.tb05393.x; PubMed=8547122 [NCBI, ExPASy, EBI, Israel, Japan] Maillet P., Vallier A., Reinhart W.H., Wyss E.J., Ott P., Texier P., Baklouti F., Tanner M.J.A., Delaunay J., Alloisio N.; "Band 3 Chur: a variant associated with band 3-deficient hereditary spherocytosis and substitution in a highly conserved position of transmembrane segment 11."; Br. J. Haematol. 91:804-810(1995).
[13]	PROTEIN SEQUENCE OF 834-911. PubMed=3372523 [NCBI, ExPASy, EBI, Israel, Japan] Kawano Y., Okubo K., Tokunaga F., Miyata T., Iwanaga S., Hamasaki N.; "Localization of the pyridoxal phosphate binding site at the COOH-terminal region of erythrocyte band 3 protein."; J. Biol. Chem. 263:8232-8238(1988).
[14]	PHOSPHORYLATION AT TYR-8; TYR-21 AND TYR-46. DOI=10.1016/0005-2736(91)90291-F; PubMed=1998697 [NCBI, ExPASy, EBI, Israel, Japan] Yannoukakos D., Vasseur C., Piau J.-P., Wajcman H., Bursaux E.; "Phosphorylation sites in human erythrocyte band 3 protein."; Biochim. Biophys. Acta 1061:253-266(1991).
[15]	PALMITOYLATION AT CYS-843. PubMed=1885574 [NCBI, ExPASy, EBI, Israel, Japan] Okubo K., Hamasaki N., Hara K., Kageura M.; "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."; J. Biol. Chem. 266:16420-16424(1991).
[16]	PHOSPHORYLATION AT TYR-8; TYR-21; TYR-359 AND TYR-904. PubMed=10942405 [NCBI, ExPASy, EBI, Israel, Japan] Brunati A.M., Bordin L., Clari G., James P., Quadroni M., Baritono E., Pinna L.A., Donella-Deana A.; "Sequential phosphorylation of protein band 3 by Syk and Lyn tyrosine kinases in intact human erythrocytes: identification of primary and secondary phosphorylation sites."; Blood 96:1550-1557(2000).
[17]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-359 AND TYR-904, AND MASS SPECTROMETRY. DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan] Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; "Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."; Cell 131:1190-1203(2007).
[18]	IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. Colinge J., Superti-Furga G., Bennett K.L.; Submitted (OCT-2008) to UniProtKB.
[19]	STRUCTURE BY ELECTRON CRYO-MICROSCOPY. PubMed=8508760 [NCBI, ExPASy, EBI, Israel, Japan] Wang D.N., Kuehlbrandt W., Sarabia V.E., Reithmeier R.A.F.; "Two-dimensional structure of the membrane domain of human band 3, the anion transport protein of the erythrocyte membrane."; EMBO J. 12:2233-2239(1993).
[20]	STRUCTURE BY ELECTRON CRYO-MICROSCOPY. PubMed=8045253 [NCBI, ExPASy, EBI, Israel, Japan] Wang D.N., Sarabia V.E., Reithmeier R.A.F., Kuehlbrandt W.; "Three-dimensional map of the dimeric membrane domain of the human erythrocyte anion exchanger, Band 3."; EMBO J. 13:3230-3235(1994).
[21]	STRUCTURE BY NMR OF 405-424 AND 436-456. DOI=10.1111/j.1432-1033.1994.tb18757.x; PubMed=8168533 [NCBI, ExPASy, EBI, Israel, Japan] Gargaro A.R., Bloomberg G.B., Dempsey C.E., Murray M., Tanner M.J.A.; "The solution structures of the first and second transmembrane-spanning segments of band 3."; Eur. J. Biochem. 221:445-454(1994).
[22]	STRUCTURE BY NMR OF 1-16. DOI=10.1021/bi00051a005; PubMed=8527430 [NCBI, ExPASy, EBI, Israel, Japan] Schneider M.L., Post C.B.; "Solution structure of a band 3 peptide inhibitor bound to aldolase: a proposed mechanism for regulating binding by tyrosine phosphorylation."; Biochemistry 34:16574-16584(1995).
[23]	STRUCTURE BY NMR OF 1-16. DOI=10.1021/bi971445b; PubMed=9454576 [NCBI, ExPASy, EBI, Israel, Japan] Eisenmesser E.Z., Post C.B.; "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."; Biochemistry 37:867-877(1998).
[24]	STRUCTURE BY NMR OF 389-430. PubMed=9765907 [NCBI, ExPASy, EBI, Israel, Japan] Chambers E.J., Askin D., Bloomberg G.B., Ring S.M., Tanner M.J.; "Studies on the structure of a transmembrane region and a cytoplasmic loop of the human red cell anion exchanger."; Biochem. Soc. Trans. 26:516-520(1998).
[25]	STRUCTURE BY NMR OF 803-835. DOI=10.1021/bi973158d; PubMed=9709005 [NCBI, ExPASy, EBI, Israel, Japan] Askin D., Bloomberg G.B., Chambers E.J., Tanner M.J.; "NMR solution structure of a cytoplasmic surface loop of the human red cell anion transporter, band 3."; Biochemistry 37:11670-11678(1998).
[26]	VARIANT MEMPHIS GLU-56. PubMed=1678289 [NCBI, ExPASy, EBI, Israel, Japan] Yannoukakos D., Vasseur C., Driancourt C., Blouquit Y., Delauney J., Wajcman H., Bursaux E.; "Human erythrocyte band 3 polymorphism (band 3 Memphis): characterization of the structural modification (Lys 56-->Glu) by protein chemistry methods."; Blood 78:1117-1120(1991).
[27]	VARIANT EL4 400-ALA--ALA-408 DEL, AND VARIANT MEMPHIS GLU-56. DOI=10.1073/pnas.88.24.11022; PubMed=1722314 [NCBI, ExPASy, EBI, Israel, Japan] Jarolim P., Palek J., Amato D., Hassan K., Sapak P., Nurse G.T., Rubin H.L., Zhai S., Sahr K.E., Liu S.-C.; "Deletion in erythrocyte band 3 gene in malaria-resistant Southeast Asian ovalocytosis."; Proc. Natl. Acad. Sci. U.S.A. 88:11022-11026(1991).
[28]	VARIANT HS ARG-327. PubMed=1378323 [NCBI, ExPASy, EBI, Israel, Japan] Jarolim P., Palek J., Rubin H.L., Prchal J.T., Korsgren C., Cohen C.M.; "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."; Blood 80:523-529(1992).
[29]	VARIANT EL4 400-ALA--ALA-408 DEL. DOI=10.1016/0022-2836(92)90254-H; PubMed=1538405 [NCBI, ExPASy, EBI, Israel, Japan] Schofield A.E., Tanner M.J.A., Pinder J.C., Clough B., Bayley P.M., Nash G.B., Dluzewski A.R., Reardon D.M., Cox T.M., Wilson R.J.M., Gratzer W.B.; "Basis of unique red cell membrane properties in hereditary ovalocytosis."; J. Mol. Biol. 223:949-958(1992).
[30]	VARIANT HS LEU-868. PubMed=8343110 [NCBI, ExPASy, EBI, Israel, Japan] Bruce L.J., Kay M.M., Lawrence C., Tanner M.J.; "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."; Biochem. J. 293:317-320(1993).
[31]	VARIANT MONTEFIORE LYS-40. PubMed=8471774 [NCBI, ExPASy, EBI, Israel, Japan] Rybicki A.C., Qiu J.J.H., Musto S., Rosen N.L., Nagel R.L., Schwartz R.S.; "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)."; Blood 81:2155-2165(1993).
[32]	VARIANT BLOOD GROUP DI(A)/MEMPHIS-II. PubMed=8206915 [NCBI, ExPASy, EBI, Israel, Japan] Bruce L.J., Anstee D.J., Spring F.A., Tanner M.J.; "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."; J. Biol. Chem. 269:16155-16158(1994).
[33]	VARIANT BLOOD GROUP WR(A). PubMed=7812009 [NCBI, ExPASy, EBI, Israel, Japan] Bruce L.J., Ring S.M., Anstee D.J., Reid M.E., Wilkinson S., Tanner M.J.; "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."; Blood 85:541-547(1995).
[34]	VARIANTS HS GLN-760; TRP-760; CYS-808 AND TRP-870. PubMed=7530501 [NCBI, ExPASy, EBI, Israel, Japan] Jarolim P., Rubin H.L., Brabec V., Chrobak L., Zolotarev A.S., Alper S.L., Brugnara C., Wichterle H., Palek J.; "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."; Blood 85:634-640(1995).
[35]	VARIANTS HS ASP-285; GLU-455; PRO-707; PRO-834 AND MET-837. PubMed=8943874 [NCBI, ExPASy, EBI, Israel, Japan] Jarolim P., Murray J.L., Rubin H.L., Taylor W.M., Prchal J.T., Ballas S.K., Snyder L.M., Chrobak L., Melrose W.D., Brabec V., Palek J.; "Characterization of 13 novel band 3 gene defects in hereditary spherocytosis with band 3 deficiency."; Blood 88:4366-4374(1996).
[36]	VARIANTS HS LYS-40; CYS-518 AND MET-663 DEL. DOI=10.1038/ng0696-214; PubMed=8640229 [NCBI, ExPASy, EBI, Israel, Japan] Eber S.W., Gonzalez J.M., Lux M.L., Scarpa A.L., Tse W.T., Dornwell M., Herbers J., Kugler W., Oezcan R., Pekrun A., Gallagher P.G., Schroeter W., Forget B.G., Lux S.E.; "Ankyrin-1 mutations are a major cause of dominant and recessive hereditary spherocytosis."; Nat. Genet. 13:214-218(1996).
[37]	VARIANTS HS SER-147 AND MET-488. PubMed=9207478 [NCBI, ExPASy, EBI, Israel, Japan] Alloisio N., Texier P., Vallier A., Ribeiro M.L., Morle L., Bozon M., Bursaux E., Maillet P., Goncalves P., Tanner M.J., Tamagnini G., Delaunay J.; "Modulation of clinical expression and band 3 deficiency in hereditary spherocytosis."; Blood 90:414-420(1997).
[38]	VARIANT HS ASN-783, AND VARIANTS ALA-38 AND MET-73. DOI=10.1046/j.1365-2141.1997.8732504.x; PubMed=9012689 [NCBI, ExPASy, EBI, Israel, Japan] Miraglia del Giudice E., Vallier A., Maillet P., Perrotta S., Cutillo S., Iolascon A., Tanner M.J., Delaunay J., Alloisio N.; "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."; Br. J. Haematol. 96:70-76(1997).
[39]	VARIANTS HS CYS-490 AND MET-837. DOI=10.1046/j.1365-2141.1997.1893005.x; PubMed=9233560 [NCBI, ExPASy, EBI, Israel, Japan] Dhermy D., Galand C., Bournier O., Boulanger L., Cynober T., Schismanoff P.O., Bursaux E., Tchernia G., Boivin P., Garbarz M.; "Heterogenous band 3 deficiency in hereditary spherocytosis related to different band 3 gene defects."; Br. J. Haematol. 98:32-40(1997).
[40]	VARIANTS DRTA CYS-589; HIS-589 AND PHE-613. PubMed=9312167 [NCBI, ExPASy, EBI, Israel, Japan] Bruce L.J., Cope D.L., Jones G.K., Schofield A.E., Burley M., Povey S., Unwin R.J., Wrong O., Tanner M.J.; "Familial distal renal tubular acidosis is associated with mutations in the red cell anion exchanger (Band 3, AE1) gene."; J. Clin. Invest. 100:1693-1707(1997).
[41]	VARIANTS BLOOD GROUPS RB(A); TR(A) AND WD(A). DOI=10.1046/j.1537-2995.1997.37697335155.x; PubMed=9191821 [NCBI, ExPASy, EBI, Israel, Japan] Jarolim P., Murray J.L., Rubin H.L., Smart E., Moulds J.M.; "Blood group antigens Rb(a), Tr(a), and Wd(a) are located in the third ectoplasmic loop of erythroid band 3."; Transfusion 37:607-615(1997).
[42]	VARIANT HS ALA-837. DOI=10.1159/000040904; PubMed=9973643 [NCBI, ExPASy, EBI, Israel, Japan] Iwase S., Ideguchi H., Takao M., Horiguchi-Yamada J., Iwasaki M., Takahara S., Sekikawa T., Mochizuki S., Yamada H.; "Band 3 Tokyo: Thr837-->Ala837 substitution in erythrocyte band 3 protein associated with spherocytic hemolysis."; Acta Haematol. 100:200-203(1998).
[43]	VARIANTS BLOOD GROUPS BOW; BP(A); ELO; HG(A); MO(A); VG(A) AND WU. PubMed=9845551 [NCBI, ExPASy, EBI, Israel, Japan] Jarolim P., Rubin H.L., Zakova D., Storry J., Reid M.E.; "Characterization of seven low incidence blood group antigens carried by erythrocyte band 3 protein."; Blood 92:4836-4843(1998).
[44]	VARIANT DRTA ASP-701. PubMed=9854053 [NCBI, ExPASy, EBI, Israel, Japan] Tanphaichitr V.S., Sumboonnanonda A., Ideguchi H., Shayakul C., Brugnara C., Takao M., Veerakul G., Alper S.L.; "Novel AE1 mutations in recessive distal renal tubular acidosis: loss-of-function is rescued by glycophorin A."; J. Clin. Invest. 102:2173-2179(1998).
[45]	VARIANTS DRTA HIS-589 AND SER-589. DOI=10.1073/pnas.95.11.6337; PubMed=9600966 [NCBI, ExPASy, EBI, Israel, Japan] Karet F.E., Gainza F.J., Gyory A.Z., Unwin R.J., Wrong O., Tanner M.J.A., Nayir A., Alpay H., Santos F., Hulton S.A., Bakkaloglu A., Ozen S., Cunningham M.J., di Pietro A., Walker W.G., Lifton R.P.; "Mutations in the chloride-bicarbonate exchanger gene AE1 cause autosomal dominant but not autosomal recessive distal renal tubular acidosis."; Proc. Natl. Acad. Sci. U.S.A. 95:6337-6342(1998).
[46]	VARIANTS BLOOD GROUP WU. DOI=10.1046/j.1537-2995.1998.38898375513.x; PubMed=9709782 [NCBI, ExPASy, EBI, Israel, Japan] Zelinski T., McManus K., Punter F., Moulds M., Coghlan G.; "A Gly565-->Ala substitution in human erythroid band 3 accounts for the Wu blood group polymorphism."; Transfusion 38:745-748(1998).
[47]	VARIANTS DRTA ASP-701; VAL-850 DEL AND ASP-858. DOI=10.1042/0264-6021:3500041; PubMed=10926824 [NCBI, ExPASy, EBI, Israel, Japan] Bruce L.J., Wrong O., Toye A.M., Young M.T., Ogle G., Ismail Z., Sinha A.K., McMaster P., Hwaihwanje I., Nash G.B., Hart S., Lavu E., Palmer R., Othman A., Unwin R.J., Tanner M.J.A.; "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."; Biochem. J. 350:41-51(2000).
[48]	VARIANT HS MET-488. PubMed=10942416 [NCBI, ExPASy, EBI, Israel, Japan] Ribeiro M.L., Alloisio N., Almeida H., Gomes C., Texier P., Lemos C., Mimoso G., Morle L., Bey-Cabet F., Rudigoz R.-C., Delaunay J., Tamagnini G.; "Severe hereditary spherocytosis and distal renal tubular acidosis associated with the total absence of band 3."; Blood 96:1602-1604(2000).
[49]	CHARACTERIZATION OF VARIANTS PRO-707; GLN-760; TRP-760; CYS-808; PRO-834; MET-837 AND TRP-870. DOI=10.1034/j.1600-0854.2000.011208.x; PubMed=11208088 [NCBI, ExPASy, EBI, Israel, Japan] Quilty J.A., Reithmeier R.A.; "Trafficking and folding defects in hereditary spherocytosis mutants of the human red cell anion exchanger."; Traffic 1:987-998(2000).
[50]	VARIANT BLOOD GROUP FR(A+) LYS-480. DOI=10.1046/j.1537-2995.2000.40101246.x; PubMed=11061863 [NCBI, ExPASy, EBI, Israel, Japan] McManus K., Lupe K., Coghlan G., Zelinski T.; "An amino acid substitution in the putative second extracellular loop of RBC band 3 accounts for the Froese blood group polymorphism."; Transfusion 40:1246-1249(2000).
[51]	VARIANTS BLOOD GROUP SW(A+) GLN-646 AND TRP-646. DOI=10.1159/000056733; PubMed=11155072 [NCBI, ExPASy, EBI, Israel, Japan] Zelinski T., Rusnak A., McManus K., Coghlan G.; "Distinctive Swann blood group genotypes: molecular investigations."; Vox Sang. 79:215-218(2000).
[52]	VARIANTS HS LYS-90 AND TRP-870. DOI=10.1046/j.1365-2141.2001.02800.x; PubMed=11380459 [NCBI, ExPASy, EBI, Israel, Japan] Bracher N.A., Lyons C.A., Wessels G., Mansvelt E., Coetzer T.L.; "Band 3 Cape Town (E90K) causes severe hereditary spherocytosis in combination with band 3 Prague III."; Br. J. Haematol. 113:689-693(2001).
[53]	VARIANTS DRTA PRO-602 AND PRO-773. DOI=10.1053/j.ajkd.2004.03.033; PubMed=15211439 [NCBI, ExPASy, EBI, Israel, Japan] Sritippayawan S., Sumboonnanonda A., Vasuvattakul S., Keskanokwong T., Sawasdee N., Paemanee A., Thuwajit P., Wilairat P., Nimmannit S., Malasit P., Yenchitsomanus P.T.; "Novel compound heterozygous SLC4A1 mutations in Thai patients with autosomal recessive distal renal tubular acidosis."; Am. J. Kidney Dis. 44:64-70(2004).
[54]	VARIANTS HS PRO-687; TYR-705; PRO-731; ARG-734 AND GLN-760. DOI=10.1038/ng1656; PubMed=16227998 [NCBI, ExPASy, EBI, Israel, Japan] Bruce L.J., Robinson H.C., Guizouarn H., Borgese F., Harrison P., King M.-J., Goede J.S., Coles S.E., Gore D.M., Lutz H.U., Ficarella R., Layton D.M., Iolascon A., Ellory J.C., Stewart G.W.; "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."; Nat. Genet. 37:1258-1263(2005).

Comments

FUNCTION: Band 3 is the major integral glycoprotein of the erythrocyte membrane. Band 3 has two functional domains. Its integral domain mediates a 1:1 exchange of inorganic anions across the membrane, whereas its cytoplasmic domain provides binding sites for cytoskeletal proteins, glycolytic enzymes, and hemoglobin.
SUBUNIT: A dimer in solution, it spans the membrane asymmetrically and appears to be tetrameric.
SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
TISSUE SPECIFICITY: Erythrocytes.
PTM: Phosphorylated on Tyr-8 and Tyr-21 most likely by SYK. PP1-resistant phosphorylation that precedes Tyr-359 and Tyr-904 phosphorylation.
PTM: Phosphorylated on Tyr-359 and Tyr-904 most likely by LYN. PP1-inhibited phosphorylation that follows Tyr-8 and Tyr-21 phosphorylation.
POLYMORPHISM: SLC4A1 is responsible for the Diego blood group system. The molecular basis of the Di(a)=Di1/Di(b)/Di2 blood group antigens is a single variation in position 854; Leu-854 corresponds to Di(a) and Pro-854 to Di(b). The molecular basis of the Wr(a)=Di3/Wr(b)/Di4 blood group antigens is a single variation in position 658; Lys-658 corresponds to Wr(a) and Glu-658 to Wr(b). The blood group antigens Wd(a)=Di5 (Waldner-type) has Met-557; Rb(a)=Di6 has Leu-548 and WARR=Di7 has Ile-552.
POLYMORPHISM: SLC4A1 is responsible for the Swann blood group system (SW) [MIM:601550]. Sw(a+) has a Gln or a Trp at position 646 and Sw(a-) has an Arg.
POLYMORPHISM: SLC4A1 is responsible for the Froese blood group system (FR) [MIM:601551]. FR(a+) has a Lys at position 480 and FR(a-) has a Glu.
DISEASE: Defects in SLC4A1 are the cause of elliptocytosis type 4 (EL4) [MIM:109270]. EL4 is a Rhesus-unlinked form of hereditary elliptocytosis, a genetically heterogeneous, autosomal dominant hematologic disorder. It is characterized by variable hemolytic anemia and elliptical or oval red cell shape.
DISEASE: Defects in SLC4A1 are a cause of hereditary spherocytosis (HS) [MIM:109270]. HS is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal.
DISEASE: Defects in SLC4A1 are the cause of autosomal dominant distal renal tubular acidosis (dRTA) [MIM:179800]. This disease is characterized by reduced ability to acidify urine, variable hyperchloremic hypokalemic metabolic acidosis, nephrocalcinosis, and nephrolithiasis.
DISEASE: Defects in SLC4A1 are the cause of autosomal recessive distal renal tubular acidosis (dRTA) [MIM:611590].
MISCELLANEOUS: Phenyl isothiocyanate inhibits anion transport in vitro.
SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family [view classification].
WEB RESOURCE: Name=Wikipedia; Note=Band 3 entry; URL="http://en.wikipedia.org/wiki/Band_3";.
WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene mutation database; URL="http://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=diego";.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=SLC4A1";.
WEB RESOURCE: Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/slc4a1/";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X12609; CAA31128.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M27819; AAA35514.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ419529; ABD74692.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ072115; AAY57324.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC096106; AAH96106.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC096107; AAH96107.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC099628; AAH99628.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC099629; AAH99629.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC101570; AAI01571.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC101574; AAI01575.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S68680; AAC60608.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00926256; -.

A36218; B3HU.

NP_000333.1; -.

3D structure databases

PDB

1BH7; NMR; -; A=803-835.	[ExPASy / RCSB / EBI]
1BNX; NMR; -; A=389-430.	[ExPASy / RCSB / EBI]
1BTQ; NMR; -; A=405-424.	[ExPASy / RCSB / EBI]
1BTR; NMR; -; A=405-424.	[ExPASy / RCSB / EBI]
1BTS; NMR; -; A=436-456.	[ExPASy / RCSB / EBI]
1BTT; NMR; -; A=436-456.	[ExPASy / RCSB / EBI]
1BZK; NMR; -; A=389-430.	[ExPASy / RCSB / EBI]
1HYN; X-ray; 2.60 A; P/Q/R/S=1-379.	[ExPASy / RCSB / EBI]
2BTA; NMR; -; A=1-15.	[ExPASy / RCSB / EBI]
2BTB; NMR; -; A=1-15.	[ExPASy / RCSB / EBI]
3BTB; NMR; -; A=1-15.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1BH7; -.
1BNX; -.
1BTQ; -.
1BTR; -.
1BTS; -.
1BTT; -.
1BZK; -.
1HYN; -.
2BTA; -.
2BTB; -.
3BTB; -.

DisProt

DP00426; -.

ModBase

P02730.

Protein family/group databases

TCDB

2.A.31.1.1; anion exchanger (AE) family.

PTM databases

PhosphoSite

P02730; -.

Organism-specific databases

GC17M039683; -.

HIX0039232; -.

HGNC:11027; SLC4A1.

HPA015584; -.

109270; gene+phenotype. [NCBI / EBI]
110500; phenotype. [NCBI / EBI]
112010; phenotype. [NCBI / EBI]
112050; phenotype. [NCBI / EBI]
130600; phenotype. [NCBI / EBI]
179800; phenotype. [NCBI / EBI]
601550; phenotype. [NCBI / EBI]
601551; phenotype. [NCBI / EBI]
611590; phenotype. [NCBI / EBI]

Orphanet

288; Elliptocytosis, hereditary.
18; Renal tubular acidosis, distal.
822; Spherocytosis hereditary.

PharmGKB

PA35895; -.

Gene expression databases

ArrayExpress

P02730; -.

Bgee

P02730; -.

GermOnline

ENSG00000004939; Homo sapiens.

Ontologies

GO:0016323;	Cellular component: basolateral plasma membrane (inferred from sequence or structural similarity from UniProtKB).
GO:0030863;	Cellular component: cortical cytoskeleton (inferred from direct assay from UniProtKB).
GO:0005887;	Cellular component: integral to plasma membrane (inferred from direct assay from UniProtKB).
GO:0030506;	Molecular function: ankyrin binding (inferred from physical interaction from UniProtKB).
GO:0005452;	Molecular function: inorganic anion exchanger activity (inferred from electronic annotation from InterPro).
GO:0043495;	Molecular function: protein anchor (traceable author statement from UniProtKB).
GO:0042803;	Molecular function: protein homodimerization activity (inferred from physical interaction from UniProtKB).
GO:0006820;	Biological process: anion transport (traceable author statement from ProtInc).
GO:0006873;	Biological process: cellular ion homeostasis (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR001717; Anion_exchange.
IPR002977; Anion_exchange_1.
IPR018241; Anion_exchange_CS.
IPR011531; HCO3_transpt_C.
IPR013769; HCO3_transpt_cyt.
IPR003020; HCO3_transpt_euk.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.1100.10; HCO3_transpt_cyt; 1.

PANTHER

PTHR11453; HCO3_transpt_euk; 1.

Pfam

PF07565; Band_3_cyto; 1.
PF00955; HCO3_cotransp; 1.
Pfam graphical view of domain structure.

PRINTS

PR00165; ANIONEXCHNGR.
PR01187; ANIONEXHNGR1.
PR01231; HCO3TRNSPORT.

TIGRFAMs

TIGR00834; ae; 1.

PROSITE

PS00219; ANION_EXCHANGER_1; 1.
PS00220; ANION_EXCHANGER_2; 1.

Proteomic databases

PRIDE

P02730; -.

Genome annotation databases

Ensembl

ENSG00000004939; Homo sapiens. [Contig view]

GeneID

6521; -.

KEGG

hsa:6521; -.

Phylogenomic databases

HOGENOM

P02730; -.

HOVERGEN

P02730; -.

OMA

P02730; DYTQLGR.

Other

NextBio

25367; -.

PMAP-CutDB

P02730; -.

SOURCE

SLC4A1; Homo sapiens.

ProtoNet

P02730.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Acetylation; Anion exchange; Blood group antigen; Direct protein sequencing; Disease mutation; Elliptocytosis; Glycoprotein; Hereditary hemolytic anemia; Ion transport; Lipoprotein; Membrane; Palmitate; Phosphoprotein; Polymorphism; Transmembrane; Transport.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 911`	`911`	`Band 3 anion transport protein.`	`PRO_0000079209`
`TOPO_DOM`	`1 403`	`403`	`Cytoplasmic.`
`TRANSMEM`	`404 424`	`21`	`Potential.`
`TRANSMEM`	`437 456`	`20`	`Potential.`
`TRANSMEM`	`460 479`	`20`	`Potential.`
`TRANSMEM`	`491 510`	`20`	`Potential.`
`TRANSMEM`	`523 541`	`19`	`Potential.`
`TOPO_DOM`	`542 568`	`27`	`Extracellular (Potential).`
`TRANSMEM`	`569 588`	`20`	`Potential.`
`TOPO_DOM`	`589 603`	`15`	`Cytoplasmic (Potential).`
`TRANSMEM`	`604 624`	`21`	`Potential.`
`TOPO_DOM`	`625 660`	`36`	`Extracellular (Potential).`
`TRANSMEM`	`661 680`	`20`	`Potential.`
`TRANSMEM`	`699 719`	`21`	`Potential.`
`TRANSMEM`	`763 780`	`18`	`Potential.`
`TRANSMEM`	`785 806`	`22`	`Potential.`
`TRANSMEM`	`844 865`	`22`	`Potential.`
`REGION`	`404 911`	`508`	`Membrane (anion exchange).`
`REGION`	`559 630`	`72`	`Involved in anion transport.`
`SITE`	`590 590`	`1`	`Important for anion transport.`
`SITE`	`681 681`	`1`	`Important for anion-proton cotransport.`
`MOD_RES`	`1 1`		`N-acetylmethionine.`
`MOD_RES`	`8 8`		`Phosphotyrosine.`
`MOD_RES`	`21 21`		`Phosphotyrosine.`
`MOD_RES`	`46 46`		`Phosphotyrosine.`
`MOD_RES`	`350 350`		`Phosphoserine (By similarity).`
`MOD_RES`	`359 359`		`Phosphotyrosine.`
`MOD_RES`	`904 904`		`Phosphotyrosine.`
`LIPID`	`843 843`		`S-palmitoyl cysteine.`
`CARBOHYD`	`642 642`		`N-linked (GlcNAc...) (Probable).`
`VARIANT`	`38 38`	`1`	`D -> A (in dbSNP:rs5035 [NCBI]).`	`VAR_014612`
`VARIANT`	`40 40`	`1`	`E -> K (in hemolytic anemia; Montefiore; dbSNP:rs45562031 [NCBI]).`	`VAR_000798`
`VARIANT`	`45 45`	`1`	`D -> E (in dbSNP:rs34700496 [NCBI]).`	`VAR_036693`
`VARIANT`	`56 56`	`1`	`K -> E (in Memphis; dbSNP:rs5036 [NCBI]).`	`VAR_000799`
`VARIANT`	`68 68`	`1`	`E -> K (in dbSNP:rs13306787 [NCBI]).`	`VAR_039290`
`VARIANT`	`73 73`	`1`	`L -> M.`	`VAR_039291`
`VARIANT`	`90 90`	`1`	`E -> K (in HS; Cape Town; dbSNP:rs28929480 [NCBI]).`	`VAR_013784`
`VARIANT`	`112 112`	`1`	`R -> S (in dbSNP:rs5037 [NCBI]).`	`VAR_014613`
`VARIANT`	`130 130`	`1`	`G -> R (in HS; Fukoka).`	`VAR_013785`
`VARIANT`	`147 147`	`1`	`P -> S (in HS; Mondego).`	`VAR_013786`
`VARIANT`	`285 285`	`1`	`A -> D (in HS; Boston).`	`VAR_013787`
`VARIANT`	`327 327`	`1`	`P -> R (in HS; Tuscaloosa; dbSNP:rs28931583 [NCBI]).`	`VAR_000800`
`VARIANT`	`400 408`	`9`	`Missing (in EL4).`	`VAR_000801`
`VARIANT`	`432 432`	`1`	`R -> W (in ELO antigen).`	`VAR_013788`
`VARIANT`	`442 442`	`1`	`I -> F (in dbSNP:rs5018 [NCBI]).`	`VAR_014614`
`VARIANT`	`455 455`	`1`	`G -> E (in HS; Benesov).`	`VAR_013789`
`VARIANT`	`480 480`	`1`	`E -> K (in FR(a+) antigen).`	`VAR_013790`
`VARIANT`	`488 488`	`1`	`V -> M (in HS; Coimbra; also in dRTA autosomal recessive form; dbSNP:rs28931584 [NCBI]).`	`VAR_013791`
`VARIANT`	`490 490`	`1`	`R -> C (in HS; Bicetre I).`	`VAR_013792`
`VARIANT`	`508 508`	`1`	`E -> K (in dbSNP:rs45568837 [NCBI]).`	`VAR_025090`
`VARIANT`	`518 518`	`1`	`R -> C (in HS; Dresden).`	`VAR_000802`
`VARIANT`	`548 548`	`1`	`P -> L (in RB(A) antigen).`	`VAR_000803`
`VARIANT`	`551 551`	`1`	`K -> N (in TR(A) antigen).`	`VAR_013793`
`VARIANT`	`552 552`	`1`	`T -> I (in WARR antigen).`	`VAR_000804`
`VARIANT`	`555 555`	`1`	`Y -> H (in VG(a) antigen).`	`VAR_013794`
`VARIANT`	`557 557`	`1`	`V -> M (in WD(a) antigen).`	`VAR_000805`
`VARIANT`	`561 561`	`1`	`P -> S (in BOW antigen).`	`VAR_013795`
`VARIANT`	`565 565`	`1`	`G -> A (in WU antigen).`	`VAR_013796`
`VARIANT`	`566 566`	`1`	`P -> A (in KREP antigen).`	`VAR_013797`
`VARIANT`	`566 566`	`1`	`P -> S (in PN(a) antigen).`	`VAR_013798`
`VARIANT`	`569 569`	`1`	`N -> K (in BP(a) antigen).`	`VAR_013799`
`VARIANT`	`586 586`	`1`	`M -> L (in dbSNP:rs5019 [NCBI]).`	`VAR_014615`
`VARIANT`	`589 589`	`1`	`R -> C (in dRTA; autosomal dominant form; reduced red cell sulfate transport and altered glycosylation of the red cell band 3 N-glycan chain).`	`VAR_015104`
`VARIANT`	`589 589`	`1`	`R -> H (in dRTA; autosomal dominant form).`	`VAR_015105`
`VARIANT`	`589 589`	`1`	`R -> S (in dRTA; autosomal dominant form).`	`VAR_015106`
`VARIANT`	`602 602`	`1`	`R -> P (in dRTA; autosomal recessive form; with hemolytic anemia).`	`VAR_039292`
`VARIANT`	`613 613`	`1`	`S -> F (in dRTA; autosomal dominant form; markedly increased red cell sulfate transport but almost normal red cell iodide transport).`	`VAR_015107`
`VARIANT`	`646 646`	`1`	`R -> Q (in SW(a+) antigen).`	`VAR_013800`
`VARIANT`	`646 646`	`1`	`R -> W (in SW(a+) antigen).`	`VAR_013801`
`VARIANT`	`656 656`	`1`	`R -> C (in HG(a) antigen).`	`VAR_013802`
`VARIANT`	`656 656`	`1`	`R -> H (in MO(a) antigen).`	`VAR_013803`
`VARIANT`	`658 658`	`1`	`E -> K (in WR(a) antigen).`	`VAR_000806`
`VARIANT`	`663 663`	`1`	`Missing (in HS; Osnabruck II).`	`VAR_000807`
`VARIANT`	`687 687`	`1`	`L -> P (in HS).`	`VAR_039293`
`VARIANT`	`688 688`	`1`	`I -> V (in dbSNP:rs5022 [NCBI]).`	`VAR_014616`
`VARIANT`	`690 690`	`1`	`S -> G (in dbSNP:rs5023 [NCBI]).`	`VAR_014617`
`VARIANT`	`701 701`	`1`	`G -> D (in dRTA; autosomal recessive form).`	`VAR_015171`
`VARIANT`	`705 705`	`1`	`D -> Y (in HS).`	`VAR_039294`
`VARIANT`	`707 707`	`1`	`L -> P (in HS; Most).`	`VAR_013804`
`VARIANT`	`714 714`	`1`	`G -> R (in HS; Okinawa).`	`VAR_013805`
`VARIANT`	`731 731`	`1`	`S -> P (in HS).`	`VAR_039295`
`VARIANT`	`734 734`	`1`	`H -> R (in HS).`	`VAR_039296`
`VARIANT`	`760 760`	`1`	`R -> Q (in HS; Prague II).`	`VAR_013806`
`VARIANT`	`760 760`	`1`	`R -> W (in HS; Hradec Kralove).`	`VAR_013807`
`VARIANT`	`771 771`	`1`	`G -> D (in HS; Chur).`	`VAR_013808`
`VARIANT`	`773 773`	`1`	`S -> P (in dRTA; autosomal recessive form; with normal red cell morphology).`	`VAR_039297`
`VARIANT`	`783 783`	`1`	`I -> N (in HS; Napoli II).`	`VAR_013809`
`VARIANT`	`808 808`	`1`	`R -> C (in HS; Jablonec).`	`VAR_013810`
`VARIANT`	`808 808`	`1`	`R -> H (in HS; Nara).`	`VAR_013811`
`VARIANT`	`832 832`	`1`	`R -> H (in dbSNP:rs5025 [NCBI]).`	`VAR_014618`
`VARIANT`	`834 834`	`1`	`H -> P (in HS; Birmingham).`	`VAR_013812`
`VARIANT`	`837 837`	`1`	`T -> A (in HS; Tokyo).`	`VAR_013813`
`VARIANT`	`837 837`	`1`	`T -> M (in HS; Philadelphia).`	`VAR_013814`
`VARIANT`	`850 850`	`1`	`Missing (in dRTA; autosomal recessive form).`	`VAR_015109`
`VARIANT`	`854 854`	`1`	`P -> L (in Di(a)/Memphis-II antigen; dbSNP:rs2285644 [NCBI]).`	`VAR_000808`
`VARIANT`	`858 858`	`1`	`A -> D (in dRTA; autosomal dominant form).`	`VAR_015108`
`VARIANT`	`862 862`	`1`	`V -> I (in dbSNP:rs5026 [NCBI]).`	`VAR_014619`
`VARIANT`	`868 868`	`1`	`P -> L (in HS; HT).`	`VAR_013815`
`VARIANT`	`870 870`	`1`	`R -> W (in HS; Prague III; dbSNP:rs28931585 [NCBI]).`	`VAR_013816`
`CONFLICT`	`11 11`		`M -> D (in Ref. 7; AA sequence).`
`CONFLICT`	`27 27`		`P -> H (in Ref. 5; AAH99628).`
`CONFLICT`	`68 68`		`E -> EE (in Ref. 7; AA sequence).`
`CONFLICT`	`759 759`		`Q -> H (in Ref. 3; ABD74692).`
`STRAND`	`58 67`	`10`
`TURN`	`68 70`	`3`
`STRAND`	`73 88`	`16`
`HELIX`	`104 115`	`12`
`STRAND`	`118 123`	`6`
`HELIX`	`128 141`	`14`
`HELIX`	`147 149`	`3`
`HELIX`	`150 157`	`8`
`HELIX`	`164 170`	`7`
`STRAND`	`173 175`	`3`
`HELIX`	`195 200`	`6`
`HELIX`	`212 219`	`8`
`STRAND`	`226 234`	`9`
`STRAND`	`241 251`	`11`
`STRAND`	`256 258`	`3`
`STRAND`	`262 270`	`9`
`HELIX`	`278 289`	`12`
`HELIX`	`292 300`	`9`
`HELIX`	`304 316`	`13`
`STRAND`	`319 321`	`3`
`HELIX`	`328 333`	`6`
`HELIX`	`335 346`	`12`
`STRAND`	`349 351`	`3`
`TURN`	`806 809`	`4`
`HELIX`	`829 833`	`5`

Sequence information

Length: 911 AA [This is the length of the unprocessed precursor]

Molecular weight: 101792 Da [This is the MW of the unprocessed precursor]

CRC64: 35EC3EE7AFF27D2F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEELQDDYED MMEENLEQEE YEDPDIPESQ MEEPAAHDTE ATATDYHTTS HPGTHKVYVE 

        70         80         90        100        110        120 
LQELVMDEKN QELRWMEAAR WVQLEENLGE NGAWGRPHLS HLTFWSLLEL RRVFTKGTVL 

       130        140        150        160        170        180 
LDLQETSLAG VANQLLDRFI FEDQIRPQDR EELLRALLLK HSHAGELEAL GGVKPAVLTR 

       190        200        210        220        230        240 
SGDPSQPLLP QHSSLETQLF CEQGDGGTEG HSPSGILEKI PPDSEATLVL VGRADFLEQP 

       250        260        270        280        290        300 
VLGFVRLQEA AELEAVELPV PIRFLFVLLG PEAPHIDYTQ LGRAAATLMS ERVFRIDAYM 

       310        320        330        340        350        360 
AQSRGELLHS LEGFLDCSLV LPPTDAPSEQ ALLSLVPVQR ELLRRRYQSS PAKPDSSFYK 

       370        380        390        400        410        420 
GLDLNGGPDD PLQQTGQLFG GLVRDIRRRY PYYLSDITDA FSPQVLAAVI FIYFAALSPA 

       430        440        450        460        470        480 
ITFGGLLGEK TRNQMGVSEL LISTAVQGIL FALLGAQPLL VVGFSGPLLV FEEAFFSFCE 

       490        500        510        520        530        540 
TNGLEYIVGR VWIGFWLILL VVLVVAFEGS FLVRFISRYT QEIFSFLISL IFIYETFSKL 

       550        560        570        580        590        600 
IKIFQDHPLQ KTYNYNVLMV PKPQGPLPNT ALLSLVLMAG TFFFAMMLRK FKNSSYFPGK 

       610        620        630        640        650        660 
LRRVIGDFGV PISILIMVLV DFFIQDTYTQ KLSVPDGFKV SNSSARGWVI HPLGLRSEFP 

       670        680        690        700        710        720 
IWMMFASALP ALLVFILIFL ESQITTLIVS KPERKMVKGS GFHLDLLLVV GMGGVAALFG 

       730        740        750        760        770        780 
MPWLSATTVR SVTHANALTV MGKASTPGAA AQIQEVKEQR ISGLLVAVLV GLSILMEPIL 

       790        800        810        820        830        840 
SRIPLAVLFG IFLYMGVTSL SGIQLFDRIL LLFKPPKYHP DVPYVKRVKT WRMHLFTGIQ 

       850        860        870        880        890        900 
IICLAVLWVV KSTPASLALP FVLILTVPLR RVLLPLIFRN VELQCLDADD AKATFDEEEG 

       910 
RDEYDEVAMP V

P02730 in FASTA format

View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools