ID B3AT_HUMAN STANDARD; PRT; 911 AA. AC P02730; P78487; DT 21-JUL-1986 (Rel. 01, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 24-JAN-2006 (Rel. 49, Last annotation update) DE Band 3 anion transport protein (Anion exchange protein 1) (AE 1) DE (Solute carrier family 4 member 1) (CD233 antigen). GN Name=SLC4A1; Synonyms=AE1, DI, EPB3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=90083213; PubMed=2594752; RA Lux S.E., John K.M., Kopito R.R., Lodish H.F.; RT "Cloning and characterization of band 3, the human erythrocyte anion- RT exchange protein (AE1)."; RL Proc. Natl. Acad. Sci. U.S.A. 86:9089-9093(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Blood; RX MEDLINE=89134172; PubMed=3223947; RA Tanner M.J.A., Martin P.G., High S.; RT "The complete amino acid sequence of the human erythrocyte membrane RT anion-transport protein deduced from the cDNA sequence."; RL Biochem. J. 256:703-712(1988). RN [3] RP PROTEIN SEQUENCE OF 1-199; 220-292 AND 347-370. RX MEDLINE=90001294; PubMed=2790053; DOI=10.1016/0167-4838(89)90116-7; RA Yannoukakos D., Vasseur C., Blouquit Y., Bursaux E., Wajcman H.; RT "Primary structure of the cytoplasmic domain of human erythrocyte RT protein band 3. Comparison with its sequence in the mouse."; RL Biochim. Biophys. Acta 998:43-49(1989). RN [4] RP PROTEIN SEQUENCE OF 1-201. RX MEDLINE=83238395; PubMed=6345535; RA Kaul R.K., Murthy S.N.P., Reddy A.G., Steck T.L., Kohler H.; RT "Amino acid sequence of the N alpha-terminal 201 residues of human RT erythrocyte membrane band 3."; RL J. Biol. Chem. 258:7981-7990(1983). RN [5] RP PROTEIN SEQUENCE OF 1-3. RX MEDLINE=79027186; PubMed=701248; RA Drickamer L.K.; RT "Orientation of the band 3 polypeptide from human erythrocyte RT membranes. Identification of NH2-terminal sequence and site of RT carbohydrate attachment."; RL J. Biol. Chem. 253:7242-7248(1978). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 66-180. RX MEDLINE=94113174; PubMed=7506871; RA Kollert-Jons A., Wagner S., Hubner S., Appelhans H., Drenckhahn D.; RT "Anion exchanger 1 in human kidney and oncocytoma differs from RT erythroid AE1 in its NH2 terminus."; RL Am. J. Physiol. 265:F813-F821(1993). RN [7] RP PROTEIN SEQUENCE OF 559-630. RX MEDLINE=83308584; PubMed=6615451; RA Brock C.J., Tanner M.J.A., Kempf C.; RT "The human erythrocyte anion-transport protein. Partial amino acid RT sequence, conformation and a possible molecular mechanism for anion RT exchange."; RL Biochem. J. 213:577-586(1983). RN [8] RP PROTEIN SEQUENCE OF 834-911. RX MEDLINE=88228050; PubMed=3372523; RA Kawano Y., Okubo K., Tokunaga F., Miyata T., Iwanaga S., Hamasaki N.; RT "Localization of the pyridoxal phosphate binding site at the COOH- RT terminal region of erythrocyte band 3 protein."; RL J. Biol. Chem. 263:8232-8238(1988). RN [9] RP ROLE OF GLU-681, AND PROTEIN SEQUENCE OF 665-688. RX MEDLINE=92332495; PubMed=1352774; RA Jennings M.L., Smith J.S.; RT "Anion-proton cotransport through the human red blood cell band 3 RT protein. Role of glutamate 681."; RL J. Biol. Chem. 267:13964-13971(1992). RN [10] RP PALMITOYLATION OF CYS-843. RX MEDLINE=91358422; PubMed=1885574; RA Okubo K., Hamasaki N., Hara K., Kageura M.; RT "Palmitoylation of cysteine 69 from the COOH-terminal of band 3 RT protein in the human erythrocyte membrane. Acylation occurs in the RT middle of the consensus sequence of F--I-IICLAVL found in band 3 RT protein and G2 protein of Rift Valley fever virus."; RL J. Biol. Chem. 266:16420-16424(1991). RN [11] RP PHOSPHORYLATION SITES TYR-8; TYR-21; TYR-359 AND TYR-904. RX MEDLINE=20400020; PubMed=10942405; RA Brunati A.M., Bordin L., Clari G., James P., Quadroni M., Baritono E., RA Pinna L.A., Donella-Deana A.; RT "Sequential phosphorylation of protein band 3 by Syk and Lyn tyrosine RT kinases in intact human erythrocytes: identification of primary and RT secondary phosphorylation sites."; RL Blood 96:1550-1557(2000). RN [12] RP VARIANT MEMPHIS GLU-56. RX MEDLINE=91329825; PubMed=1678289; RA Yannoukakos D., Vasseur C., Driancourt C., Blouquit Y., Delauney J., RA Wajcman H., Bursaux E.; RT "Human erythrocyte band 3 polymorphism (band 3 Memphis): RT characterization of the structural modification (Lys 56-->Glu) by RT protein chemistry methods."; RL Blood 78:1117-1120(1991). RN [13] RP VARIANT HE 400-ALA--ALA-408 DEL, AND VARIANT MEMPHIS GLU-56. RX MEDLINE=92107882; PubMed=1722314; RA Jarolim P., Palek J., Amato D., Hassan K., Sapak P., Nurse G.T., RA Rubin H.L., Zhai S., Sahr K.E., Liu S.-C.; RT "Deletion in erythrocyte band 3 gene in malaria-resistant Southeast RT Asian ovalocytosis."; RL Proc. Natl. Acad. Sci. U.S.A. 88:11022-11026(1991). RN [14] RP VARIANT HS ARG-327. RX MEDLINE=92329950; PubMed=1378323; RA Jarolim P., Palek J., Rubin H.L., Prchal J.T., Korsgren C., RA Cohen C.M.; RT "Band 3 Tuscaloosa: Pro-327-->Arg substitution in the cytoplasmic RT domain of erythrocyte band 3 protein associated with spherocytic RT hemolytic anemia and partial deficiency of protein 4.2."; RL Blood 80:523-529(1992). RN [15] RP VARIANT HE 400-ALA--ALA-408 DEL. RX MEDLINE=92167271; PubMed=1538405; RA Schofield A.E., Tanner M.J.A., Pinder J.C., Clough B., Bayley P.M., RA Nash G.B., Dluzewski A.R., Reardon D.M., Cox T.M., Wilson R.J.M., RA Gratzer W.B.; RT "Basis of unique red cell membrane properties in hereditary RT ovalocytosis."; RL J. Mol. Biol. 223:949-958(1992). RN [16] RP VARIANT HS LEU-868. RX MEDLINE=93343855; PubMed=8343110; RA Bruce L.J., Kay M.M., Lawrence C., Tanner M.J.; RT "Band 3 HT, a human red-cell variant associated with acanthocytosis RT and increased anion transport, carries the mutation Pro-868-->Leu in RT the membrane domain of band 3."; RL Biochem. J. 293:317-320(1993). RN [17] RP VARIANT MONTEFIORE LYS-40. RX MEDLINE=93229758; PubMed=8471774; RA Rybicki A.C., Qiu J.J.H., Musto S., Rosen N.L., Nagel R.L., RA Schwartz R.S.; RT "Human erythrocyte protein 4.2 deficiency associated with hemolytic RT anemia and a homozygous 40 glutamic acid-->lysine substitution in the RT cytoplasmic domain of band 3 (band 3Montefiore)."; RL Blood 81:2155-2165(1993). RN [18] RP VARIANT BLOOD GROUP DI(A)/MEMPHIS-II. RX MEDLINE=94266802; PubMed=8206915; RA Bruce L.J., Anstee D.J., Spring F.A., Tanner M.J.; RT "Band 3 Memphis variant II. Altered stilbene disulfonate binding and RT the Diego (Dia) blood group antigen are associated with the human RT erythrocyte band 3 mutation Pro-854-->Leu."; RL J. Biol. Chem. 269:16155-16158(1994). RN [19] RP VARIANT BLOOD GROUP WR(A). RX MEDLINE=95111140; PubMed=7812009; RA Bruce L.J., Ring S.M., Anstee D.J., Reid M.E., Wilkinson S., RA Tanner M.J.; RT "Changes in the blood group Wright antigens are associated with a RT mutation at amino acid 658 in human erythrocyte band 3: a site of RT interaction between band 3 and glycophorin A under certain RT conditions."; RL Blood 85:541-547(1995). RN [20] RP VARIANTS HS GLN-760; TRP-760; CYS-808 AND TRP-870. RX MEDLINE=95134893; PubMed=7530501; RA Jarolim P., Rubin H.L., Brabec V., Chrobak L., Zolotarev A.S., RA Alper S.L., Brugnara C., Wichterle H., Palek J.; RT "Mutations of conserved arginines in the membrane domain of erythroid RT band 3 lead to a decrease in membrane-associated band 3 and to the RT phenotype of hereditary spherocytosis."; RL Blood 85:634-640(1995). RN [21] RP VARIANT HS ASP-771. RX MEDLINE=96136073; PubMed=8547122; RA Maillet P., Vallier A., Reinhart W.H., Wyss E.J., Ott P., Texier P., RA Baklouti F., Tanner M.J., Delaunay J., Alloisio N.; RT "Band 3 Chur: a variant associated with band 3-deficient hereditary RT spherocytosis and substitution in a highly conserved position of RT transmembrane segment 11."; RL Br. J. Haematol. 91:804-810(1995). RN [22] RP VARIANTS HS ASP-285; GLU-455; PRO-707; PRO-834 AND MET-837. RX MEDLINE=97099297; PubMed=8943874; RA Jarolim P., Murray J.L., Rubin H.L., Taylor W.M., Prchal J.T., RA Ballas S.K., Snyder L.M., Chrobak L., Melrose W.D., Brabec V., RA Palek J.; RT "Characterization of 13 novel band 3 gene defects in hereditary RT spherocytosis with band 3 deficiency."; RL Blood 88:4366-4374(1996). RN [23] RP VARIANTS HS LYS-40; CYS-518 AND MET-663 DEL. RX MEDLINE=96225450; PubMed=8640229; RA Eber S.W., Gonzalez J.M., Lux M.L., Scarpa A.L., Tse W.T., RA Dornwell M., Herbers J., Kugler W., Oezcan R., Pekrun A., RA Gallagher P.G., Schroeter W., Forget B.G., Lux S.E.; RT "Ankyrin-1 mutations are a major cause of dominant and recessive RT hereditary spherocytosis."; RL Nat. Genet. 13:214-218(1996). RN [24] RP VARIANTS HS SER-147 AND MET-488. RX MEDLINE=97351102; PubMed=9207478; RA Alloisio N., Texier P., Vallier A., Ribeiro M.L., Morle L., Bozon M., RA Bursaux E., Maillet P., Goncalves P., Tanner M.J., Tamagnini G., RA Delaunay J.; RT "Modulation of clinical expression and band 3 deficiency in hereditary RT spherocytosis."; RL Blood 90:414-420(1997). RN [25] RP VARIANT HS ASN-783. RX MEDLINE=97164927; PubMed=9012689; RX DOI=10.1046/j.1365-2141.1997.8732504.x; RA Miraglia del Giudice E., Vallier A., Maillet P., Perrotta S., RA Cutillo S., Iolascon A., Tanner M.J., Delaunay J., Alloisio N.; RT "Novel band 3 variants (bands 3 Foggia, Napoli I and Napoli II) RT associated with hereditary spherocytosis and band 3 deficiency: status RT of the D38A polymorphism within the EPB3 locus."; RL Br. J. Haematol. 96:70-76(1997). RN [26] RP VARIANTS HS CYS-490 AND MET-837. RX MEDLINE=97376789; PubMed=9233560; RX DOI=10.1046/j.1365-2141.1997.1893005.x; RA Dhermy D., Galand C., Bournier O., Boulanger L., Cynober T., RA Schismanoff P.O., Bursaux E., Tchernia G., Boivin P., Garbarz M.; RT "Heterogenous band 3 deficiency in hereditary spherocytosis related to RT different band 3 gene defects."; RL Br. J. Haematol. 98:32-40(1997). RN [27] RP VARIANTS DRTA CYS-589; HIS-589 AND PHE-613. RX MEDLINE=97459993; PubMed=9312167; RA Bruce L.J., Cope D.L., Jones G.K., Schofield A.E., Burley M., RA Povey S., Unwin R.J., Wrong O., Tanner M.J.; RT "Familial distal renal tubular acidosis is associated with mutations RT in the red cell anion exchanger (Band 3, AE1) gene."; RL J. Clin. Invest. 100:1693-1707(1997). RN [28] RP VARIANTS BLOOD GROUPS RB(A); TR(A) AND WD(A). RX MEDLINE=97335155; PubMed=9191821; RX DOI=10.1046/j.1537-2995.1997.37697335155.x; RA Jarolim P., Murray J.L., Rubin H.L., Smart E., Moulds J.M.; RT "Blood group antigens Rb(a), Tr(a), and Wd(a) are located in the third RT ectoplasmic loop of erythroid band 3."; RL Transfusion 37:607-615(1997). RN [29] RP VARIANT HS ALA-837. RX MEDLINE=99141072; PubMed=9973643; DOI=10.1159/000040904; RA Iwase S., Ideguchi H., Takao M., Horiguchi-Yamada J., Iwasaki M., RA Takahara S., Sekikawa T., Mochizuki S., Yamada H.; RT "Band 3 Tokyo: Thr837-->Ala837 substitution in erythrocyte band 3 RT protein associated with spherocytic hemolysis."; RL Acta Haematol. 100:200-203(1998). RN [30] RP VARIANTS BLOOD GROUPS BOW; BP(A); ELO; HG(A); MO(A); VG(A) AND WU. RX MEDLINE=99061802; PubMed=9845551; RA Jarolim P., Rubin H.L., Zakova D., Storry J., Reid M.E.; RT "Characterization of seven low incidence blood group antigens carried RT by erythrocyte band 3 protein."; RL Blood 92:4836-4843(1998). RN [31] RP VARIANT DRTA ASP-701. RX MEDLINE=99072839; PubMed=9854053; RA Tanphaichitr V.S., Sumboonnanonda A., Ideguchi H., Shayakul C., RA Brugnara C., Takao M., Veerakul G., Alper S.L.; RT "Novel AE1 mutations in recessive distal renal tubular acidosis: loss- RT of-function is rescued by glycophorin A."; RL J. Clin. Invest. 102:2173-2179(1998). RN [32] RP VARIANTS DRTA HIS-589 AND SER-589. RX MEDLINE=98263357; PubMed=9600966; DOI=10.1073/pnas.95.11.6337; RA Karet F.E., Gainza F.J., Gyory A.Z., Unwin R.J., Wrong O., RA Tanner M.J.A., Nayir A., Alpay H., Santos F., Hulton S.A., RA Bakkaloglu A., Ozen S., Cunningham M.J., di Pietro A., Walker W.G., RA Lifton R.P.; RT "Mutations in the chloride-bicarbonate exchanger gene AE1 cause RT autosomal dominant but not autosomal recessive distal renal tubular RT acidosis."; RL Proc. Natl. Acad. Sci. U.S.A. 95:6337-6342(1998). RN [33] RP VARIANTS BLOOD GROUP WU. RX MEDLINE=98375513; PubMed=9709782; RX DOI=10.1046/j.1537-2995.1998.38898375513.x; RA Zelinski T., McManus K., Punter F., Moulds M., Coghlan G.; RT "A Gly565-->Ala substitution in human erythroid band 3 accounts for RT the Wu blood group polymorphism."; RL Transfusion 38:745-748(1998). RN [34] RP VARIANTS DRTA ASP-701; VAL-850 DEL AND ASP-858. RX MEDLINE=20386868; PubMed=10926824; DOI=10.1042/0264-6021:3500041; RA Bruce L.J., Wrong O., Toye A.M., Young M.T., Ogle G., Ismail Z., RA Sinha A.K., McMaster P., Hwaihwanje I., Nash G.B., Hart S., Lavu E., RA Palmer R., Othman A., Unwin R.J., Tanner M.J.A.; RT "Band 3 mutations, renal tubular acidosis and South-East Asian RT ovalocytosis in Malaysia and Papua New Guinea: loss of up to 95% band RT 3 transport in red cells."; RL Biochem. J. 350:41-51(2000). RN [35] RP CHARACTERIZATION OF VARIANTS PRO-707; GLN-760; TRP-760; CYS-808; RP PRO-834; MET-837 AND TRP-870. RX MEDLINE=21129019; PubMed=11208088; RA Quilty J.A., Reithmeier R.A.; RT "Trafficking and folding defects in hereditary spherocytosis mutants RT of the human red cell anion exchanger."; RL Traffic 1:987-998(2000). RN [36] RP VARIANTS BLOOD GROUPS SW(A) AND SW(!). RX MEDLINE=21068643; PubMed=11155072; DOI=10.1159/000056733; RA Zelinski T., Rusnak A., McManus K., Coghlan G.; RT "Distinctive Swann blood group genotypes: molecular investigations."; RL Vox Sang. 79:215-218(2000). RN [37] RP VARIANTS HS LYS-90 AND TRP-870. RX MEDLINE=21275193; PubMed=11380459; RX DOI=10.1046/j.1365-2141.2001.02800.x; RA Bracher N.A., Lyons C.A., Wessels G., Mansvelt E., Coetzer T.L.; RT "Band 3 Cape Town (E90K) causes severe hereditary spherocytosis in RT combination with band 3 Prague III."; RL Br. J. Haematol. 113:689-693(2001). RN [38] RP PHOSPHORYLATION SITES. RX MEDLINE=91152059; PubMed=1998697; DOI=10.1016/0005-2736(91)90291-F; RA Yannoukakos D., Vasseur C., Piau J.-P., Wajcman H., Bursaux E.; RT "Phosphorylation sites in human erythrocyte band 3 protein."; RL Biochim. Biophys. Acta 1061:253-266(1991). RN [39] RP STRUCTURE BY ELECTRON CRYO-MICROSCOPY. RX MEDLINE=93285092; PubMed=8508760; RA Wang D.N., Kuehlbrandt W., Sarabia V.E., Reithmeier R.A.F.; RT "Two-dimensional structure of the membrane domain of human band 3, the RT anion transport protein of the erythrocyte membrane."; RL EMBO J. 12:2233-2239(1993). RN [40] RP STRUCTURE BY ELECTRON CRYO-MICROSCOPY. RX MEDLINE=94320586; PubMed=8045253; RA Wang D.N., Sarabia V.E., Reithmeier R.A.F., Kuehlbrandt W.; RT "Three-dimensional map of the dimeric membrane domain of the human RT erythrocyte anion exchanger, Band 3."; RL EMBO J. 13:3230-3235(1994). RN [41] RP STRUCTURE BY NMR OF 1-16. RX MEDLINE=96118374; PubMed=8527430; RA Schneider M.L., Post C.B.; RT "Solution structure of a band 3 peptide inhibitor bound to aldolase: a RT proposed mechanism for regulating binding by tyrosine RT phosphorylation."; RL Biochemistry 34:16574-16584(1995). RN [42] RP STRUCTURE BY NMR OF 1-16. RX MEDLINE=98118173; PubMed=9454576; DOI=10.1021/bi971445b; RA Eisenmesser E.Z., Post C.B.; RT "Insights into tyrosine phosphorylation control of protein-protein RT association from the NMR structure of a band 3 peptide inhibitor bound RT to glyceraldehyde-3-phosphate dehydrogenase."; RL Biochemistry 37:867-877(1998). RN [43] RP STRUCTURE BY NMR OF 389-430. RX MEDLINE=98439044; PubMed=9765907; RA Chambers E.J., Askin D., Bloomberg G.B., Ring S.M., Tanner M.J.; RT "Studies on the structure of a transmembrane region and a cytoplasmic RT loop of the human red cell anion exchanger."; RL Biochem. Soc. Trans. 26:516-520(1998). RN [44] RP STRUCTURE BY NMR OF 405-424 AND 436-456. RX MEDLINE=94222092; PubMed=8168533; RA Gargaro A.R., Bloomberg G.B., Dempsey C.E., Murray M., Tanner M.J.A.; RT "The solution structures of the first and second transmembrane- RT spanning segments of band 3."; RL Eur. J. Biochem. 221:445-454(1994). RN [45] RP STRUCTURE BY NMR OF 803-835. RX MEDLINE=98376451; PubMed=9709005; DOI=10.1021/bi973158d; RA Askin D., Bloomberg G.B., Chambers E.J., Tanner M.J.; RT "NMR solution structure of a cytoplasmic surface loop of the human red RT cell anion transporter, band 3."; RL Biochemistry 37:11670-11678(1998). CC -!- FUNCTION: Band 3 is the major integral glycoprotein of the CC erythrocyte membrane. Band 3 has two functional domains. Its CC integral domain mediates a 1:1 exchange of inorganic anions across CC the membrane, whereas its cytoplasmic domain provides binding CC sites for cytoskeletal proteins, glycolytic enzymes, and CC hemoglobin. CC -!- SUBUNIT: A dimer in solution, it spans the membrane asymmetrically CC and appears to be tetrameric. CC -!- SUBCELLULAR LOCATION: Integral membrane protein. CC -!- TISSUE SPECIFICITY: Erythrocytes. CC -!- PTM: Phosphorylated on Tyr-8 and Tyr-21 most likely by SYK. PP1- CC resistant phosphorylation that precedes Tyr-359 and Tyr-904 CC phosphorylation. CC -!- PTM: Phosphorylated on Tyr-359 and Tyr-904 most likely by LYN. CC PP1-inhibited phosphorylation that follows Tyr-8 and Tyr-21 CC phosphorylation. CC -!- POLYMORPHISM: SLC4A1 is responsible for the Diego blood group CC system. The molecular basis of the Di(a)=Di1/Di(b)/Di2 blood group CC antigens is a single variation in position 854; Leu-854 CC corresponds to Di(a) and Pro-854 to Di(b). The molecular basis of CC the Wr(a)=Di3/Wr(b)/Di4 blood group antigens is a single variation CC in position 658; Lys-658 corresponds to Wr(a) and Glu-658 to CC Wr(b). The blood group antigens Wd(a)=Di5 (Waldner-type) has Met- CC 557; Rb(a)=Di6 has Leu-548 and WARR=Di7 has Ile-552. CC -!- DISEASE: Defects in SLC4A1 are a cause of hereditary CC elliptocytosis (HE) [MIM:109270, 166900, 130600]; also known as CC hereditary ovalocytosis (HO). It is a genetically heterogeneous, CC autosomal dominant disorder. It is characterized by variable CC hemolytic anemia and elliptical or oval red cell shape. CC Ovalocytosis/elliptocytosis due to SLC4A1 defects is rhesus- CC unliked (elliptocytosis 2 or EL2). It can also be referred to as CC elliptocytosis 4 (EL4). CC -!- DISEASE: Defects in SLC4A1 are a cause of hereditary spherocytosis CC (HS) [MIM:109270]. HS is a hematologic disorder leading to chronic CC hemolytic anemia and characterized by numerous abnormally shaped CC erythrocytes which are generally spheroidal. CC -!- DISEASE: Defects in SLC4A1 are a cause of familial distal renal CC tubular acidosis (dRTA) [MIM:179800]. This disease is CC characterized by reduced ability to acidify urine, variable CC hyperchloremic hypokalemic metabolic acidosis, nephrocalcinosis, CC and nephrolithiasis. Inheritance is generally autosomal dominant, CC but recessive forms have also been reported. CC -!- MISCELLANEOUS: Phenyl isothiocyanate inhibits anion transport in CC vitro. CC -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family. CC -!- DATABASE: NAME=Blood group antigen mutation database; CC NOTE=Diego (Di) blood group system; CC WWW="http://www.bioc.aecom.yu.edu/bgmut/diego.htm". CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M27819; AAA35514.1; -; mRNA. DR EMBL; X12609; CAA31128.1; -; mRNA. DR EMBL; S68680; AAC60608.2; -; mRNA. DR PIR; A36218; B3HU. DR PDB; 1BH7; NMR; @=803-835. DR PDB; 1BNX; NMR; A=409-430. DR PDB; 1BTQ; NMR; @=405-424. DR PDB; 1BTR; NMR; @=405-424. DR PDB; 1BTS; NMR; @=436-456. DR PDB; 1BTT; NMR; @=436-456. DR PDB; 1BZK; NMR; A=389-430. DR PDB; 1HYN; X-ray; P/Q/R/S=1-379. DR PDB; 3BTB; NMR; @=-. DR Ensembl; ENSG00000004939; Homo sapiens. DR HGNC; HGNC:11027; SLC4A1. DR MIM; 109270; -. DR MIM; 166900; -. DR MIM; 130600; -. DR MIM; 110500; -. DR MIM; 112010; -. DR MIM; 112050; -. DR MIM; 179800; -. DR GO; GO:0005887; C:integral to plasma membrane; TAS. DR GO; GO:0015380; F:anion exchanger activity; TAS. DR GO; GO:0008509; F:anion transporter activity; TAS. DR GO; GO:0006820; P:anion transport; TAS. DR GO; GO:0006873; P:cell ion homeostasis; TAS. DR InterPro; IPR001717; Anion_exchange. DR InterPro; IPR002977; Anion_exchngr_1. DR InterPro; IPR011531; HCO3_transpt. DR InterPro; IPR003020; HCO3_transpt_euk. DR PANTHER; PTHR11453:SF5; Anion_exchange; 1. DR PANTHER; PTHR11453; HCO3_transpt_euk; 1. DR Pfam; PF07565; Band_3_cyto; 1. DR Pfam; PF00955; HCO3_cotransp; 1. DR PRINTS; PR00165; ANIONEXCHNGR. DR PRINTS; PR01187; ANIONEXHNGR1. DR PRINTS; PR01231; HCO3TRNSPORT. DR TIGRFAMs; TIGR00834; ae; 1. DR PROSITE; PS00219; ANION_EXCHANGER_1; 1. DR PROSITE; PS00220; ANION_EXCHANGER_2; 1. KW 3D-structure; Acetylation; Anion exchange; Antigen; KW Blood group antigen; Direct protein sequencing; Disease mutation; KW Elliptocytosis; Glycoprotein; Hereditary hemolytic anemia; KW Ion transport; Lipoprotein; Membrane; Palmitate; Phosphorylation; KW Polymorphism; Transmembrane; Transport. FT TOPO_DOM 1 403 Cytoplasmic. FT TRANSMEM 404 424 Potential. FT TRANSMEM 437 456 Potential. FT TRANSMEM 460 479 Potential. FT TRANSMEM 491 510 Potential. FT TRANSMEM 523 541 Potential. FT TOPO_DOM 542 568 Exoplasmic loop (Potential). FT TRANSMEM 569 588 Potential. FT TOPO_DOM 589 603 Cytoplasmic (Potential). FT TRANSMEM 604 624 Potential. FT TOPO_DOM 625 660 Exoplasmic loop (Potential). FT TRANSMEM 661 680 Potential. FT TRANSMEM 699 719 Potential. FT TRANSMEM 763 780 Potential. FT TRANSMEM 785 806 Potential. FT TRANSMEM 844 865 Potential. FT REGION 404 911 Membrane (anion exchange). FT REGION 559 630 Involved in anion transport. FT SITE 590 590 Important for anion transport. FT SITE 681 681 Important for anion-proton cotransport. FT MOD_RES 1 1 N-acetylmethionine. FT MOD_RES 8 8 Phosphotyrosine. FT MOD_RES 21 21 Phosphotyrosine (partial). FT MOD_RES 29 29 Phosphoserine (by CK). FT MOD_RES 46 46 Phosphotyrosine (partial). FT MOD_RES 50 50 Phosphoserine (by CK). FT MOD_RES 359 359 Phosphotyrosine. FT MOD_RES 904 904 Phosphotyrosine. FT LIPID 843 843 S-palmitoyl cysteine. FT CARBOHYD 642 642 N-linked (GlcNAc...) (Probable). FT VARIANT 38 38 D -> A (in dbSNP:5035). FT /FTId=VAR_014612. FT VARIANT 40 40 E -> K (in hemolytic anemia; Montefiore). FT /FTId=VAR_000798. FT VARIANT 56 56 K -> E (in Memphis; dbSNP:5036). FT /FTId=VAR_000799. FT VARIANT 90 90 E -> K (in HS; Cape Town). FT /FTId=VAR_013784. FT VARIANT 112 112 R -> S (in dbSNP:5037). FT /FTId=VAR_014613. FT VARIANT 130 130 G -> R (in HS; Fukoka). FT /FTId=VAR_013785. FT VARIANT 147 147 P -> S (in HS; Mondego). FT /FTId=VAR_013786. FT VARIANT 285 285 A -> D (in HS; Boston). FT /FTId=VAR_013787. FT VARIANT 327 327 P -> R (in HS; Tuscaloosa). FT /FTId=VAR_000800. FT VARIANT 400 408 Missing (in HE). FT /FTId=VAR_000801. FT VARIANT 432 432 R -> W (in ELO antigen). FT /FTId=VAR_013788. FT VARIANT 442 442 I -> F (in dbSNP:5018). FT /FTId=VAR_014614. FT VARIANT 455 455 G -> E (in HS; Benesov). FT /FTId=VAR_013789. FT VARIANT 480 480 E -> K (in FR(a) antigen). FT /FTId=VAR_013790. FT VARIANT 488 488 V -> M (in HS; Coimbra). FT /FTId=VAR_013791. FT VARIANT 490 490 R -> C (in HS; Bicetre I). FT /FTId=VAR_013792. FT VARIANT 518 518 R -> C (in HS; Dresden). FT /FTId=VAR_000802. FT VARIANT 548 548 P -> L (in RB(A) antigen). FT /FTId=VAR_000803. FT VARIANT 551 551 K -> N (in TR(A) antigen). FT /FTId=VAR_013793. FT VARIANT 552 552 T -> I (in WARR antigen). FT /FTId=VAR_000804. FT VARIANT 555 555 Y -> H (in VG(a) antigen). FT /FTId=VAR_013794. FT VARIANT 557 557 V -> M (in WD(a) antigen). FT /FTId=VAR_000805. FT VARIANT 561 561 P -> S (in BOW antigen). FT /FTId=VAR_013795. FT VARIANT 565 565 G -> A (in WU antigen). FT /FTId=VAR_013796. FT VARIANT 566 566 P -> A (in KREP antigen). FT /FTId=VAR_013797. FT VARIANT 566 566 P -> S (in PN(a) antigen). FT /FTId=VAR_013798. FT VARIANT 569 569 N -> K (in BP(a) antigen). FT /FTId=VAR_013799. FT VARIANT 586 586 M -> L (in dbSNP:5019). FT /FTId=VAR_014615. FT VARIANT 589 589 R -> C (in dRTA; autosomal dominant form; FT reduced red cell sulfate transport and FT altered glycosylation of the red cell FT band 3 N-glycan chain). FT /FTId=VAR_015104. FT VARIANT 589 589 R -> H (in dRTA; autosomal dominant FT form). FT /FTId=VAR_015105. FT VARIANT 589 589 R -> S (in dRTA; autosomal dominant FT form). FT /FTId=VAR_015106. FT VARIANT 613 613 S -> F (in dRTA; autosomal dominant form; FT markedly increased red cell sulfate FT transport but almost normal red cell FT iodide transport). FT /FTId=VAR_015107. FT VARIANT 646 646 R -> Q (in SW(a) antigen). FT /FTId=VAR_013800. FT VARIANT 646 646 R -> W (in SW(!) antigen). FT /FTId=VAR_013801. FT VARIANT 656 656 R -> C (in HG(a) antigen). FT /FTId=VAR_013802. FT VARIANT 656 656 R -> H (in MO(a) antigen). FT /FTId=VAR_013803. FT VARIANT 658 658 E -> K (in WR(a) antigen). FT /FTId=VAR_000806. FT VARIANT 663 663 Missing (in HS; Osnabruck II). FT /FTId=VAR_000807. FT VARIANT 688 688 I -> V (in dbSNP:5022). FT /FTId=VAR_014616. FT VARIANT 690 690 S -> G (in dbSNP:5023). FT /FTId=VAR_014617. FT VARIANT 701 701 G -> D (in dRTA; autosomal recessive FT form). FT /FTId=VAR_015171. FT VARIANT 707 707 L -> P (in HS; Most). FT /FTId=VAR_013804. FT VARIANT 714 714 G -> R (in HS; Okinawa). FT /FTId=VAR_013805. FT VARIANT 760 760 R -> Q (in HS; Prague II). FT /FTId=VAR_013806. FT VARIANT 760 760 R -> W (in HS; Hradec Kralove). FT /FTId=VAR_013807. FT VARIANT 771 771 G -> D (in HS; Chur). FT /FTId=VAR_013808. FT VARIANT 783 783 I -> N (in HS; Napoli II). FT /FTId=VAR_013809. FT VARIANT 808 808 R -> C (in HS; Jablonec). FT /FTId=VAR_013810. FT VARIANT 808 808 R -> H (in HS; Nara). FT /FTId=VAR_013811. FT VARIANT 832 832 R -> H (in dbSNP:5025). FT /FTId=VAR_014618. FT VARIANT 834 834 H -> P (in HS; Birmingham). FT /FTId=VAR_013812. FT VARIANT 837 837 T -> A (in HS; Tokyo). FT /FTId=VAR_013813. FT VARIANT 837 837 T -> M (in HS; Philadelphia). FT /FTId=VAR_013814. FT VARIANT 850 850 Missing (in dRTA; autosomal recessive FT form). FT /FTId=VAR_015109. FT VARIANT 854 854 P -> L (in Di(a)/Memphis-II antigen; FT dbSNP:2285644). FT /FTId=VAR_000808. FT VARIANT 858 858 A -> D (in dRTA; autosomal dominant FT form). FT /FTId=VAR_015108. FT VARIANT 862 862 V -> I (in dbSNP:5026). FT /FTId=VAR_014619. FT VARIANT 868 868 P -> L (in HS; HT). FT /FTId=VAR_013815. FT VARIANT 870 870 R -> W (in HS; Prague III). FT /FTId=VAR_013816. FT CONFLICT 11 11 M -> D (in Ref. 4). FT CONFLICT 68 68 E -> EE (in Ref. 4). FT STRAND 58 67 FT TURN 68 70 FT STRAND 73 88 FT TURN 90 91 FT STRAND 92 92 FT STRAND 94 94 FT STRAND 98 98 FT STRAND 102 102 FT HELIX 104 115 FT TURN 116 116 FT STRAND 118 123 FT STRAND 127 127 FT HELIX 128 141 FT TURN 142 143 FT STRAND 144 145 FT HELIX 147 157 FT TURN 158 158 FT STRAND 159 159 FT STRAND 161 162 FT HELIX 164 170 FT TURN 171 171 FT STRAND 173 175 FT STRAND 177 178 FT TURN 180 181 FT STRAND 182 182 FT STRAND 184 185 FT STRAND 188 189 FT HELIX 195 200 FT STRAND 204 205 FT STRAND 207 208 FT TURN 210 211 FT HELIX 212 219 FT STRAND 220 220 FT TURN 222 223 FT STRAND 226 234 FT TURN 235 236 FT STRAND 238 239 FT STRAND 241 251 FT TURN 254 255 FT STRAND 256 258 FT STRAND 262 270 FT TURN 274 275 FT HELIX 278 289 FT TURN 290 290 FT STRAND 291 291 FT HELIX 292 300 FT STRAND 302 303 FT HELIX 304 316 FT TURN 317 317 FT STRAND 319 321 FT STRAND 326 326 FT HELIX 328 333 FT STRAND 334 334 FT HELIX 335 346 FT TURN 347 347 FT STRAND 391 391 FT TURN 392 394 FT HELIX 395 422 FT STRAND 423 424 FT STRAND 426 427 FT HELIX 437 453 FT TURN 454 455 FT TURN 806 809 FT STRAND 816 817 FT TURN 827 828 FT HELIX 829 833 FT TURN 834 834 SQ SEQUENCE 911 AA; 101792 MW; 35EC3EE7AFF27D2F CRC64; MEELQDDYED MMEENLEQEE YEDPDIPESQ MEEPAAHDTE ATATDYHTTS HPGTHKVYVE LQELVMDEKN QELRWMEAAR WVQLEENLGE NGAWGRPHLS HLTFWSLLEL RRVFTKGTVL LDLQETSLAG VANQLLDRFI FEDQIRPQDR EELLRALLLK HSHAGELEAL GGVKPAVLTR SGDPSQPLLP QHSSLETQLF CEQGDGGTEG HSPSGILEKI PPDSEATLVL VGRADFLEQP VLGFVRLQEA AELEAVELPV PIRFLFVLLG PEAPHIDYTQ LGRAAATLMS ERVFRIDAYM AQSRGELLHS LEGFLDCSLV LPPTDAPSEQ ALLSLVPVQR ELLRRRYQSS PAKPDSSFYK GLDLNGGPDD PLQQTGQLFG GLVRDIRRRY PYYLSDITDA FSPQVLAAVI FIYFAALSPA ITFGGLLGEK TRNQMGVSEL LISTAVQGIL FALLGAQPLL VVGFSGPLLV FEEAFFSFCE TNGLEYIVGR VWIGFWLILL VVLVVAFEGS FLVRFISRYT QEIFSFLISL IFIYETFSKL IKIFQDHPLQ KTYNYNVLMV PKPQGPLPNT ALLSLVLMAG TFFFAMMLRK FKNSSYFPGK LRRVIGDFGV PISILIMVLV DFFIQDTYTQ KLSVPDGFKV SNSSARGWVI HPLGLRSEFP IWMMFASALP ALLVFILIFL ESQITTLIVS KPERKMVKGS GFHLDLLLVV GMGGVAALFG MPWLSATTVR SVTHANALTV MGKASTPGAA AQIQEVKEQR ISGLLVAVLV GLSILMEPIL SRIPLAVLFG IFLYMGVTSL SGIQLFDRIL LLFKPPKYHP DVPYVKRVKT WRMHLFTGIQ IICLAVLWVV KSTPASLALP FVLILTVPLR RVLLPLIFRN VELQCLDADD AKATFDEEEG RDEYDEVAMP V //