ID B3AT_HUMAN Reviewed; 911 AA. AC P02730; G4V2I6; P78487; Q1ZZ45; Q4KKW9; Q4VB84; Q9UCY7; Q9UDJ1; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 3. DT 27-MAR-2024, entry version 274. DE RecName: Full=Band 3 anion transport protein {ECO:0000305}; DE AltName: Full=Anion exchange protein 1; DE Short=AE 1; DE Short=Anion exchanger 1; DE AltName: Full=Solute carrier family 4 member 1; DE AltName: CD_antigen=CD233; GN Name=SLC4A1 {ECO:0000312|HGNC:HGNC:11027}; Synonyms=AE1, DI, EPB3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Blood; RX PubMed=3223947; DOI=10.1042/bj2560703; RA Tanner M.J.A., Martin P.G., High S.; RT "The complete amino acid sequence of the human erythrocyte membrane anion- RT transport protein deduced from the cDNA sequence."; RL Biochem. J. 256:703-712(1988). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2594752; DOI=10.1073/pnas.86.23.9089; 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 [3] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-38. RX PubMed=16252102; DOI=10.1007/s00467-005-2061-z; RA Choo K.E., Nicoli T.K., Bruce L.J., Tanner M.J., Ruiz-Linares A., RA Wrong O.M.; RT "Recessive distal renal tubular acidosis in Sarawak caused by AE1 RT mutations."; RL Pediatr. Nephrol. 21:212-217(2006). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Blood; RA Hsu K., Huang S.-Y., Chi N., Lin M.; RT "Novel anion exchanger-1 expression in Southeast Asian populations."; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-38; GLU-56; LYS-508 AND RP ILE-862. RG SeattleSNPs variation discovery resource; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-27. RC TISSUE=Cerebellum; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP PROTEIN SEQUENCE OF 1-199; 220-292 AND 347-370, AND ACETYLATION AT MET-1. RX 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 protein RT band 3. Comparison with its sequence in the mouse."; RL Biochim. Biophys. Acta 998:43-49(1989). RN [9] RP PROTEIN SEQUENCE OF 1-201. RX PubMed=6345535; DOI=10.1016/s0021-9258(20)82016-x; 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 [10] RP PROTEIN SEQUENCE OF 1-3. RX PubMed=701248; DOI=10.1016/s0021-9258(17)34491-5; RA Drickamer L.K.; RT "Orientation of the band 3 polypeptide from human erythrocyte membranes. RT Identification of NH2-terminal sequence and site of carbohydrate RT attachment."; RL J. Biol. Chem. 253:7242-7248(1978). RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] OF 66-180 (ISOFORM 2), SUBCELLULAR LOCATION, AND RP TISSUE SPECIFICITY. RX PubMed=7506871; DOI=10.1152/ajprenal.1993.265.6.f813; RA Kollert-Jons A., Wagner S., Hubner S., Appelhans H., Drenckhahn D.; RT "Anion exchanger 1 in human kidney and oncocytoma differs from erythroid RT AE1 in its NH2 terminus."; RL Am. J. Physiol. 265:F813-F821(1993). RN [12] RP PROTEIN SEQUENCE OF 361-372; 390-399; 604-613; 632-639; 647-656; 699-729; RP 731-743; 761-781 AND 818-826, AND SYNTHESIS OF 646-656 AND 817-827. RX PubMed=1527044; DOI=10.1016/s0021-9258(18)41763-2; RA Kang D., Okubo K., Hamasaki N., Kuroda N., Shiraki H.; RT "A structural study of the membrane domain of band 3 by tryptic digestion. RT Conformational change of band 3 in situ induced by alkali treatment."; RL J. Biol. Chem. 267:19211-19217(1992). RN [13] RP PROTEIN SEQUENCE OF 559-630. RX PubMed=6615451; DOI=10.1042/bj2130577; 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 [14] RP PROTEIN SEQUENCE OF 665-688, AND ROLE OF GLU-681. RX PubMed=1352774; DOI=10.1016/s0021-9258(19)49664-6; RA Jennings M.L., Smith J.S.; RT "Anion-proton cotransport through the human red blood cell band 3 protein. RT Role of glutamate 681."; RL J. Biol. Chem. 267:13964-13971(1992). RN [15] RP NUCLEOTIDE SEQUENCE [MRNA] OF 757-778, AND VARIANT SPH4 ASP-771. RX PubMed=8547122; DOI=10.1111/j.1365-2141.1995.tb05393.x; RA Maillet P., Vallier A., Reinhart W.H., Wyss E.J., Ott P., Texier P., RA Baklouti F., Tanner M.J.A., 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 [16] RP PROTEIN SEQUENCE OF 834-911. RX PubMed=3372523; DOI=10.1016/s0021-9258(18)68468-6; RA Kawano Y., Okubo K., Tokunaga F., Miyata T., Iwanaga S., Hamasaki N.; RT "Localization of the pyridoxal phosphate binding site at the COOH-terminal RT region of erythrocyte band 3 protein."; RL J. Biol. Chem. 263:8232-8238(1988). RN [17] RP INTERACTION WITH P.FALCIPARUM FBPA (MICROBIAL INFECTION), AND TISSUE RP SPECIFICITY. RX PubMed=2204832; DOI=10.1016/0166-6851(90)90189-s; RA Doebeli H., Trzeciak A., Gillessen D., Matile H., Srivastava I.K., RA Perrin L.H., Jakob P.E., Certa U.; RT "Expression, purification, biochemical characterization and inhibition of RT recombinant Plasmodium falciparum aldolase."; RL Mol. Biochem. Parasitol. 41:259-268(1990). RN [18] RP PHOSPHORYLATION AT TYR-8; TYR-21 AND TYR-46. RX 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 [19] RP PALMITOYLATION AT CYS-843. RX PubMed=1885574; DOI=10.1016/s0021-9258(18)55315-1; RA Okubo K., Hamasaki N., Hara K., Kageura M.; RT "Palmitoylation of cysteine 69 from the COOH-terminal of band 3 protein in RT the human erythrocyte membrane. Acylation occurs in the middle of the RT consensus sequence of F--I-IICLAVL found in band 3 protein and G2 protein RT of Rift Valley fever virus."; RL J. Biol. Chem. 266:16420-16424(1991). RN [20] RP INTERACTION WITH ANK1. RX PubMed=7665627; DOI=10.1074/jbc.270.37.22050; RA Michaely P., Bennett V.; RT "The ANK repeats of erythrocyte ankyrin form two distinct but cooperative RT binding sites for the erythrocyte anion exchanger."; RL J. Biol. Chem. 270:22050-22057(1995). RN [21] RP GLYCOSYLATION AT ASN-642. RX PubMed=10861210; DOI=10.1042/0264-6021:3490051; RA Li J., Quilty J., Popov M., Reithmeier R.A.; RT "Processing of N-linked oligosaccharide depends on its location in the RT anion exchanger, AE1, membrane glycoprotein."; RL Biochem. J. 349:51-57(2000). RN [22] RP PHOSPHORYLATION AT TYR-8; TYR-21; TYR-359 AND TYR-904. RX 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 [23] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH P.FALCIPARUM MSP1 RP (MICROBIAL INFECTION). RX PubMed=12692305; DOI=10.1073/pnas.0834959100; RA Goel V.K., Li X., Chen H., Liu S.C., Chishti A.H., Oh S.S.; RT "Band 3 is a host receptor binding merozoite surface protein 1 during the RT Plasmodium falciparum invasion of erythrocytes."; RL Proc. Natl. Acad. Sci. U.S.A. 100:5164-5169(2003). RN [24] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH P.FALCIPARUM MSP9 RP (MICROBIAL INFECTION). RX PubMed=14630931; DOI=10.1074/jbc.m308716200; RA Li X., Chen H., Oo T.H., Daly T.M., Bergman L.W., Liu S.C., Chishti A.H., RA Oh S.S.; RT "A co-ligand complex anchors Plasmodium falciparum merozoites to the RT erythrocyte invasion receptor band 3."; RL J. Biol. Chem. 279:5765-5771(2004). RN [25] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [26] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH STOM, AND RP SUBUNIT. RX PubMed=23219802; DOI=10.1016/j.bbamem.2012.11.030; RA Rungaldier S., Oberwagner W., Salzer U., Csaszar E., Prohaska R.; RT "Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in RT human erythrocyte membrane domains."; RL Biochim. Biophys. Acta 1828:956-966(2013). RN [27] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [28] RP INTERACTION WITH TMEM139 (ISOFORM 2). RX PubMed=26049106; DOI=10.1016/j.bbrc.2015.05.128; RA Nuiplot N.O., Junking M., Duangtum N., Khunchai S., Sawasdee N., RA Yenchitsomanus P.T., Akkarapatumwong V.; RT "Transmembrane protein 139 (TMEM139) interacts with human kidney isoform of RT anion exchanger 1 (kAE1)."; RL Biochem. Biophys. Res. Commun. 463:706-711(2015). RN [29] RP FUNCTION, TRANSPORTER ACTIVITY, AND INTERACTION WITH STOM. RX PubMed=28387307; DOI=10.1038/srep46170; RA Genetet S., Desrames A., Chouali Y., Ripoche P., Lopez C., RA Mouro-Chanteloup I.; RT "Stomatin modulates the activity of the Anion Exchanger 1 (AE1, SLC4A1)."; RL Sci. Rep. 7:46170-46170(2017). RN [30] RP STRUCTURE BY ELECTRON MICROSCOPY. RX PubMed=8508760; DOI=10.1002/j.1460-2075.1993.tb05876.x; 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 [31] RP STRUCTURE BY ELECTRON MICROSCOPY. RX PubMed=8045253; DOI=10.1002/j.1460-2075.1994.tb06624.x; 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 [32] {ECO:0007744|PDB:1BTQ, ECO:0007744|PDB:1BTR, ECO:0007744|PDB:1BTS, ECO:0007744|PDB:1BTT} RP STRUCTURE BY NMR OF 405-424 AND 436-456. RX PubMed=8168533; DOI=10.1111/j.1432-1033.1994.tb18757.x; 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-spanning RT segments of band 3."; RL Eur. J. Biochem. 221:445-454(1994). RN [33] {ECO:0007744|PDB:2BTA, ECO:0007744|PDB:2BTB} RP STRUCTURE BY NMR OF 1-16. RX PubMed=8527430; DOI=10.1021/bi00051a005; 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 phosphorylation."; RL Biochemistry 34:16574-16584(1995). RN [34] {ECO:0007744|PDB:3BTB} RP STRUCTURE BY NMR OF 1-16. RX 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 to RT glyceraldehyde-3-phosphate dehydrogenase."; RL Biochemistry 37:867-877(1998). RN [35] {ECO:0007744|PDB:1BNX} RP STRUCTURE BY NMR OF 389-430. RX PubMed=9765907; DOI=10.1042/bst0260516; 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 loop RT of the human red cell anion exchanger."; RL Biochem. Soc. Trans. 26:516-520(1998). RN [36] {ECO:0007744|PDB:1BH7} RP STRUCTURE BY NMR OF 803-835. RX 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 cell RT anion transporter, band 3."; RL Biochemistry 37:11670-11678(1998). RN [37] {ECO:0007744|PDB:1HYN} RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-379, AND SUBUNIT. RX PubMed=11049968; RA Zhang D., Kiyatkin A., Bolin J.T., Low P.S.; RT "Crystallographic structure and functional interpretation of the RT cytoplasmic domain of erythrocyte membrane band 3."; RL Blood 96:2925-2933(2000). RN [38] {ECO:0007744|PDB:4KY9} RP X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS) OF 51-356, FUNCTION, SUBCELLULAR RP LOCATION, GLYCOSYLATION AT ASN-642, MUTAGENESIS OF GLU-85; ARG-283; ASN-642 RP AND GLU-681, CHARACTERIZATION OF VARIANT ACANTHOCYTOSIS LEU-868, AND RP TRANSPORTER ACTIVITY. RX PubMed=24121512; DOI=10.1074/jbc.m113.511865; RA Shnitsar V., Li J., Li X., Calmettes C., Basu A., Casey J.R., Moraes T.F., RA Reithmeier R.A.; RT "A substrate access tunnel in the cytosolic domain is not an essential RT feature of the solute carrier 4 (SLC4) family of bicarbonate RT transporters."; RL J. Biol. Chem. 288:33848-33860(2013). RN [39] {ECO:0007744|PDB:4YZF} RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS), TISSUE SPECIFICITY, SUBCELLULAR RP LOCATION, TOPOLOGY, AND GLYCOSYLATION. RX PubMed=26542571; DOI=10.1126/science.aaa4335; RA Arakawa T., Kobayashi-Yurugi T., Alguel Y., Iwanari H., Hatae H., Iwata M., RA Abe Y., Hino T., Ikeda-Suno C., Kuma H., Kang D., Murata T., Hamakubo T., RA Cameron A.D., Kobayashi T., Hamasaki N., Iwata S.; RT "Crystal structure of the anion exchanger domain of human erythrocyte band RT 3."; RL Science 350:680-684(2015). RN [40] RP STRUCTURE BY ELECTRON MICROSCOPY (2.30 ANGSTROMS), FUNCTION, SUBUNIT, RP ANKYRIN-1 COMPLEX IDENTIFICATION, GLYCOSYLATION AT ASN-642, AND INTERACTION RP WITH GYPA; EPB42 AND ANK1. RX PubMed=35835865; DOI=10.1038/s41594-022-00792-w; RA Vallese F., Kim K., Yen L.Y., Johnston J.D., Noble A.J., Cali T., RA Clarke O.B.; RT "Architecture of the human erythrocyte ankyrin-1 complex."; RL Nat. Struct. Mol. Biol. 29:706-718(2022). RN [41] RP VARIANT MEMPHIS GLU-56. RX 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): characterization RT of the structural modification (Lys 56-->Glu) by protein chemistry RT methods."; RL Blood 78:1117-1120(1991). RN [42] RP VARIANT SAO 400-ALA--ALA-408 DEL, AND VARIANT MEMPHIS GLU-56. RX PubMed=1722314; DOI=10.1073/pnas.88.24.11022; 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 Asian RT ovalocytosis."; RL Proc. Natl. Acad. Sci. U.S.A. 88:11022-11026(1991). RN [43] RP VARIANT SPH4 ARG-327. RX PubMed=1378323; RA Jarolim P., Palek J., Rubin H.L., Prchal J.T., Korsgren C., Cohen C.M.; RT "Band 3 Tuscaloosa: Pro-327-->Arg substitution in the cytoplasmic domain of RT erythrocyte band 3 protein associated with spherocytic hemolytic anemia and RT partial deficiency of protein 4.2."; RL Blood 80:523-529(1992). RN [44] RP VARIANT SAO 400-ALA--ALA-408 DEL, CHARACTERIZATION OF VARIANT SAO RP 400-ALA--ALA-408 DEL, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RX PubMed=1538405; DOI=10.1016/0022-2836(92)90254-h; 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 ovalocytosis."; RL J. Mol. Biol. 223:949-958(1992). RN [45] RP VARIANT ACANTHOCYTOSIS LEU-868. RX PubMed=8343110; DOI=10.1042/bj2930317; RA Bruce L.J., Kay M.M., Lawrence C., Tanner M.J.; RT "Band 3 HT, a human red-cell variant associated with acanthocytosis and RT increased anion transport, carries the mutation Pro-868-->Leu in the RT membrane domain of band 3."; RL Biochem. J. 293:317-320(1993). RN [46] RP VARIANT LYS-40. RX PubMed=8471774; RA Rybicki A.C., Qiu J.J.H., Musto S., Rosen N.L., Nagel R.L., Schwartz R.S.; RT "Human erythrocyte protein 4.2 deficiency associated with hemolytic anemia RT and a homozygous 40 glutamic acid-->lysine substitution in the cytoplasmic RT domain of band 3 (band 3Montefiore)."; RL Blood 81:2155-2165(1993). RN [47] RP VARIANTS BLOOD GROUP DI(A)/MEMPHIS-II GLU-56 AND LEU-854. RX PubMed=8206915; DOI=10.1016/s0021-9258(17)33986-8; RA Bruce L.J., Anstee D.J., Spring F.A., Tanner M.J.; RT "Band 3 Memphis variant II. Altered stilbene disulfonate binding and the RT Diego (Dia) blood group antigen are associated with the human erythrocyte RT band 3 mutation Pro-854-->Leu."; RL J. Biol. Chem. 269:16155-16158(1994). RN [48] RP VARIANT BLOOD GROUP WR(A) LYS-658. RX PubMed=7812009; RA Bruce L.J., Ring S.M., Anstee D.J., Reid M.E., Wilkinson S., Tanner M.J.; RT "Changes in the blood group Wright antigens are associated with a mutation RT at amino acid 658 in human erythrocyte band 3: a site of interaction RT between band 3 and glycophorin A under certain conditions."; RL Blood 85:541-547(1995). RN [49] RP VARIANTS SPH4 GLN-760; TRP-760; CYS-808 AND TRP-870. RX PubMed=7530501; RA Jarolim P., Rubin H.L., Brabec V., Chrobak L., Zolotarev A.S., Alper S.L., RA Brugnara C., Wichterle H., Palek J.; RT "Mutations of conserved arginines in the membrane domain of erythroid band RT 3 lead to a decrease in membrane-associated band 3 and to the phenotype of RT hereditary spherocytosis."; RL Blood 85:634-640(1995). RN [50] RP VARIANTS SPH4 ASP-285; GLU-455; PRO-707; PRO-834 AND MET-837. RX PubMed=8943874; RA Jarolim P., Murray J.L., Rubin H.L., Taylor W.M., Prchal J.T., Ballas S.K., RA Snyder L.M., Chrobak L., Melrose W.D., Brabec V., 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 [51] RP VARIANTS SPH4 CYS-518 AND MET-663 DEL, AND VARIANT LYS-40. RX PubMed=8640229; DOI=10.1038/ng0696-214; RA Eber S.W., Gonzalez J.M., Lux M.L., Scarpa A.L., Tse W.T., Dornwell M., RA Herbers J., Kugler W., Oezcan R., Pekrun A., Gallagher P.G., Schroeter W., RA Forget B.G., Lux S.E.; RT "Ankyrin-1 mutations are a major cause of dominant and recessive hereditary RT spherocytosis."; RL Nat. Genet. 13:214-218(1996). RN [52] RP VARIANTS SPH4 SER-147 AND MET-488. RX 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 [53] RP VARIANT SPH4 ASN-783, AND VARIANTS ALA-38 AND MET-73. RX PubMed=9012689; DOI=10.1046/j.1365-2141.1997.8732504.x; RA Miraglia del Giudice E., Vallier A., Maillet P., Perrotta S., Cutillo S., RA Iolascon A., Tanner M.J., Delaunay J., Alloisio N.; RT "Novel band 3 variants (bands 3 Foggia, Napoli I and Napoli II) associated RT with hereditary spherocytosis and band 3 deficiency: status of the D38A RT polymorphism within the EPB3 locus."; RL Br. J. Haematol. 96:70-76(1997). RN [54] RP VARIANTS SPH4 CYS-490 AND MET-837. RX PubMed=9233560; 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 [55] RP ERRATUM OF PUBMED:9233560. RA Dhermy D., Galand C., Bournier O., Boulanger L., Cynober T., RA Schismanoff P.O., Bursaux E., Tchernia G., Boivin P., Garbarz M.; RL Br. J. Haematol. 99:474-474(1997). RN [56] RP VARIANTS DRTA1 CYS-589; HIS-589 AND PHE-613. RX PubMed=9312167; DOI=10.1172/jci119694; RA Bruce L.J., Cope D.L., Jones G.K., Schofield A.E., Burley M., Povey S., RA Unwin R.J., Wrong O., Tanner M.J.; RT "Familial distal renal tubular acidosis is associated with mutations in the RT red cell anion exchanger (Band 3, AE1) gene."; RL J. Clin. Invest. 100:1693-1707(1997). RN [57] RP VARIANTS BLOOD GROUPS RB(A); TR(A) AND WD(A). RX PubMed=9191821; 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 [58] RP VARIANT SPH4 ALA-837. RX 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 protein RT associated with spherocytic hemolysis."; RL Acta Haematol. 100:200-203(1998). RN [59] RP VARIANTS BLOOD GROUPS BOW; BP(A); ELO; HG(A); MO(A); VG(A) AND WU. RX 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 by RT erythrocyte band 3 protein."; RL Blood 92:4836-4843(1998). RN [60] RP VARIANT DRTA4 ASP-701. RX PubMed=9854053; DOI=10.1172/jci4836; 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-of- RT function is rescued by glycophorin A."; RL J. Clin. Invest. 102:2173-2179(1998). RN [61] RP VARIANTS DRTA1 HIS-589 AND SER-589. RX PubMed=9600966; DOI=10.1073/pnas.95.11.6337; RA Karet F.E., Gainza F.J., Gyory A.Z., Unwin R.J., Wrong O., Tanner M.J.A., RA Nayir A., Alpay H., Santos F., Hulton S.A., Bakkaloglu A., Ozen S., RA Cunningham M.J., di Pietro A., Walker W.G., Lifton R.P.; RT "Mutations in the chloride-bicarbonate exchanger gene AE1 cause autosomal RT dominant but not autosomal recessive distal renal tubular acidosis."; RL Proc. Natl. Acad. Sci. U.S.A. 95:6337-6342(1998). RN [62] RP VARIANTS BLOOD GROUP WU. RX PubMed=9709782; 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 the Wu RT blood group polymorphism."; RL Transfusion 38:745-748(1998). RN [63] RP VARIANT SPH4 HIS-490. RX PubMed=10580570; DOI=10.1111/j.1600-0609.1999.tb01141.x; RA Lima P.R.M., Sales T.S.I., Costa F.F., Saad S.T.O.; RT "Arginine 490 is a hot spot for mutation in the band 3 gene in hereditary RT spherocytosis."; RL Eur. J. Haematol. 63:360-361(1999). RN [64] RP VARIANTS DRTA4 ASP-701 AND VAL-850 DEL, VARIANT DRTA1 ASP-858, FUNCTION, RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND TRANSPORTER ACTIVITY. RX PubMed=10926824; DOI=10.1042/bj3500041; 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 ovalocytosis RT in Malaysia and Papua New Guinea: loss of up to 95% band 3 transport in red RT cells."; RL Biochem. J. 350:41-51(2000). RN [65] RP VARIANT SPH4 MET-488. RX PubMed=10942416; RA Ribeiro M.L., Alloisio N., Almeida H., Gomes C., Texier P., Lemos C., RA Mimoso G., Morle L., Bey-Cabet F., Rudigoz R.-C., Delaunay J., RA Tamagnini G.; RT "Severe hereditary spherocytosis and distal renal tubular acidosis RT associated with the total absence of band 3."; RL Blood 96:1602-1604(2000). RN [66] RP VARIANTS SPH4 ARG-130; ARG-455; ARG-714; TRP-760; GLN-760; HIS-808; ARG-837 RP AND MET-837, AND VARIANTS ALA-38; GLU-56; ASP-72 AND LEU-854. RX PubMed=10745622; RA Yawata Y., Kanzaki A., Yawata A., Doerfler W., Oezcan R., Eber S.W.; RT "Characteristic features of the genotype and phenotype of hereditary RT spherocytosis in the Japanese population."; RL Int. J. Hematol. 71:118-135(2000). RN [67] RP CHARACTERIZATION OF VARIANTS PRO-707; GLN-760; TRP-760; CYS-808; PRO-834; RP MET-837 AND TRP-870. RX PubMed=11208088; DOI=10.1034/j.1600-0854.2000.011208.x; RA Quilty J.A., Reithmeier R.A.; RT "Trafficking and folding defects in hereditary spherocytosis mutants of the RT human red cell anion exchanger."; RL Traffic 1:987-998(2000). RN [68] RP VARIANTS BLOOD GROUP NFLD+ ASP-429 AND ALA-561, AND VARIANT BLOOD GROUP RP BOW+ SER-561. RX PubMed=10738034; DOI=10.1046/j.1537-2995.2000.40030325.x; RA McManus K., Pongoski J., Coghlan G., Zelinski T.; RT "Amino acid substitutions in human erythroid protein band 3 account for the RT low-incidence antigens NFLD and BOW."; RL Transfusion 40:325-329(2000). RN [69] RP VARIANT BLOOD GROUP FR(A+) LYS-480. RX PubMed=11061863; DOI=10.1046/j.1537-2995.2000.40101246.x; RA McManus K., Lupe K., Coghlan G., Zelinski T.; RT "An amino acid substitution in the putative second extracellular loop of RT RBC band 3 accounts for the Froese blood group polymorphism."; RL Transfusion 40:1246-1249(2000). RN [70] RP VARIANTS BLOOD GROUP SW(A+) GLN-646 AND TRP-646. RX 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 [71] RP VARIANTS SPH4 LYS-90 AND TRP-870. RX PubMed=11380459; 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 [72] RP VARIANT DRTA4 HIS-602, AND VARIANTS DRTA-NRC ASP-701 AND PRO-773. RX PubMed=15211439; DOI=10.1053/j.ajkd.2004.03.033; RA Sritippayawan S., Sumboonnanonda A., Vasuvattakul S., Keskanokwong T., RA Sawasdee N., Paemanee A., Thuwajit P., Wilairat P., Nimmannit S., RA Malasit P., Yenchitsomanus P.T.; RT "Novel compound heterozygous SLC4A1 mutations in Thai patients with RT autosomal recessive distal renal tubular acidosis."; RL Am. J. Kidney Dis. 44:64-70(2004). RN [73] RP VARIANT DRTA1 ARG-609, FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF RP VARIANT DRTA1 ARG-609, AND TRANSPORTER ACTIVITY. RX PubMed=14734552; DOI=10.1074/jbc.m400188200; RA Rungroj N., Devonald M.A.J., Cuthbert A.W., Reimann F., Akkarapatumwong V., RA Yenchitsomanus P.-T., Bennett W.M., Karet F.E.; RT "A novel missense mutation in AE1 causing autosomal dominant distal renal RT tubular acidosis retains normal transport function but is mistargeted in RT polarized epithelial cells."; RL J. Biol. Chem. 279:13833-13838(2004). RN [74] RP VARIANT SPH4 LYS-663. RX PubMed=15813913; DOI=10.1111/j.1600-0609.2004.00405.x; RA Lima P.R.M., Baratti M.O., Chiattone M.L., Costa F.F., Saad S.T.O.; RT "Band 3Tambau: a de novo mutation in the AE1 gene associated with RT hereditary spherocytosis. Implications for anion exchange and insertion RT into the red blood cell membrane."; RL Eur. J. Haematol. 74:396-401(2005). RN [75] RP INVOLVEMENT IN CHC AND SPH4, VARIANT GLU-56, VARIANTS CHC PRO-687; PRO-731 RP AND ARG-734, VARIANTS SPH4 TYR-705 AND GLN-760, CHARACTERIZATION OF RP VARIANTS CHC PRO-687; PRO-731 AND ARG-734, CHARACTERIZATION OF VARIANTS RP SPH4 TYR-705 AND GLN-760, FUNCTION, AND TRANSPORTER ACTIVITY. RX PubMed=16227998; DOI=10.1038/ng1656; RA Bruce L.J., Robinson H.C., Guizouarn H., Borgese F., Harrison P., RA King M.-J., Goede J.S., Coles S.E., Gore D.M., Lutz H.U., Ficarella R., RA Layton D.M., Iolascon A., Ellory J.C., Stewart G.W.; RT "Monovalent cation leaks in human red cells caused by single amino-acid RT substitutions in the transport domain of the band 3 chloride-bicarbonate RT exchanger, AE1."; RL Nat. Genet. 37:1258-1263(2005). RN [76] RP CHARACTERIZATION OF VARIANT DRTA4 ASP-701, CHARACTERIZATION OF VARIANT RP DRTA1 ASP-858, SUBUNIT, SUBCELLULAR LOCATION, AND FUNCTION. RX PubMed=20151848; DOI=10.3109/09687681003588020; RA Ungsupravate D., Sawasdee N., Khositseth S., Udomchaiprasertkul W., RA Khoprasert S., Li J., Reithmeier R.A., Yenchitsomanus P.T.; RT "Impaired trafficking and intracellular retention of mutant kidney anion RT exchanger 1 proteins (G701D and A858D) associated with distal renal tubular RT acidosis."; RL Mol. Membr. Biol. 27:92-103(2010). RN [77] RP VARIANT ILE-862. RX PubMed=21849667; DOI=10.1152/ajpcell.00054.2011; RA Stewart A.K., Shmukler B.E., Vandorpe D.H., Rivera A., Heneghan J.F., RA Li X., Hsu A., Karpatkin M., O'Neill A.F., Bauer D.E., Heeney M.M., RA John K., Kuypers F.A., Gallagher P.G., Lux S.E., Brugnara C., RA Westhoff C.M., Alper S.L.; RT "Loss-of-function and gain-of-function phenotypes of stomatocytosis mutant RT RhAG F65S."; RL Am. J. Physiol. 301:C1325-C1343(2011). RN [78] RP VARIANTS DRTA4 400-ALA--ALA-408 DEL AND ASN-444, AND CHARACTERIZATION OF RP VARIANT DRTA4 ASN-444. RX PubMed=36320073; DOI=10.1186/s12920-022-01381-y; RA Deejai N., Sawasdee N., Nettuwakul C., Wanachiwanawin W., Sritippayawan S., RA Yenchitsomanus P.T., Rungroj N.; RT "Impaired trafficking and instability of mutant kidney anion exchanger 1 RT proteins associated with autosomal recessive distal renal tubular RT acidosis."; RL BMC Med. Genomics 15:228-228(2022). CC -!- FUNCTION: Functions both as a transporter that mediates electroneutral CC anion exchange across the cell membrane and as a structural protein CC (PubMed:35835865, PubMed:10926824, PubMed:14734552, PubMed:16227998, CC PubMed:24121512, PubMed:28387307, PubMed:1538405, PubMed:20151848). CC Component of the ankyrin-1 complex of the erythrocyte membrane; CC required for normal flexibility and stability of the erythrocyte CC membrane and for normal erythrocyte shape via the interactions of its CC cytoplasmic domain with cytoskeletal proteins, glycolytic enzymes, and CC hemoglobin (PubMed:35835865, PubMed:1538405, PubMed:20151848). CC Functions as a transporter that mediates the 1:1 exchange of inorganic CC anions across the erythrocyte membrane. Mediates chloride-bicarbonate CC exchange in the kidney, and is required for normal acidification of the CC urine (PubMed:10926824, PubMed:14734552, PubMed:16227998, CC PubMed:24121512, PubMed:28387307). {ECO:0000269|PubMed:10926824, CC ECO:0000269|PubMed:14734552, ECO:0000269|PubMed:1538405, CC ECO:0000269|PubMed:16227998, ECO:0000269|PubMed:20151848, CC ECO:0000269|PubMed:24121512, ECO:0000269|PubMed:28387307, CC ECO:0000269|PubMed:35835865}. CC -!- FUNCTION: (Microbial infection) Acts as a receptor for P.falciparum CC (isolate 3D7) MSP9 and thus, facilitates merozoite invasion of CC erythrocytes (PubMed:14630931). Acts as a receptor for P.falciparum CC (isolate 3D7) MSP1 and thus, facilitates merozoite invasion of CC erythrocytes (PubMed:12692305). {ECO:0000269|PubMed:12692305, CC ECO:0000269|PubMed:14630931}. CC -!- CATALYTIC ACTIVITY: CC Reaction=chloride(out) + hydrogencarbonate(in) = chloride(in) + CC hydrogencarbonate(out); Xref=Rhea:RHEA:72363, ChEBI:CHEBI:17544, CC ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:10926824, CC ECO:0000269|PubMed:14734552, ECO:0000269|PubMed:16227998, CC ECO:0000269|PubMed:24121512, ECO:0000269|PubMed:28387307}; CC -!- ACTIVITY REGULATION: Phenyl isothiocyanate inhibits anion transport in CC vitro. CC -!- SUBUNIT: A dimer in solution, but in its membrane environment, it CC exists primarily as a mixture of dimers and tetramers and spans the CC membrane asymmetrically (PubMed:35835865). Component of the ankyrin-1 CC complex in the erythrocyte, composed of ANK1, RHCE, RHAG, SLC4A1, CC EPB42, GYPA, GYPB and AQP1 (PubMed:35835865). Interacts with STOM; this CC interaction positively regulates SLC4A1 activity (PubMed:23219802, CC PubMed:28387307). Interacts with GYPA; a GYPA monomer is bound at each CC end of the SLC4A1 dimer forming an heterotetramer (PubMed:35835865). CC Three SLC4A1 dimers (Band 3-I, Band 3-II and Band 3-III) participates CC in the ankyrin-1 complex (PubMed:35835865). Interacts (via the CC cytoplasmic domain) with EPB42; this interaction is mediated by the CC SLC4A1 Band 3-I dimer (PubMed:35835865). Interacts (via the cytoplasmic CC domain) directly with ANK1; this interaction is mediated by the SLC4A1 CC Band 3-II and Band 3-III dimers (PubMed:35835865, PubMed:7665627). CC {ECO:0000269|PubMed:11049968, ECO:0000269|PubMed:20151848, CC ECO:0000269|PubMed:23219802, ECO:0000269|PubMed:28387307, CC ECO:0000269|PubMed:35835865, ECO:0000269|PubMed:7665627}. CC -!- SUBUNIT: [Isoform 2]: Interacts with TMEM139 (PubMed:26049106). CC {ECO:0000269|PubMed:26049106}. CC -!- SUBUNIT: (Microbial infection) Interacts (via N-terminus) with CC P.falciparum (isolate K1) aldolase FBPA; the interaction inhibits FBPA CC catalytic activity. {ECO:0000269|PubMed:2204832}. CC -!- SUBUNIT: (Microbial infection) Interacts (via the 5ABC region) with CC P.falciparum (isolate 3D7) MSP9/ABRA (via N-terminus). CC {ECO:0000269|PubMed:14630931}. CC -!- SUBUNIT: (Microbial infection) Interacts (via the 5ABC region) with CC P.falciparum (isolate 3D7) MSP1 p42 subunit. CC {ECO:0000269|PubMed:12692305}. CC -!- INTERACTION: CC P02730; Q08AM2: ADAM33; NbExp=3; IntAct=EBI-7576138, EBI-10225815; CC P02730; P05026: ATP1B1; NbExp=8; IntAct=EBI-7576138, EBI-714630; CC P02730; O95393: BMP10; NbExp=3; IntAct=EBI-7576138, EBI-3922513; CC P02730; Q9BXR6: CFHR5; NbExp=3; IntAct=EBI-7576138, EBI-11579371; CC P02730; P02724: GYPA; NbExp=5; IntAct=EBI-7576138, EBI-702665; CC P02730; P27105: STOM; NbExp=14; IntAct=EBI-7576138, EBI-1211440; CC P02730; Q9H2L4: TMEM60; NbExp=3; IntAct=EBI-7576138, EBI-2852148; CC P02730; P46406: GAPDH; Xeno; NbExp=4; IntAct=EBI-7576138, EBI-2750726; CC P02730; A5K5E5: PVX_088820; Xeno; NbExp=8; IntAct=EBI-7576138, EBI-11621504; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10926824, CC ECO:0000269|PubMed:24121512, ECO:0000269|PubMed:26542571, CC ECO:0000269|PubMed:7506871}; Multi-pass membrane protein CC {ECO:0000269|PubMed:26542571}. Basolateral cell membrane CC {ECO:0000269|PubMed:7506871}; Multi-pass membrane protein CC {ECO:0000269|PubMed:7506871}. Note=Detected in the erythrocyte cell CC membrane and on the basolateral membrane of alpha-intercalated cells in CC the collecting duct in the kidney. {ECO:0000269|PubMed:7506871}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=eAE1, Erythrocyte; CC IsoId=P02730-1; Sequence=Displayed; CC Name=2 {ECO:0000269|PubMed:7506871}; Synonyms=kAE1, Kidney; CC IsoId=P02730-2; Sequence=VSP_057833; CC -!- TISSUE SPECIFICITY: Detected in erythrocytes (at protein level). CC {ECO:0000269|PubMed:10926824, ECO:0000269|PubMed:1538405, CC ECO:0000269|PubMed:2204832, ECO:0000269|PubMed:23219802, CC ECO:0000269|PubMed:26542571, ECO:0000269|PubMed:7506871}. CC -!- TISSUE SPECIFICITY: [Isoform 2]: Expressed in kidney (at protein CC level). {ECO:0000269|PubMed:7506871}. 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. {ECO:0000269|PubMed:10942405, CC ECO:0000269|PubMed:1998697}. CC -!- PTM: Phosphorylated on Tyr-359 and Tyr-904 most likely by LYN. PP1- CC inhibited phosphorylation that follows Tyr-8 and Tyr-21 CC phosphorylation. {ECO:0000269|PubMed:10942405, CC ECO:0000269|PubMed:1998697}. CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:26542571}. CC -!- POLYMORPHISM: SLC4A1 is responsible for the Diego blood group system CC [MIM:110500]. The molecular basis of the Di(a)=Di1/Di(b)/Di2 blood CC group 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 the CC Wr(a)=Di3/Wr(b)/Di4 blood group antigens is a single variation in CC position 658; Lys-658 corresponds to Wr(a) and Glu-658 to Wr(b). The CC blood group antigens Wd(a)=Di5 (Waldner-type) has Met-557; Rb(a)=Di6 CC has Leu-548 and WARR=Di7 has Ile-552. CC -!- POLYMORPHISM: SLC4A1 is responsible for the Swann blood group system CC (SW) [MIM:601550]. Sw(a+) has a Gln or a Trp at position 646 and Sw(a-) CC has an Arg. CC -!- POLYMORPHISM: SLC4A1 is responsible for the Froese blood group system CC (FR) [MIM:601551]. FR(a+) has a Lys at position 480 and FR(a-) has a CC Glu. CC -!- POLYMORPHISM: Genetic variations in SLC4A1 are involved in resistance CC to malaria [MIM:611162]. CC -!- DISEASE: Ovalocytosis, Southeast Asian (SAO) [MIM:166900]: An autosomal CC dominant hematologic disorder characterized by ovalocytic erythrocytes CC that are rigid and exhibit reduced expression of many erythrocyte CC antigens. Clinical manifestations include mild hemolysis, intermittent CC jaundice and gallstones. However, the disorder is most often CC asymptomatic. {ECO:0000269|PubMed:1538405, ECO:0000269|PubMed:1722314}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- DISEASE: Spherocytosis 4 (SPH4) [MIM:612653]: An autosomal dominant CC form of spherocytosis, a group of hematologic disorders characterized CC by the presence of numerous abnormally shaped erythrocytes which are CC generally spheroidal. Affected individuals have anemia, jaundice, and CC splenomegaly. Clinical severity is variable. Some individuals are CC asymptomatic, whereas others have severe hemolytic anemia requiring CC erythrocyte transfusion. {ECO:0000269|PubMed:10580570, CC ECO:0000269|PubMed:10745622, ECO:0000269|PubMed:10942416, CC ECO:0000269|PubMed:11380459, ECO:0000269|PubMed:1378323, CC ECO:0000269|PubMed:15813913, ECO:0000269|PubMed:16227998, CC ECO:0000269|PubMed:7530501, ECO:0000269|PubMed:8547122, CC ECO:0000269|PubMed:8640229, ECO:0000269|PubMed:8943874, CC ECO:0000269|PubMed:9012689, ECO:0000269|PubMed:9207478, CC ECO:0000269|PubMed:9233560, ECO:0000269|PubMed:9973643}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Renal tubular acidosis, distal, 1 (DRTA1) [MIM:179800]: An CC autosomal dominant disease characterized by reduced ability to acidify CC urine, variable hyperchloremic hypokalemic metabolic acidosis, CC nephrocalcinosis, and nephrolithiasis. It is due to functional failure CC of alpha-intercalated cells of the cortical collecting duct of the CC distal nephron, where vectorial proton transport is required for CC urinary acidification. {ECO:0000269|PubMed:10926824, CC ECO:0000269|PubMed:14734552, ECO:0000269|PubMed:20151848, CC ECO:0000269|PubMed:9312167, ECO:0000269|PubMed:9600966}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Renal tubular acidosis, distal, 4, with hemolytic anemia CC (DRTA4) [MIM:611590]: An autosomal recessive disease characterized by CC the association of hemolytic anemia with distal renal tubular acidosis, CC the reduced ability to acidify urine resulting in variable CC hyperchloremic hypokalemic metabolic acidosis, nephrocalcinosis, and CC nephrolithiasis. {ECO:0000269|PubMed:10926824, CC ECO:0000269|PubMed:15211439, ECO:0000269|PubMed:20151848, CC ECO:0000269|PubMed:36320073, ECO:0000269|PubMed:9854053}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Renal tubular acidosis, distal, with normal red cell CC morphology (dRTA-NRC) [MIM:611590]: A disease characterized by reduced CC ability to acidify urine, variable hyperchloremic hypokalemic metabolic CC acidosis, nephrocalcinosis, and nephrolithiasis. It is due to CC functional failure of alpha-intercalated cells of the cortical CC collecting duct of the distal nephron, where vectorial proton transport CC is required for urinary acidification. {ECO:0000269|PubMed:15211439}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- DISEASE: Cryohydrocytosis (CHC) [MIM:185020]: An autosomal dominant CC disorder of red cell membrane permeability characterized by cold- CC induced changes in cell volume, resulting in cold-sensitive CC stomatocytosis, and increased erythrocyte osmotic fragility and CC autohemolysis at 4 degrees Celsius. Patients present with mild to CC moderate hemolytic anemia, splenomegaly, fatigue, and CC pseudohyperkalemia due to a potassium leak from the erythrocytes. CC {ECO:0000269|PubMed:16227998}. Note=The disease is caused by variants CC affecting distinct genetic loci, including the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family. CC {ECO:0000305}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=Band 3 entry; CC URL="https://en.wikipedia.org/wiki/Band_3"; CC -!- WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene mutation CC database; CC URL="https://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=diego"; CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/slc4a1/"; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/42325/SLC4A1"; 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; X12609; CAA31128.1; -; mRNA. DR EMBL; M27819; AAA35514.1; -; mRNA. DR EMBL; DQ419529; ABD74692.1; -; mRNA. DR EMBL; GQ981383; ADN39420.1; -; mRNA. DR EMBL; GQ981384; ADN39421.1; -; mRNA. DR EMBL; DQ072115; AAY57324.1; -; Genomic_DNA. DR EMBL; CH471178; EAW51614.1; -; Genomic_DNA. DR EMBL; BC096106; AAH96106.1; -; mRNA. DR EMBL; BC096107; AAH96107.1; -; mRNA. DR EMBL; BC099628; AAH99628.1; -; mRNA. DR EMBL; BC099629; AAH99629.1; -; mRNA. DR EMBL; BC101570; AAI01571.1; -; mRNA. DR EMBL; BC101574; AAI01575.1; -; mRNA. DR EMBL; S68680; AAC60608.2; -; mRNA. DR CCDS; CCDS11481.1; -. [P02730-1] DR PIR; A36218; B3HU. DR RefSeq; NP_000333.1; NM_000342.3. [P02730-1] DR RefSeq; XP_005257650.1; XM_005257593.4. [P02730-2] DR PDB; 1BH7; NMR; -; A=803-835. DR PDB; 1BNX; NMR; -; A=389-430. DR PDB; 1BTQ; NMR; -; A=405-424. DR PDB; 1BTR; NMR; -; A=405-424. DR PDB; 1BTS; NMR; -; A=436-456. DR PDB; 1BTT; NMR; -; A=436-456. DR PDB; 1BZK; NMR; -; A=389-430. DR PDB; 1HYN; X-ray; 2.60 A; P/Q/R/S=1-379. DR PDB; 2BTA; NMR; -; A=1-15. DR PDB; 2BTB; NMR; -; A=1-15. DR PDB; 3BTB; NMR; -; A=1-15. DR PDB; 4KY9; X-ray; 2.23 A; A/P=51-356. DR PDB; 4YZF; X-ray; 3.50 A; A/B/C/D=1-911. DR PDB; 7TVZ; EM; 3.60 A; A/B=1-911. DR PDB; 7TW0; EM; 4.60 A; A/B=1-911. DR PDB; 7TW1; EM; 4.60 A; A/B=1-911. DR PDB; 7TW2; EM; 4.80 A; A/B=1-911. DR PDB; 7TW3; EM; 4.40 A; A/B=1-911. DR PDB; 7TW5; EM; 5.70 A; A/B=1-911. DR PDB; 7TW6; EM; 5.60 A; A/B/J/K=1-911. DR PDB; 7TY4; EM; 2.99 A; A/B=1-911. DR PDB; 7TY6; EM; 2.98 A; A/B=1-911. DR PDB; 7TY7; EM; 3.37 A; A/B=1-911. DR PDB; 7TY8; EM; 3.18 A; A/B=1-911. DR PDB; 7TYA; EM; 3.07 A; A/B=1-911. DR PDB; 7UZ3; EM; 2.35 A; C/E=1-911. DR PDB; 7UZU; EM; 2.30 A; W=1-911. DR PDB; 7UZV; EM; 2.50 A; C/E=1-911. DR PDB; 7V07; EM; 2.80 A; C/E=1-911. DR PDB; 7V0K; EM; 2.40 A; O/P/W=1-911. DR PDB; 7V0M; EM; 2.70 A; W=1-911. DR PDB; 7V0T; EM; 2.70 A; C/E=1-911. DR PDB; 7V0U; EM; 3.00 A; D/F=1-911. DR PDB; 7V0Y; EM; 3.00 A; C/E=1-911. DR PDB; 7V19; EM; 3.30 A; C/E=1-911. DR PDB; 8CRQ; EM; 3.20 A; C/E=1-911. DR PDB; 8CRR; EM; 3.00 A; C/E=1-911. DR PDB; 8CRT; EM; 3.00 A; C/E=1-911. DR PDB; 8CS9; EM; 2.74 A; V/Y/Z/e/f/g=1-911. DR PDB; 8CSL; EM; 25.00 A; V/W/Y/Z/e/f/g=1-911. DR PDB; 8CSV; EM; 2.70 A; W=1-911. DR PDB; 8CSY; EM; 2.70 A; C/E=1-911. DR PDB; 8CT3; EM; 3.30 A; C/E=1-911. DR PDB; 8CTE; EM; 2.90 A; P/T/W=1-911. DR PDB; 8T6U; EM; 3.13 A; A/B=369-891. DR PDB; 8T6V; EM; 2.95 A; A/B=369-891. DR PDBsum; 1BH7; -. DR PDBsum; 1BNX; -. DR PDBsum; 1BTQ; -. DR PDBsum; 1BTR; -. DR PDBsum; 1BTS; -. DR PDBsum; 1BTT; -. DR PDBsum; 1BZK; -. DR PDBsum; 1HYN; -. DR PDBsum; 2BTA; -. DR PDBsum; 2BTB; -. DR PDBsum; 3BTB; -. DR PDBsum; 4KY9; -. DR PDBsum; 4YZF; -. DR PDBsum; 7TVZ; -. DR PDBsum; 7TW0; -. DR PDBsum; 7TW1; -. DR PDBsum; 7TW2; -. DR PDBsum; 7TW3; -. DR PDBsum; 7TW5; -. DR PDBsum; 7TW6; -. DR PDBsum; 7TY4; -. DR PDBsum; 7TY6; -. DR PDBsum; 7TY7; -. DR PDBsum; 7TY8; -. DR PDBsum; 7TYA; -. DR PDBsum; 7UZ3; -. DR PDBsum; 7UZU; -. DR PDBsum; 7UZV; -. DR PDBsum; 7V07; -. DR PDBsum; 7V0K; -. DR PDBsum; 7V0M; -. DR PDBsum; 7V0T; -. DR PDBsum; 7V0U; -. DR PDBsum; 7V0Y; -. DR PDBsum; 7V19; -. DR PDBsum; 8CRQ; -. DR PDBsum; 8CRR; -. DR PDBsum; 8CRT; -. DR PDBsum; 8CS9; -. DR PDBsum; 8CSL; -. DR PDBsum; 8CSV; -. DR PDBsum; 8CSY; -. DR PDBsum; 8CT3; -. DR PDBsum; 8CTE; -. DR PDBsum; 8T6U; -. DR PDBsum; 8T6V; -. DR AlphaFoldDB; P02730; -. DR EMDB; EMD-26142; -. DR EMDB; EMD-26146; -. DR EMDB; EMD-26147; -. DR EMDB; EMD-26148; -. DR EMDB; EMD-26149; -. DR EMDB; EMD-26151; -. DR EMDB; EMD-26153; -. DR EMDB; EMD-26154; -. DR EMDB; EMD-26165; -. DR EMDB; EMD-26167; -. DR EMDB; EMD-26168; -. DR EMDB; EMD-26169; -. DR EMDB; EMD-26171; -. DR EMDB; EMD-26874; -. DR EMDB; EMD-26918; -. DR EMDB; EMD-26919; -. DR EMDB; EMD-26940; -. DR EMDB; EMD-26943; -. DR EMDB; EMD-26944; -. DR EMDB; EMD-26950; -. DR EMDB; EMD-26951; -. DR EMDB; EMD-26953; -. DR EMDB; EMD-26954; -. DR EMDB; EMD-26955; -. DR EMDB; EMD-26956; -. DR EMDB; EMD-26958; -. DR EMDB; EMD-26960; -. DR EMDB; EMD-26965; -. DR EMDB; EMD-26972; -. DR EMDB; EMD-26975; -. DR EMDB; EMD-26979; -. DR EMDB; EMD-26988; -. DR EMDB; EMD-41081; -. DR EMDB; EMD-41082; -. DR SMR; P02730; -. DR BioGRID; 112412; 23. DR CORUM; P02730; -. DR DIP; DIP-42428N; -. DR ELM; P02730; -. DR IntAct; P02730; 29. DR MINT; P02730; -. DR STRING; 9606.ENSP00000262418; -. DR MoonDB; P02730; Curated. DR MoonProt; P02730; -. DR TCDB; 2.A.31.1.1; the anion exchanger (ae) family. DR GlyConnect; 1024; 1 N-Linked glycan (1 site), 1 O-GlcNAc glycan (3 sites). DR GlyCosmos; P02730; 4 sites, 2 glycans. DR GlyGen; P02730; 4 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (3 sites). DR iPTMnet; P02730; -. DR PhosphoSitePlus; P02730; -. DR SwissPalm; P02730; -. DR BioMuta; SLC4A1; -. DR DMDM; 114787; -. DR jPOST; P02730; -. DR MassIVE; P02730; -. DR PaxDb; 9606-ENSP00000262418; -. DR PeptideAtlas; P02730; -. DR ProteomicsDB; 51557; -. DR ABCD; P02730; 36 sequenced antibodies. DR Antibodypedia; 2977; 379 antibodies from 36 providers. DR DNASU; 6521; -. DR Ensembl; ENST00000262418.12; ENSP00000262418.6; ENSG00000004939.16. [P02730-1] DR GeneID; 6521; -. DR KEGG; hsa:6521; -. DR MANE-Select; ENST00000262418.12; ENSP00000262418.6; NM_000342.4; NP_000333.1. DR UCSC; uc002igf.5; human. [P02730-1] DR AGR; HGNC:11027; -. DR CTD; 6521; -. DR DisGeNET; 6521; -. DR GeneCards; SLC4A1; -. DR GeneReviews; SLC4A1; -. DR HGNC; HGNC:11027; SLC4A1. DR HPA; ENSG00000004939; Tissue enriched (bone). DR MalaCards; SLC4A1; -. DR MIM; 109270; gene+phenotype. DR MIM; 110500; phenotype. DR MIM; 112010; phenotype. DR MIM; 112050; phenotype. DR MIM; 130600; phenotype. DR MIM; 166900; phenotype. DR MIM; 179800; phenotype. DR MIM; 185020; phenotype. DR MIM; 601550; phenotype. DR MIM; 601551; phenotype. DR MIM; 611162; phenotype. DR MIM; 611590; phenotype. DR MIM; 612653; phenotype. DR neXtProt; NX_P02730; -. DR OpenTargets; ENSG00000004939; -. DR Orphanet; 93608; Autosomal dominant distal renal tubular acidosis. DR Orphanet; 3202; Dehydrated hereditary stomatocytosis. DR Orphanet; 93610; Distal renal tubular acidosis with anemia. DR Orphanet; 398088; Hereditary cryohydrocytosis with normal stomatin. DR Orphanet; 822; Hereditary spherocytosis. DR Orphanet; 98868; Southeast Asian ovalocytosis. DR PharmGKB; PA35895; -. DR VEuPathDB; HostDB:ENSG00000004939; -. DR eggNOG; KOG1172; Eukaryota. DR GeneTree; ENSGT00940000157423; -. DR HOGENOM; CLU_002289_1_0_1; -. DR InParanoid; P02730; -. DR OMA; YSHFPIW; -. DR OrthoDB; 1013180at2759; -. DR PhylomeDB; P02730; -. DR TreeFam; TF313630; -. DR PathwayCommons; P02730; -. DR Reactome; R-HSA-1237044; Erythrocytes take up carbon dioxide and release oxygen. DR Reactome; R-HSA-1247673; Erythrocytes take up oxygen and release carbon dioxide. DR Reactome; R-HSA-425381; Bicarbonate transporters. DR Reactome; R-HSA-5619050; Defective SLC4A1 causes hereditary spherocytosis type 4 (HSP4), distal renal tubular acidosis (dRTA) and dRTA with hemolytic anemia (dRTA-HA). DR SignaLink; P02730; -. DR SIGNOR; P02730; -. DR BioGRID-ORCS; 6521; 37 hits in 1164 CRISPR screens. DR ChiTaRS; SLC4A1; human. DR EvolutionaryTrace; P02730; -. DR GeneWiki; Band_3; -. DR GenomeRNAi; 6521; -. DR Pharos; P02730; Tbio. DR PRO; PR:P02730; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; P02730; Protein. DR Bgee; ENSG00000004939; Expressed in trabecular bone tissue and 140 other cell types or tissues. DR ExpressionAtlas; P02730; baseline and differential. DR GO; GO:0170014; C:ankyrin-1 complex; IDA:UniProtKB. DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB. DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB. DR GO; GO:0030863; C:cortical cytoskeleton; IDA:UniProtKB. DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:Ensembl. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; NAS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0030018; C:Z disc; ISS:UniProtKB. DR GO; GO:0030506; F:ankyrin binding; IPI:BHF-UCL. DR GO; GO:0015106; F:bicarbonate transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0015108; F:chloride transmembrane transporter activity; ISS:UniProtKB. DR GO; GO:0140900; F:chloride:bicarbonate antiporter activity; IDA:UniProtKB. DR GO; GO:0030492; F:hemoglobin binding; IEA:Ensembl. DR GO; GO:0008509; F:monoatomic anion transmembrane transporter activity; TAS:ProtInc. DR GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL. DR GO; GO:0043495; F:protein-membrane adaptor activity; TAS:BHF-UCL. DR GO; GO:0005452; F:solute:inorganic anion antiporter activity; IDA:UniProtKB. DR GO; GO:0015701; P:bicarbonate transport; IDA:UniProtKB. DR GO; GO:0007596; P:blood coagulation; IEA:Ensembl. DR GO; GO:1902476; P:chloride transmembrane transport; IDA:UniProtKB. DR GO; GO:0006821; P:chloride transport; ISS:UniProtKB. DR GO; GO:0048821; P:erythrocyte development; IEA:Ensembl. DR GO; GO:0006873; P:intracellular monoatomic ion homeostasis; TAS:ProtInc. DR GO; GO:0006820; P:monoatomic anion transport; TAS:ProtInc. DR GO; GO:1904539; P:negative regulation of glycolytic process through fructose-6-phosphate; IEA:Ensembl. DR GO; GO:0035811; P:negative regulation of urine volume; IEA:Ensembl. DR GO; GO:0045852; P:pH elevation; IEA:Ensembl. DR GO; GO:0017121; P:plasma membrane phospholipid scrambling; IEA:Ensembl. DR GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl. DR GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR DisProt; DP01167; -. DR Gene3D; 1.10.287.570; Helical hairpin bin; 1. DR InterPro; IPR001717; Anion_exchange. DR InterPro; IPR002977; Anion_exchange_1. DR InterPro; IPR018241; Anion_exchange_CS. DR InterPro; IPR013769; Band3_cytoplasmic_dom. DR InterPro; IPR011531; HCO3_transpt-like_TM_dom. DR InterPro; IPR003020; HCO3_transpt_euk. DR InterPro; IPR016152; PTrfase/Anion_transptr. DR NCBIfam; TIGR00834; ae; 1. DR PANTHER; PTHR11453; ANION EXCHANGE PROTEIN; 1. DR PANTHER; PTHR11453:SF12; BAND 3 ANION TRANSPORT PROTEIN; 1. DR Pfam; PF07565; Band_3_cyto; 1. DR Pfam; PF00955; HCO3_cotransp; 2. DR PRINTS; PR00165; ANIONEXCHNGR. DR PRINTS; PR01187; ANIONEXHNGR1. DR PRINTS; PR01231; HCO3TRNSPORT. DR SUPFAM; SSF55804; Phoshotransferase/anion transport protein; 1. DR PROSITE; PS00219; ANION_EXCHANGER_1; 1. DR PROSITE; PS00220; ANION_EXCHANGER_2; 1. DR Genevisible; P02730; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Anion exchange; KW Blood group antigen; Cell membrane; Direct protein sequencing; KW Disease variant; Elliptocytosis; Glycoprotein; Hereditary hemolytic anemia; KW Ion transport; Lipoprotein; Membrane; Palmitate; Phosphoprotein; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..911 FT /note="Band 3 anion transport protein" FT /id="PRO_0000079209" FT TOPO_DOM 1..403 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:26542571" FT TRANSMEM 404..427 FT /note="Helical; Name=1" FT /evidence="ECO:0000269|PubMed:26542571" FT TOPO_DOM 428..435 FT /note="Extracellular" FT /evidence="ECO:0000269|PubMed:26542571" FT TRANSMEM 436..456 FT /note="Helical; Name=2" FT /evidence="ECO:0000269|PubMed:26542571" FT TOPO_DOM 457..459 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:26542571" FT TRANSMEM 460..476 FT /note="Discontinuously helical; Name=3" FT /evidence="ECO:0000269|PubMed:26542571" FT TOPO_DOM 477..485 FT /note="Extracellular" FT /evidence="ECO:0000269|PubMed:26542571" FT TRANSMEM 486..506 FT /note="Helical; Name=4" FT /evidence="ECO:0000269|PubMed:26542571" FT TOPO_DOM 507..518 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:26542571" FT TRANSMEM 519..541 FT /note="Helical; Name=5" FT /evidence="ECO:0000269|PubMed:26542571" FT TOPO_DOM 542..570 FT /note="Extracellular" FT /evidence="ECO:0000269|PubMed:26542571" FT TRANSMEM 571..591 FT /note="Helical; Name=6" FT /evidence="ECO:0000269|PubMed:26542571" FT TOPO_DOM 592..602 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:26542571" FT TRANSMEM 603..623 FT /note="Helical; Name=7" FT /evidence="ECO:0000269|PubMed:26542571" FT TOPO_DOM 624..663 FT /note="Extracellular" FT /evidence="ECO:0000269|PubMed:26542571" FT TRANSMEM 664..684 FT /note="Helical; Name=8" FT /evidence="ECO:0000269|PubMed:26542571" FT TOPO_DOM 685..700 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:26542571" FT TRANSMEM 701..719 FT /note="Helical; Name=9" FT /evidence="ECO:0000269|PubMed:26542571" FT TRANSMEM 720..737 FT /note="Discontinuously helical; Name=10" FT /evidence="ECO:0000269|PubMed:26542571" FT TOPO_DOM 738..760 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:26542571" FT TRANSMEM 761..781 FT /note="Helical; Name=11" FT /evidence="ECO:0000269|PubMed:26542571" FT TRANSMEM 782..800 FT /note="Helical; Name=12" FT /evidence="ECO:0000269|PubMed:26542571" FT TOPO_DOM 801..838 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:26542571" FT INTRAMEM 839..869 FT /note="Discontinuously helical" FT /evidence="ECO:0000269|PubMed:26542571" FT TOPO_DOM 870..911 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:26542571" FT REGION 1..40 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 13..31 FT /note="(Microbial infection) Interaction with P.falciparum FT (isolate K1) FBPA" FT /evidence="ECO:0000269|PubMed:2204832" FT REGION 55..290 FT /note="Globular" FT REGION 176..185 FT /note="Interaction with ANK1" FT /evidence="ECO:0000305" FT REGION 304..357 FT /note="Dimerization arm" FT REGION 559..630 FT /note="Involved in anion transport" FT REGION 720..761 FT /note="(Microbial infection) 5ABC region; interaction with FT P.falciparum (isolate 3D7) MSP9" FT /evidence="ECO:0000269|PubMed:14630931" FT COMPBIAS 1..29 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 590 FT /note="Important for anion transport" FT SITE 681 FT /note="Important for anion-proton cotransport" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000269|PubMed:2790053, FT ECO:0000269|PubMed:701248" FT MOD_RES 8 FT /note="Phosphotyrosine" FT /evidence="ECO:0000269|PubMed:10942405, FT ECO:0000269|PubMed:1998697" FT MOD_RES 21 FT /note="Phosphotyrosine" FT /evidence="ECO:0000269|PubMed:10942405, FT ECO:0000269|PubMed:1998697" FT MOD_RES 46 FT /note="Phosphotyrosine" FT /evidence="ECO:0000269|PubMed:1998697" FT MOD_RES 185 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P23562" FT MOD_RES 350 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P04919" FT MOD_RES 359 FT /note="Phosphotyrosine" FT /evidence="ECO:0000269|PubMed:10942405" FT MOD_RES 904 FT /note="Phosphotyrosine" FT /evidence="ECO:0000269|PubMed:10942405" FT LIPID 843 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000269|PubMed:1885574" FT CARBOHYD 642 FT /note="N-linked (GlcNAc...) (complex) asparagine" FT /evidence="ECO:0000269|PubMed:10861210, FT ECO:0000269|PubMed:24121512, ECO:0000269|PubMed:35835865" FT VAR_SEQ 1..65 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000269|PubMed:7506871" FT /id="VSP_057833" FT VARIANT 27 FT /note="P -> H" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_058035" FT VARIANT 38 FT /note="D -> A (in dbSNP:rs5035)" FT /evidence="ECO:0000269|PubMed:10745622, FT ECO:0000269|PubMed:16252102, ECO:0000269|PubMed:9012689, FT ECO:0000269|Ref.5" FT /id="VAR_014612" FT VARIANT 40 FT /note="E -> K (found in patients with hemolytic anemia; FT uncertain significance; Montefiore; dbSNP:rs45562031)" FT /evidence="ECO:0000269|PubMed:8471774, FT ECO:0000269|PubMed:8640229" FT /id="VAR_000798" FT VARIANT 45 FT /note="D -> E (in dbSNP:rs34700496)" FT /id="VAR_036693" FT VARIANT 56 FT /note="K -> E (in Di(a)/Memphis-II antigen; dbSNP:rs5036)" FT /evidence="ECO:0000269|PubMed:10745622, FT ECO:0000269|PubMed:16227998, ECO:0000269|PubMed:1678289, FT ECO:0000269|PubMed:1722314, ECO:0000269|PubMed:8206915, FT ECO:0000269|Ref.5" FT /id="VAR_000799" FT VARIANT 68 FT /note="E -> K (in dbSNP:rs13306787)" FT /id="VAR_039290" FT VARIANT 72 FT /note="E -> D (in dbSNP:rs13306788)" FT /evidence="ECO:0000269|PubMed:10745622" FT /id="VAR_058036" FT VARIANT 73 FT /note="L -> M (in dbSNP:rs781490287)" FT /evidence="ECO:0000269|PubMed:9012689" FT /id="VAR_039291" FT VARIANT 90 FT /note="E -> K (in SPH4; Cape Town; dbSNP:rs28929480)" FT /evidence="ECO:0000269|PubMed:11380459" FT /id="VAR_013784" FT VARIANT 112 FT /note="R -> S (in dbSNP:rs5037)" FT /id="VAR_014613" FT VARIANT 130 FT /note="G -> R (in SPH4; Fukoka; dbSNP:rs121912749)" FT /evidence="ECO:0000269|PubMed:10745622" FT /id="VAR_013785" FT VARIANT 147 FT /note="P -> S (in SPH4; Mondego)" FT /evidence="ECO:0000269|PubMed:9207478" FT /id="VAR_013786" FT VARIANT 285 FT /note="A -> D (in SPH4; Boston)" FT /evidence="ECO:0000269|PubMed:8943874" FT /id="VAR_013787" FT VARIANT 327 FT /note="P -> R (in SPH4; Tuscaloosa; dbSNP:rs28931583)" FT /evidence="ECO:0000269|PubMed:1378323" FT /id="VAR_000800" FT VARIANT 400..408 FT /note="Missing (in SAO and DRTA4; increased rigidity of the FT erythrocyte membrane leading to increased resistance to FT shear stress and increased resistance to P.falciparum)" FT /evidence="ECO:0000269|PubMed:1538405, FT ECO:0000269|PubMed:1722314, ECO:0000269|PubMed:36320073" FT /id="VAR_000801" FT VARIANT 429 FT /note="E -> D (in NFLD+ antigen; dbSNP:rs1048804130)" FT /evidence="ECO:0000269|PubMed:10738034" FT /id="VAR_058037" FT VARIANT 432 FT /note="R -> W (in ELO antigen; dbSNP:rs373768879)" FT /id="VAR_013788" FT VARIANT 442 FT /note="I -> F (in dbSNP:rs5018)" FT /id="VAR_014614" FT VARIANT 444 FT /note="T -> N (in DRTA4; decreased expression; decreased FT stability; no effect on dimerization; dbSNP:rs754973425)" FT /evidence="ECO:0000269|PubMed:36320073" FT /id="VAR_087559" FT VARIANT 455 FT /note="G -> E (in SPH4; Benesov)" FT /evidence="ECO:0000269|PubMed:8943874" FT /id="VAR_013789" FT VARIANT 455 FT /note="G -> R (in SPH4; Yamagata)" FT /evidence="ECO:0000269|PubMed:10745622" FT /id="VAR_058038" FT VARIANT 480 FT /note="E -> K (in FR(a+) antigen; dbSNP:rs121912756)" FT /evidence="ECO:0000269|PubMed:11061863" FT /id="VAR_013790" FT VARIANT 488 FT /note="V -> M (in SPH4; Coimbra; also in AR-dRTA; FT dbSNP:rs28931584)" FT /evidence="ECO:0000269|PubMed:10942416, FT ECO:0000269|PubMed:9207478" FT /id="VAR_013791" FT VARIANT 490 FT /note="R -> C (in SPH4; Bicetre I; dbSNP:rs1398477044)" FT /evidence="ECO:0000269|PubMed:9233560" FT /id="VAR_013792" FT VARIANT 490 FT /note="R -> H (in SPH4; Pinhal; dbSNP:rs1598299485)" FT /evidence="ECO:0000269|PubMed:10580570" FT /id="VAR_058039" FT VARIANT 508 FT /note="E -> K (in dbSNP:rs45568837)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_025090" FT VARIANT 518 FT /note="R -> C (in SPH4; Dresden; dbSNP:rs868742796)" FT /evidence="ECO:0000269|PubMed:8640229" FT /id="VAR_000802" FT VARIANT 548 FT /note="P -> L (in RB(A) antigen; dbSNP:rs879202054)" FT /id="VAR_000803" FT VARIANT 551 FT /note="K -> N (in TR(A) antigen)" FT /id="VAR_013793" FT VARIANT 552 FT /note="T -> I (in WARR antigen)" FT /id="VAR_000804" FT VARIANT 555 FT /note="Y -> H (in VG(a) antigen)" FT /id="VAR_013794" FT VARIANT 557 FT /note="V -> M (in WD(a) antigen; dbSNP:rs121912743)" FT /id="VAR_000805" FT VARIANT 561 FT /note="P -> A (in NFLD+ antigen)" FT /evidence="ECO:0000269|PubMed:10738034" FT /id="VAR_058040" FT VARIANT 561 FT /note="P -> S (in BOW antigen)" FT /evidence="ECO:0000269|PubMed:10738034" FT /id="VAR_013795" FT VARIANT 565 FT /note="G -> A (in WU antigen; dbSNP:rs551784583)" FT /id="VAR_013796" FT VARIANT 566 FT /note="P -> A (in KREP antigen)" FT /id="VAR_013797" FT VARIANT 566 FT /note="P -> S (in PN(a) antigen; dbSNP:rs1393742050)" FT /id="VAR_013798" FT VARIANT 569 FT /note="N -> K (in BP(a) antigen)" FT /id="VAR_013799" FT VARIANT 586 FT /note="M -> L (in dbSNP:rs5019)" FT /id="VAR_014615" FT VARIANT 589 FT /note="R -> C (in DRTA1; reduced red cell sulfate transport FT and altered glycosylation of the red cell band 3 N-glycan FT chain; dbSNP:rs121912745)" FT /evidence="ECO:0000269|PubMed:9312167" FT /id="VAR_015104" FT VARIANT 589 FT /note="R -> H (in DRTA1; dbSNP:rs121912744)" FT /evidence="ECO:0000269|PubMed:9312167, FT ECO:0000269|PubMed:9600966" FT /id="VAR_015105" FT VARIANT 589 FT /note="R -> S (in DRTA1; dbSNP:rs121912745)" FT /evidence="ECO:0000269|PubMed:9600966" FT /id="VAR_015106" FT VARIANT 602 FT /note="R -> H (in DRTA4; dbSNP:rs121912754)" FT /evidence="ECO:0000269|PubMed:15211439" FT /id="VAR_039292" FT VARIANT 609 FT /note="G -> R (in DRTA1; detected subapically and at the FT apical membrane as well as at the basolateral membrane in FT contrast to the normal basolateral appearance of wild-type FT protein; dbSNP:rs878853002)" FT /evidence="ECO:0000269|PubMed:14734552" FT /id="VAR_058041" FT VARIANT 613 FT /note="S -> F (in DRTA1; markedly increased red cell FT sulfate transport but almost normal red cell iodide FT transport; dbSNP:rs121912746)" FT /evidence="ECO:0000269|PubMed:9312167" FT /id="VAR_015107" FT VARIANT 646 FT /note="R -> Q (in SW(a+) antigen; dbSNP:rs121912757)" FT /evidence="ECO:0000269|PubMed:11155072" FT /id="VAR_013800" FT VARIANT 646 FT /note="R -> W (in SW(a+) antigen; dbSNP:rs121912758)" FT /evidence="ECO:0000269|PubMed:11155072" FT /id="VAR_013801" FT VARIANT 656 FT /note="R -> C (in HG(a) antigen; dbSNP:rs372514760)" FT /id="VAR_013802" FT VARIANT 656 FT /note="R -> H (in MO(a) antigen; dbSNP:rs758868427)" FT /id="VAR_013803" FT VARIANT 658 FT /note="E -> K (in WR(a) antigen; dbSNP:rs75731670)" FT /evidence="ECO:0000269|PubMed:7812009" FT /id="VAR_000806" FT VARIANT 663 FT /note="M -> K (in SPH4; Tambau)" FT /evidence="ECO:0000269|PubMed:15813913" FT /id="VAR_058042" FT VARIANT 663 FT /note="Missing (in SPH4; Osnabruck II)" FT /evidence="ECO:0000269|PubMed:8640229" FT /id="VAR_000807" FT VARIANT 687 FT /note="L -> P (in CHC; Blackburn; induces abnormal cations FT sodium and potassium fluxes; decreases anion chloride FT transport; dbSNP:rs863225463)" FT /evidence="ECO:0000269|PubMed:16227998" FT /id="VAR_039293" FT VARIANT 688 FT /note="I -> V (in dbSNP:rs5022)" FT /id="VAR_014616" FT VARIANT 690 FT /note="S -> G (in dbSNP:rs5023)" FT /id="VAR_014617" FT VARIANT 701 FT /note="G -> D (in DRTA4 and dRTA-NRC; impairs expression at FT the cell membrane; dbSNP:rs121912748)" FT /evidence="ECO:0000269|PubMed:10926824, FT ECO:0000269|PubMed:15211439, ECO:0000269|PubMed:20151848, FT ECO:0000269|PubMed:9854053" FT /id="VAR_015171" FT VARIANT 705 FT /note="D -> Y (in SPH4; Horam; induces abnormal cations FT sodium and potassium fluxes; decreases anion chloride FT transport)" FT /evidence="ECO:0000269|PubMed:16227998" FT /id="VAR_039294" FT VARIANT 707 FT /note="L -> P (in SPH4; Most)" FT /evidence="ECO:0000269|PubMed:11208088, FT ECO:0000269|PubMed:8943874" FT /id="VAR_013804" FT VARIANT 714 FT /note="G -> R (in SPH4; Okinawa)" FT /evidence="ECO:0000269|PubMed:10745622" FT /id="VAR_013805" FT VARIANT 731 FT /note="S -> P (in CHC; Hemel; induces abnormal cations FT sodium and potassium fluxes; decreases anion chloride FT transport; dbSNP:rs863225461)" FT /evidence="ECO:0000269|PubMed:16227998" FT /id="VAR_039295" FT VARIANT 734 FT /note="H -> R (in CHC; Hurstpierpont; induces abnormal FT cations sodium and potassium fluxes; decreases anion FT chloride transport; dbSNP:rs863225462)" FT /evidence="ECO:0000269|PubMed:16227998" FT /id="VAR_039296" FT VARIANT 760 FT /note="R -> Q (in SPH4; Prague II; induces abnormal cations FT sodium and potassium fluxes; decreases anion chloride FT transport; dbSNP:rs121912755)" FT /evidence="ECO:0000269|PubMed:10745622, FT ECO:0000269|PubMed:11208088, ECO:0000269|PubMed:16227998, FT ECO:0000269|PubMed:7530501" FT /id="VAR_013806" FT VARIANT 760 FT /note="R -> W (in SPH4; Hradec Kralove; dbSNP:rs373916826)" FT /evidence="ECO:0000269|PubMed:10745622, FT ECO:0000269|PubMed:11208088, ECO:0000269|PubMed:7530501" FT /id="VAR_013807" FT VARIANT 771 FT /note="G -> D (in SPH4; Chur; dbSNP:rs121912741)" FT /evidence="ECO:0000269|PubMed:8547122" FT /id="VAR_013808" FT VARIANT 773 FT /note="S -> P (in dRTA-NRC; dbSNP:rs121912753)" FT /evidence="ECO:0000269|PubMed:15211439" FT /id="VAR_039297" FT VARIANT 783 FT /note="I -> N (in SPH4; Napoli II)" FT /evidence="ECO:0000269|PubMed:9012689" FT /id="VAR_013809" FT VARIANT 808 FT /note="R -> C (in SPH4; Jablonec; dbSNP:rs1167814744)" FT /evidence="ECO:0000269|PubMed:11208088, FT ECO:0000269|PubMed:7530501" FT /id="VAR_013810" FT VARIANT 808 FT /note="R -> H (in SPH4; Nara; dbSNP:rs866727908)" FT /evidence="ECO:0000269|PubMed:10745622" FT /id="VAR_013811" FT VARIANT 832 FT /note="R -> H (in dbSNP:rs5025)" FT /id="VAR_014618" FT VARIANT 834 FT /note="H -> P (in SPH4; Birmingham)" FT /evidence="ECO:0000269|PubMed:11208088, FT ECO:0000269|PubMed:8943874" FT /id="VAR_013812" FT VARIANT 837 FT /note="T -> A (in SPH4; Tokyo; dbSNP:rs121912750)" FT /evidence="ECO:0000269|PubMed:9973643" FT /id="VAR_013813" FT VARIANT 837 FT /note="T -> M (in SPH4; Philadelphia)" FT /evidence="ECO:0000269|PubMed:10745622, FT ECO:0000269|PubMed:11208088, ECO:0000269|PubMed:8943874, FT ECO:0000269|PubMed:9233560" FT /id="VAR_013814" FT VARIANT 837 FT /note="T -> R (in SPH4; Nagoya)" FT /evidence="ECO:0000269|PubMed:10745622" FT /id="VAR_058043" FT VARIANT 850 FT /note="Missing (in DRTA4; dbSNP:rs121912752)" FT /evidence="ECO:0000269|PubMed:10926824" FT /id="VAR_015109" FT VARIANT 854 FT /note="P -> L (in Di(a)/Memphis-II antigen; FT dbSNP:rs2285644)" FT /evidence="ECO:0000269|PubMed:10745622, FT ECO:0000269|PubMed:8206915" FT /id="VAR_000808" FT VARIANT 858 FT /note="A -> D (in DRTA1; impairs expression at the cell FT membrane; dbSNP:rs121912751)" FT /evidence="ECO:0000269|PubMed:10926824, FT ECO:0000269|PubMed:20151848" FT /id="VAR_015108" FT VARIANT 862 FT /note="V -> I (in dbSNP:rs5026)" FT /evidence="ECO:0000269|PubMed:21849667, ECO:0000269|Ref.5" FT /id="VAR_014619" FT VARIANT 868 FT /note="P -> L (in acanthocytosis; slightly increases FT transporter activity; impairs expression at the cell FT membrane; dbSNP:rs121912759)" FT /evidence="ECO:0000269|PubMed:24121512, FT ECO:0000269|PubMed:8343110" FT /id="VAR_013815" FT VARIANT 870 FT /note="R -> W (in SPH4; Prague III; dbSNP:rs28931585)" FT /evidence="ECO:0000269|PubMed:11208088, FT ECO:0000269|PubMed:11380459, ECO:0000269|PubMed:7530501" FT /id="VAR_013816" FT MUTAGEN 85 FT /note="E->A,R: Impairs expression at the cell membrane." FT /evidence="ECO:0000269|PubMed:24121512" FT MUTAGEN 283 FT /note="R->A,E,S: Impairs expression at the cell membrane." FT /evidence="ECO:0000269|PubMed:24121512" FT MUTAGEN 642 FT /note="N->D: Loss of N-glycosylation site." FT /evidence="ECO:0000269|PubMed:24121512" FT MUTAGEN 681 FT /note="E->Q: Impairs expression at the cell membrane." FT /evidence="ECO:0000269|PubMed:24121512" FT CONFLICT 11 FT /note="M -> D (in Ref. 9; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 68 FT /note="E -> EE (in Ref. 9; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 759 FT /note="Q -> H (in Ref. 3; ABD74692)" FT /evidence="ECO:0000305" FT HELIX 5..7 FT /evidence="ECO:0007829|PDB:7UZU" FT HELIX 9..16 FT /evidence="ECO:0007829|PDB:7UZU" FT HELIX 18..21 FT /evidence="ECO:0007829|PDB:7UZU" FT HELIX 43..46 FT /evidence="ECO:0007829|PDB:7UZV" FT STRAND 58..66 FT /evidence="ECO:0007829|PDB:4KY9" FT STRAND 68..70 FT /evidence="ECO:0007829|PDB:4KY9" FT STRAND 73..88 FT /evidence="ECO:0007829|PDB:4KY9" FT STRAND 90..92 FT /evidence="ECO:0007829|PDB:4KY9" FT HELIX 104..115 FT /evidence="ECO:0007829|PDB:4KY9" FT STRAND 118..123 FT /evidence="ECO:0007829|PDB:4KY9" FT HELIX 128..141 FT /evidence="ECO:0007829|PDB:4KY9" FT HELIX 147..149 FT /evidence="ECO:0007829|PDB:4KY9" FT HELIX 150..157 FT /evidence="ECO:0007829|PDB:4KY9" FT HELIX 164..169 FT /evidence="ECO:0007829|PDB:4KY9" FT STRAND 173..175 FT /evidence="ECO:0007829|PDB:7UZV" FT STRAND 180..185 FT /evidence="ECO:0007829|PDB:7UZV" FT STRAND 188..190 FT /evidence="ECO:0007829|PDB:4KY9" FT HELIX 195..200 FT /evidence="ECO:0007829|PDB:4KY9" FT HELIX 212..219 FT /evidence="ECO:0007829|PDB:1HYN" FT STRAND 226..234 FT /evidence="ECO:0007829|PDB:4KY9" FT STRAND 241..251 FT /evidence="ECO:0007829|PDB:4KY9" FT STRAND 256..258 FT /evidence="ECO:0007829|PDB:1HYN" FT STRAND 262..270 FT /evidence="ECO:0007829|PDB:4KY9" FT HELIX 278..290 FT /evidence="ECO:0007829|PDB:4KY9" FT HELIX 292..300 FT /evidence="ECO:0007829|PDB:4KY9" FT HELIX 304..316 FT /evidence="ECO:0007829|PDB:4KY9" FT STRAND 319..321 FT /evidence="ECO:0007829|PDB:4KY9" FT HELIX 329..332 FT /evidence="ECO:0007829|PDB:4KY9" FT HELIX 333..335 FT /evidence="ECO:0007829|PDB:4KY9" FT HELIX 336..347 FT /evidence="ECO:0007829|PDB:4KY9" FT STRAND 350..352 FT /evidence="ECO:0007829|PDB:7UZV" FT HELIX 380..389 FT /evidence="ECO:0007829|PDB:7UZ3" FT HELIX 390..392 FT /evidence="ECO:0007829|PDB:7UZ3" FT HELIX 395..398 FT /evidence="ECO:0007829|PDB:7UZ3" FT HELIX 403..431 FT /evidence="ECO:0007829|PDB:7UZ3" FT HELIX 437..454 FT /evidence="ECO:0007829|PDB:7UZ3" FT STRAND 460..463 FT /evidence="ECO:0007829|PDB:7TY4" FT HELIX 466..481 FT /evidence="ECO:0007829|PDB:7UZ3" FT HELIX 486..506 FT /evidence="ECO:0007829|PDB:7UZ3" FT HELIX 509..515 FT /evidence="ECO:0007829|PDB:7UZ3" FT HELIX 518..546 FT /evidence="ECO:0007829|PDB:7UZ3" FT STRAND 560..562 FT /evidence="ECO:0007829|PDB:7UZ3" FT HELIX 570..593 FT /evidence="ECO:0007829|PDB:7UZ3" FT STRAND 594..597 FT /evidence="ECO:0007829|PDB:7TY8" FT HELIX 599..607 FT /evidence="ECO:0007829|PDB:7UZ3" FT HELIX 609..622 FT /evidence="ECO:0007829|PDB:7UZ3" FT STRAND 636..638 FT /evidence="ECO:0007829|PDB:7UZ3" FT TURN 643..645 FT /evidence="ECO:0007829|PDB:7UZ3" FT STRAND 655..657 FT /evidence="ECO:0007829|PDB:7UZ3" FT HELIX 661..666 FT /evidence="ECO:0007829|PDB:7UZ3" FT HELIX 668..689 FT /evidence="ECO:0007829|PDB:7UZ3" FT HELIX 692..694 FT /evidence="ECO:0007829|PDB:7UZ3" FT HELIX 702..718 FT /evidence="ECO:0007829|PDB:7UZ3" FT STRAND 725..727 FT /evidence="ECO:0007829|PDB:7TY4" FT HELIX 728..737 FT /evidence="ECO:0007829|PDB:7UZ3" FT STRAND 739..741 FT /evidence="ECO:0007829|PDB:7UZ3" FT STRAND 753..756 FT /evidence="ECO:0007829|PDB:7UZ3" FT HELIX 761..772 FT /evidence="ECO:0007829|PDB:7UZ3" FT HELIX 773..775 FT /evidence="ECO:0007829|PDB:7UZ3" FT HELIX 777..780 FT /evidence="ECO:0007829|PDB:7UZ3" FT HELIX 785..798 FT /evidence="ECO:0007829|PDB:7UZ3" FT TURN 799..802 FT /evidence="ECO:0007829|PDB:7UZ3" FT HELIX 804..811 FT /evidence="ECO:0007829|PDB:7UZ3" FT HELIX 816..818 FT /evidence="ECO:0007829|PDB:7UZ3" FT HELIX 823..826 FT /evidence="ECO:0007829|PDB:7UZ3" FT HELIX 830..851 FT /evidence="ECO:0007829|PDB:7UZ3" FT HELIX 854..858 FT /evidence="ECO:0007829|PDB:7UZ3" FT HELIX 859..864 FT /evidence="ECO:0007829|PDB:7UZ3" FT HELIX 866..872 FT /evidence="ECO:0007829|PDB:7UZ3" FT HELIX 874..877 FT /evidence="ECO:0007829|PDB:7UZ3" FT HELIX 880..886 FT /evidence="ECO:0007829|PDB:7UZ3" 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 //