B3AT_HUMAN
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 03-AUG-2022, entry version 265.
DE RecName: Full=Band 3 anion transport protein;
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; 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 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 [24]
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 [25]
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 [26]
RP INTERACTION WITH TM139.
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 [27]
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 [28]
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 [29]
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 [30]
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 [31]
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 [32]
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 [33]
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 [34]
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 [35]
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, AND CHARACTERIZATION OF VARIANT ACANTHOCYTOSIS LEU-868.
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 [36]
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 [37]
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 [38]
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 [39]
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 [40]
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 [41]
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 [42]
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 [43]
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 [44]
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 [45]
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 [46]
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 [47]
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 [48]
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 [49]
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 [50]
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 [51]
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 [52]
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 [53]
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 [54]
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 [55]
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 [56]
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 [57]
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 [58]
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 [59]
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 [60]
RP VARIANTS DRTA4 ASP-701 AND VAL-850 DEL, VARIANT DRTA1 ASP-858, FUNCTION,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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 [61]
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 [62]
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 [63]
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 [64]
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 [65]
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 [66]
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 [67]
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 [68]
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 [69]
RP VARIANT DRTA1 ARG-609, FUNCTION, SUBCELLULAR LOCATION, AND CHARACTERIZATION
RP OF VARIANT DRTA1 ARG-609.
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 [70]
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 [71]
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, AND CHARACTERIZATION OF VARIANTS
RP SPH4 TYR-705 AND GLN-760.
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 [72]
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 [73]
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).
CC -!- FUNCTION: Functions both as a transporter that mediates electroneutral
CC anion exchange across the cell membrane and as a structural protein.
CC Major integral membrane glycoprotein 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. Functions as a transporter that mediates the 1:1 exchange
CC of inorganic anions across the erythrocyte membrane. Mediates chloride-
CC bicarbonate exchange in the kidney, and is required for normal
CC acidification of the urine. {ECO:0000269|PubMed:10926824,
CC ECO:0000269|PubMed:14734552, ECO:0000269|PubMed:1538405,
CC ECO:0000269|PubMed:20151848, ECO:0000269|PubMed:24121512}.
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. Interacts (via cytoplasmic N-terminal domain)
CC with ANK1 (via N-terminal ANK repeats); tetramer formation is critical
CC for ankyrin association. Interacts with STOM. Isoform 2 interacts with
CC TM139 (PubMed:26049106). {ECO:0000269|PubMed:11049968,
CC ECO:0000269|PubMed:20151848, ECO:0000269|PubMed:23219802,
CC ECO:0000269|PubMed:26049106, ECO:0000269|PubMed:7665627}.
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 -!- 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]: A hereditary
CC hematologic disorder characterized by ovalocytic erythrocytes that are
CC rigid and exhibit reduced expression of many erythrocyte antigens.
CC Clinical manifestations include mild hemolysis, intermittent jaundice
CC and gallstones. However, the disorder is most often asymptomatic.
CC {ECO:0000269|PubMed:1538405, ECO:0000269|PubMed:1722314}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Spherocytosis 4 (SPH4) [MIM:612653]: Spherocytosis is a
CC hematologic disorder leading to chronic hemolytic anemia and
CC characterized by numerous abnormally shaped erythrocytes which are
CC generally spheroidal. {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:9854053}. Note=The disease is caused by variants
CC affecting the gene represented in this 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="http://atlasgeneticsoncology.org/Genes/SLC4A1ID42325ch17q21.html";
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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 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 AlphaFoldDB; P02730; -.
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-Linked glycan (3 sites).
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; P02730; -.
DR PeptideAtlas; P02730; -.
DR PRIDE; P02730; -.
DR ProteomicsDB; 51557; -.
DR ABCD; P02730; 36 sequenced antibodies.
DR Antibodypedia; 2977; 317 antibodies from 35 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 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; VWGRPHL; -.
DR OrthoDB; 265068at2759; -.
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; 36 hits in 1083 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 139 other tissues.
DR ExpressionAtlas; P02730; baseline and differential.
DR Genevisible; P02730; HS.
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:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030018; C:Z disc; ISS:UniProtKB.
DR GO; GO:0008509; F:anion transmembrane transporter activity; TAS:ProtInc.
DR GO; GO:0015301; F:anion:anion antiporter activity; IDA: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:0030492; F:hemoglobin binding; IEA:Ensembl.
DR GO; GO:0005452; F:inorganic anion exchanger activity; IDA:UniProtKB.
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:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006820; P:anion transport; IDA:UniProtKB.
DR GO; GO:0015701; P:bicarbonate transport; IDA:UniProtKB.
DR GO; GO:0007596; P:blood coagulation; IEA:Ensembl.
DR GO; GO:0006873; P:cellular ion homeostasis; TAS:ProtInc.
DR GO; GO:0006821; P:chloride transport; ISS:UniProtKB.
DR GO; GO:0048821; P:erythrocyte development; IEA:Ensembl.
DR GO; GO:0050801; P:ion homeostasis; IBA:GO_Central.
DR GO; GO:1904539; P:negative regulation of glycolytic process through fructose-6-phosphate; IEA:Ensembl.
DR GO; GO:0051354; P:negative regulation of oxidoreductase activity; 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; 3.40.930.10; -; 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 PANTHER; PTHR11453; PTHR11453; 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; SSF55804; 1.
DR TIGRFAMs; TIGR00834; ae; 1.
DR PROSITE; PS00219; ANION_EXCHANGER_1; 1.
DR PROSITE; PS00220; ANION_EXCHANGER_2; 1.
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 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"
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 unknown pathological significance; Montefiore;
FT 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; 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"
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 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 STRAND 9..12
FT /evidence="ECO:0007829|PDB:2BTA"
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:1HYN"
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 349..351
FT /evidence="ECO:0007829|PDB:1HYN"
FT HELIX 383..393
FT /evidence="ECO:0007829|PDB:4YZF"
FT TURN 394..400
FT /evidence="ECO:0007829|PDB:4YZF"
FT HELIX 403..430
FT /evidence="ECO:0007829|PDB:4YZF"
FT TURN 431..433
FT /evidence="ECO:0007829|PDB:4YZF"
FT HELIX 437..454
FT /evidence="ECO:0007829|PDB:4YZF"
FT HELIX 466..481
FT /evidence="ECO:0007829|PDB:4YZF"
FT HELIX 486..506
FT /evidence="ECO:0007829|PDB:4YZF"
FT HELIX 509..515
FT /evidence="ECO:0007829|PDB:4YZF"
FT HELIX 518..546
FT /evidence="ECO:0007829|PDB:4YZF"
FT HELIX 570..593
FT /evidence="ECO:0007829|PDB:4YZF"
FT STRAND 594..597
FT /evidence="ECO:0007829|PDB:4YZF"
FT HELIX 599..607
FT /evidence="ECO:0007829|PDB:4YZF"
FT HELIX 609..623
FT /evidence="ECO:0007829|PDB:4YZF"
FT STRAND 655..657
FT /evidence="ECO:0007829|PDB:4YZF"
FT HELIX 663..666
FT /evidence="ECO:0007829|PDB:4YZF"
FT HELIX 668..689
FT /evidence="ECO:0007829|PDB:4YZF"
FT HELIX 703..718
FT /evidence="ECO:0007829|PDB:4YZF"
FT HELIX 728..735
FT /evidence="ECO:0007829|PDB:4YZF"
FT HELIX 761..780
FT /evidence="ECO:0007829|PDB:4YZF"
FT HELIX 785..799
FT /evidence="ECO:0007829|PDB:4YZF"
FT HELIX 804..813
FT /evidence="ECO:0007829|PDB:4YZF"
FT HELIX 823..827
FT /evidence="ECO:0007829|PDB:4YZF"
FT TURN 828..831
FT /evidence="ECO:0007829|PDB:4YZF"
FT HELIX 832..850
FT /evidence="ECO:0007829|PDB:4YZF"
FT HELIX 854..858
FT /evidence="ECO:0007829|PDB:4YZF"
FT HELIX 859..873
FT /evidence="ECO:0007829|PDB:4YZF"
FT TURN 875..877
FT /evidence="ECO:0007829|PDB:4YZF"
FT TURN 880..882
FT /evidence="ECO:0007829|PDB:4YZF"
FT HELIX 883..886
FT /evidence="ECO:0007829|PDB:4YZF"
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
