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Band 3 anion transport protein (Anion exchange protein 1) (AE 1) (Anion exchanger 1) (Solute carrier family 4 member 1) (CD antigen CD233)

 B3AT_HUMAN              Reviewed;         911 AA.
P02730; G4V2I6; P78487; Q1ZZ45; Q4KKW9; Q4VB84; Q9UCY7; Q9UDJ1;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 3.
30-AUG-2017, entry version 230.
RecName: Full=Band 3 anion transport protein;
AltName: Full=Anion exchange protein 1;
Short=AE 1;
Short=Anion exchanger 1;
AltName: Full=Solute carrier family 4 member 1;
AltName: CD_antigen=CD233;
Name=SLC4A1; Synonyms=AE1, DI, EPB3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Blood;
PubMed=3223947; DOI=10.1042/bj2560703;
Tanner M.J.A., Martin P.G., High S.;
"The complete amino acid sequence of the human erythrocyte membrane
anion-transport protein deduced from the cDNA sequence.";
Biochem. J. 256:703-712(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2594752; DOI=10.1073/pnas.86.23.9089;
Lux S.E., John K.M., Kopito R.R., Lodish H.F.;
"Cloning and characterization of band 3, the human erythrocyte anion-
exchange protein (AE1).";
Proc. Natl. Acad. Sci. U.S.A. 86:9089-9093(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-38.
PubMed=16252102; DOI=10.1007/s00467-005-2061-z;
Choo K.E., Nicoli T.K., Bruce L.J., Tanner M.J., Ruiz-Linares A.,
Wrong O.M.;
"Recessive distal renal tubular acidosis in Sarawak caused by AE1
mutations.";
Pediatr. Nephrol. 21:212-217(2006).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Blood;
Hsu K., Huang S.-Y., Chi N., Lin M.;
"Novel anion exchanger-1 expression in Southeast Asian populations.";
Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-38; GLU-56;
LYS-508 AND ILE-862.
SeattleSNPs variation discovery resource;
Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-27.
TISSUE=Cerebellum;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 1-199; 220-292 AND 347-370, AND ACETYLATION AT
MET-1.
PubMed=2790053; DOI=10.1016/0167-4838(89)90116-7;
Yannoukakos D., Vasseur C., Blouquit Y., Bursaux E., Wajcman H.;
"Primary structure of the cytoplasmic domain of human erythrocyte
protein band 3. Comparison with its sequence in the mouse.";
Biochim. Biophys. Acta 998:43-49(1989).
[9]
PROTEIN SEQUENCE OF 1-201.
PubMed=6345535;
Kaul R.K., Murthy S.N.P., Reddy A.G., Steck T.L., Kohler H.;
"Amino acid sequence of the N alpha-terminal 201 residues of human
erythrocyte membrane band 3.";
J. Biol. Chem. 258:7981-7990(1983).
[10]
PROTEIN SEQUENCE OF 1-3.
PubMed=701248;
Drickamer L.K.;
"Orientation of the band 3 polypeptide from human erythrocyte
membranes. Identification of NH2-terminal sequence and site of
carbohydrate attachment.";
J. Biol. Chem. 253:7242-7248(1978).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 66-180 (ISOFORM 2), SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
PubMed=7506871;
Kollert-Jons A., Wagner S., Hubner S., Appelhans H., Drenckhahn D.;
"Anion exchanger 1 in human kidney and oncocytoma differs from
erythroid AE1 in its NH2 terminus.";
Am. J. Physiol. 265:F813-F821(1993).
[12]
PROTEIN SEQUENCE OF 361-372; 390-399; 604-613; 632-639; 647-656;
699-729; 731-743; 761-781 AND 818-826, AND SYNTHESIS OF 646-656 AND
817-827.
PubMed=1527044;
Kang D., Okubo K., Hamasaki N., Kuroda N., Shiraki H.;
"A structural study of the membrane domain of band 3 by tryptic
digestion. Conformational change of band 3 in situ induced by alkali
treatment.";
J. Biol. Chem. 267:19211-19217(1992).
[13]
PROTEIN SEQUENCE OF 559-630.
PubMed=6615451; DOI=10.1042/bj2130577;
Brock C.J., Tanner M.J.A., Kempf C.;
"The human erythrocyte anion-transport protein. Partial amino acid
sequence, conformation and a possible molecular mechanism for anion
exchange.";
Biochem. J. 213:577-586(1983).
[14]
PROTEIN SEQUENCE OF 665-688, AND ROLE OF GLU-681.
PubMed=1352774;
Jennings M.L., Smith J.S.;
"Anion-proton cotransport through the human red blood cell band 3
protein. Role of glutamate 681.";
J. Biol. Chem. 267:13964-13971(1992).
[15]
NUCLEOTIDE SEQUENCE [MRNA] OF 757-778, AND VARIANT SPH4 ASP-771.
PubMed=8547122; DOI=10.1111/j.1365-2141.1995.tb05393.x;
Maillet P., Vallier A., Reinhart W.H., Wyss E.J., Ott P., Texier P.,
Baklouti F., Tanner M.J.A., Delaunay J., Alloisio N.;
"Band 3 Chur: a variant associated with band 3-deficient hereditary
spherocytosis and substitution in a highly conserved position of
transmembrane segment 11.";
Br. J. Haematol. 91:804-810(1995).
[16]
PROTEIN SEQUENCE OF 834-911.
PubMed=3372523;
Kawano Y., Okubo K., Tokunaga F., Miyata T., Iwanaga S., Hamasaki N.;
"Localization of the pyridoxal phosphate binding site at the COOH-
terminal region of erythrocyte band 3 protein.";
J. Biol. Chem. 263:8232-8238(1988).
[17]
PHOSPHORYLATION AT TYR-8; TYR-21 AND TYR-46.
PubMed=1998697; DOI=10.1016/0005-2736(91)90291-F;
Yannoukakos D., Vasseur C., Piau J.-P., Wajcman H., Bursaux E.;
"Phosphorylation sites in human erythrocyte band 3 protein.";
Biochim. Biophys. Acta 1061:253-266(1991).
[18]
PALMITOYLATION AT CYS-843.
PubMed=1885574;
Okubo K., Hamasaki N., Hara K., Kageura M.;
"Palmitoylation of cysteine 69 from the COOH-terminal of band 3
protein in the human erythrocyte membrane. Acylation occurs in the
middle of the consensus sequence of F--I-IICLAVL found in band 3
protein and G2 protein of Rift Valley fever virus.";
J. Biol. Chem. 266:16420-16424(1991).
[19]
INTERACTION WITH ANK1.
PubMed=7665627; DOI=10.1074/jbc.270.37.22050;
Michaely P., Bennett V.;
"The ANK repeats of erythrocyte ankyrin form two distinct but
cooperative binding sites for the erythrocyte anion exchanger.";
J. Biol. Chem. 270:22050-22057(1995).
[20]
GLYCOSYLATION AT ASN-642.
PubMed=10861210; DOI=10.1042/0264-6021:3490051;
Li J., Quilty J., Popov M., Reithmeier R.A.;
"Processing of N-linked oligosaccharide depends on its location in the
anion exchanger, AE1, membrane glycoprotein.";
Biochem. J. 349:51-57(2000).
[21]
PHOSPHORYLATION AT TYR-8; TYR-21; TYR-359 AND TYR-904.
PubMed=10942405;
Brunati A.M., Bordin L., Clari G., James P., Quadroni M., Baritono E.,
Pinna L.A., Donella-Deana A.;
"Sequential phosphorylation of protein band 3 by Syk and Lyn tyrosine
kinases in intact human erythrocytes: identification of primary and
secondary phosphorylation sites.";
Blood 96:1550-1557(2000).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[23]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH STOM, AND
SUBUNIT.
PubMed=23219802; DOI=10.1016/j.bbamem.2012.11.030;
Rungaldier S., Oberwagner W., Salzer U., Csaszar E., Prohaska R.;
"Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1
in human erythrocyte membrane domains.";
Biochim. Biophys. Acta 1828:956-966(2013).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[25]
INTERACTION WITH TM139.
PubMed=26049106; DOI=10.1016/j.bbrc.2015.05.128;
Nuiplot N.O., Junking M., Duangtum N., Khunchai S., Sawasdee N.,
Yenchitsomanus P.T., Akkarapatumwong V.;
"Transmembrane protein 139 (TMEM139) interacts with human kidney
isoform of anion exchanger 1 (kAE1).";
Biochem. Biophys. Res. Commun. 463:706-711(2015).
[26]
STRUCTURE BY ELECTRON CRYOMICROSCOPY.
PubMed=8508760;
Wang D.N., Kuehlbrandt W., Sarabia V.E., Reithmeier R.A.F.;
"Two-dimensional structure of the membrane domain of human band 3, the
anion transport protein of the erythrocyte membrane.";
EMBO J. 12:2233-2239(1993).
[27]
STRUCTURE BY ELECTRON CRYOMICROSCOPY.
PubMed=8045253;
Wang D.N., Sarabia V.E., Reithmeier R.A.F., Kuehlbrandt W.;
"Three-dimensional map of the dimeric membrane domain of the human
erythrocyte anion exchanger, Band 3.";
EMBO J. 13:3230-3235(1994).
[28]
STRUCTURE BY NMR OF 405-424 AND 436-456.
PubMed=8168533; DOI=10.1111/j.1432-1033.1994.tb18757.x;
Gargaro A.R., Bloomberg G.B., Dempsey C.E., Murray M., Tanner M.J.A.;
"The solution structures of the first and second transmembrane-
spanning segments of band 3.";
Eur. J. Biochem. 221:445-454(1994).
[29]
STRUCTURE BY NMR OF 1-16.
PubMed=8527430; DOI=10.1021/bi00051a005;
Schneider M.L., Post C.B.;
"Solution structure of a band 3 peptide inhibitor bound to aldolase: a
proposed mechanism for regulating binding by tyrosine
phosphorylation.";
Biochemistry 34:16574-16584(1995).
[30]
STRUCTURE BY NMR OF 1-16.
PubMed=9454576; DOI=10.1021/bi971445b;
Eisenmesser E.Z., Post C.B.;
"Insights into tyrosine phosphorylation control of protein-protein
association from the NMR structure of a band 3 peptide inhibitor bound
to glyceraldehyde-3-phosphate dehydrogenase.";
Biochemistry 37:867-877(1998).
[31]
STRUCTURE BY NMR OF 389-430.
PubMed=9765907; DOI=10.1042/bst0260516;
Chambers E.J., Askin D., Bloomberg G.B., Ring S.M., Tanner M.J.;
"Studies on the structure of a transmembrane region and a cytoplasmic
loop of the human red cell anion exchanger.";
Biochem. Soc. Trans. 26:516-520(1998).
[32]
STRUCTURE BY NMR OF 803-835.
PubMed=9709005; DOI=10.1021/bi973158d;
Askin D., Bloomberg G.B., Chambers E.J., Tanner M.J.;
"NMR solution structure of a cytoplasmic surface loop of the human red
cell anion transporter, band 3.";
Biochemistry 37:11670-11678(1998).
[33]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-379, AND SUBUNIT.
PubMed=11049968;
Zhang D., Kiyatkin A., Bolin J.T., Low P.S.;
"Crystallographic structure and functional interpretation of the
cytoplasmic domain of erythrocyte membrane band 3.";
Blood 96:2925-2933(2000).
[34]
X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS) OF 51-356, FUNCTION,
SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-642, MUTAGENESIS OF GLU-85;
ARG-283; ASN-642 AND GLU-681, AND CHARACTERIZATION OF VARIANT
ACANTHOCYTOSIS LEU-868.
PubMed=24121512; DOI=10.1074/jbc.M113.511865;
Shnitsar V., Li J., Li X., Calmettes C., Basu A., Casey J.R.,
Moraes T.F., Reithmeier R.A.;
"A substrate access tunnel in the cytosolic domain is not an essential
feature of the solute carrier 4 (SLC4) family of bicarbonate
transporters.";
J. Biol. Chem. 288:33848-33860(2013).
[35]
X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS), TISSUE SPECIFICITY,
SUBCELLULAR LOCATION, TOPOLOGY, AND GLYCOSYLATION.
PubMed=26542571; DOI=10.1126/science.aaa4335;
Arakawa T., Kobayashi-Yurugi T., Alguel Y., Iwanari H., Hatae H.,
Iwata M., Abe Y., Hino T., Ikeda-Suno C., Kuma H., Kang D., Murata T.,
Hamakubo T., Cameron A.D., Kobayashi T., Hamasaki N., Iwata S.;
"Crystal structure of the anion exchanger domain of human erythrocyte
band 3.";
Science 350:680-684(2015).
[36]
VARIANT MEMPHIS GLU-56.
PubMed=1678289;
Yannoukakos D., Vasseur C., Driancourt C., Blouquit Y., Delauney J.,
Wajcman H., Bursaux E.;
"Human erythrocyte band 3 polymorphism (band 3 Memphis):
characterization of the structural modification (Lys 56-->Glu) by
protein chemistry methods.";
Blood 78:1117-1120(1991).
[37]
VARIANT SAO 400-ALA--ALA-408 DEL, AND VARIANT MEMPHIS GLU-56.
PubMed=1722314; DOI=10.1073/pnas.88.24.11022;
Jarolim P., Palek J., Amato D., Hassan K., Sapak P., Nurse G.T.,
Rubin H.L., Zhai S., Sahr K.E., Liu S.-C.;
"Deletion in erythrocyte band 3 gene in malaria-resistant Southeast
Asian ovalocytosis.";
Proc. Natl. Acad. Sci. U.S.A. 88:11022-11026(1991).
[38]
VARIANT SPH4 ARG-327.
PubMed=1378323;
Jarolim P., Palek J., Rubin H.L., Prchal J.T., Korsgren C.,
Cohen C.M.;
"Band 3 Tuscaloosa: Pro-327-->Arg substitution in the cytoplasmic
domain of erythrocyte band 3 protein associated with spherocytic
hemolytic anemia and partial deficiency of protein 4.2.";
Blood 80:523-529(1992).
[39]
VARIANT SAO 400-ALA--ALA-408 DEL, CHARACTERIZATION OF VARIANT SAO
400-ALA--ALA-408 DEL, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=1538405; DOI=10.1016/0022-2836(92)90254-H;
Schofield A.E., Tanner M.J.A., Pinder J.C., Clough B., Bayley P.M.,
Nash G.B., Dluzewski A.R., Reardon D.M., Cox T.M., Wilson R.J.M.,
Gratzer W.B.;
"Basis of unique red cell membrane properties in hereditary
ovalocytosis.";
J. Mol. Biol. 223:949-958(1992).
[40]
VARIANT ACANTHOCYTOSIS LEU-868.
PubMed=8343110; DOI=10.1042/bj2930317;
Bruce L.J., Kay M.M., Lawrence C., Tanner M.J.;
"Band 3 HT, a human red-cell variant associated with acanthocytosis
and increased anion transport, carries the mutation Pro-868-->Leu in
the membrane domain of band 3.";
Biochem. J. 293:317-320(1993).
[41]
VARIANT LYS-40.
PubMed=8471774;
Rybicki A.C., Qiu J.J.H., Musto S., Rosen N.L., Nagel R.L.,
Schwartz R.S.;
"Human erythrocyte protein 4.2 deficiency associated with hemolytic
anemia and a homozygous 40 glutamic acid-->lysine substitution in the
cytoplasmic domain of band 3 (band 3Montefiore).";
Blood 81:2155-2165(1993).
[42]
VARIANTS BLOOD GROUP DI(A)/MEMPHIS-II GLU-56 AND LEU-854.
PubMed=8206915;
Bruce L.J., Anstee D.J., Spring F.A., Tanner M.J.;
"Band 3 Memphis variant II. Altered stilbene disulfonate binding and
the Diego (Dia) blood group antigen are associated with the human
erythrocyte band 3 mutation Pro-854-->Leu.";
J. Biol. Chem. 269:16155-16158(1994).
[43]
VARIANT BLOOD GROUP WR(A) LYS-658.
PubMed=7812009;
Bruce L.J., Ring S.M., Anstee D.J., Reid M.E., Wilkinson S.,
Tanner M.J.;
"Changes in the blood group Wright antigens are associated with a
mutation at amino acid 658 in human erythrocyte band 3: a site of
interaction between band 3 and glycophorin A under certain
conditions.";
Blood 85:541-547(1995).
[44]
VARIANTS SPH4 GLN-760; TRP-760; CYS-808 AND TRP-870.
PubMed=7530501;
Jarolim P., Rubin H.L., Brabec V., Chrobak L., Zolotarev A.S.,
Alper S.L., Brugnara C., Wichterle H., Palek J.;
"Mutations of conserved arginines in the membrane domain of erythroid
band 3 lead to a decrease in membrane-associated band 3 and to the
phenotype of hereditary spherocytosis.";
Blood 85:634-640(1995).
[45]
VARIANTS SPH4 ASP-285; GLU-455; PRO-707; PRO-834 AND MET-837.
PubMed=8943874;
Jarolim P., Murray J.L., Rubin H.L., Taylor W.M., Prchal J.T.,
Ballas S.K., Snyder L.M., Chrobak L., Melrose W.D., Brabec V.,
Palek J.;
"Characterization of 13 novel band 3 gene defects in hereditary
spherocytosis with band 3 deficiency.";
Blood 88:4366-4374(1996).
[46]
VARIANTS SPH4 CYS-518 AND MET-663 DEL, AND VARIANT LYS-40.
PubMed=8640229; DOI=10.1038/ng0696-214;
Eber S.W., Gonzalez J.M., Lux M.L., Scarpa A.L., Tse W.T.,
Dornwell M., Herbers J., Kugler W., Oezcan R., Pekrun A.,
Gallagher P.G., Schroeter W., Forget B.G., Lux S.E.;
"Ankyrin-1 mutations are a major cause of dominant and recessive
hereditary spherocytosis.";
Nat. Genet. 13:214-218(1996).
[47]
VARIANTS SPH4 SER-147 AND MET-488.
PubMed=9207478;
Alloisio N., Texier P., Vallier A., Ribeiro M.L., Morle L., Bozon M.,
Bursaux E., Maillet P., Goncalves P., Tanner M.J., Tamagnini G.,
Delaunay J.;
"Modulation of clinical expression and band 3 deficiency in hereditary
spherocytosis.";
Blood 90:414-420(1997).
[48]
VARIANT SPH4 ASN-783, AND VARIANTS ALA-38 AND MET-73.
PubMed=9012689; DOI=10.1046/j.1365-2141.1997.8732504.x;
Miraglia del Giudice E., Vallier A., Maillet P., Perrotta S.,
Cutillo S., Iolascon A., Tanner M.J., Delaunay J., Alloisio N.;
"Novel band 3 variants (bands 3 Foggia, Napoli I and Napoli II)
associated with hereditary spherocytosis and band 3 deficiency: status
of the D38A polymorphism within the EPB3 locus.";
Br. J. Haematol. 96:70-76(1997).
[49]
VARIANTS SPH4 CYS-490 AND MET-837.
PubMed=9233560; DOI=10.1046/j.1365-2141.1997.1893005.x;
Dhermy D., Galand C., Bournier O., Boulanger L., Cynober T.,
Schismanoff P.O., Bursaux E., Tchernia G., Boivin P., Garbarz M.;
"Heterogenous band 3 deficiency in hereditary spherocytosis related to
different band 3 gene defects.";
Br. J. Haematol. 98:32-40(1997).
[50]
ERRATUM.
Dhermy D., Galand C., Bournier O., Boulanger L., Cynober T.,
Schismanoff P.O., Bursaux E., Tchernia G., Boivin P., Garbarz M.;
Br. J. Haematol. 99:474-474(1997).
[51]
VARIANTS AD-DRTA CYS-589; HIS-589 AND PHE-613.
PubMed=9312167; DOI=10.1172/JCI119694;
Bruce L.J., Cope D.L., Jones G.K., Schofield A.E., Burley M.,
Povey S., Unwin R.J., Wrong O., Tanner M.J.;
"Familial distal renal tubular acidosis is associated with mutations
in the red cell anion exchanger (Band 3, AE1) gene.";
J. Clin. Invest. 100:1693-1707(1997).
[52]
VARIANTS BLOOD GROUPS RB(A); TR(A) AND WD(A).
PubMed=9191821; DOI=10.1046/j.1537-2995.1997.37697335155.x;
Jarolim P., Murray J.L., Rubin H.L., Smart E., Moulds J.M.;
"Blood group antigens Rb(a), Tr(a), and Wd(a) are located in the third
ectoplasmic loop of erythroid band 3.";
Transfusion 37:607-615(1997).
[53]
VARIANT SPH4 ALA-837.
PubMed=9973643; DOI=10.1159/000040904;
Iwase S., Ideguchi H., Takao M., Horiguchi-Yamada J., Iwasaki M.,
Takahara S., Sekikawa T., Mochizuki S., Yamada H.;
"Band 3 Tokyo: Thr837-->Ala837 substitution in erythrocyte band 3
protein associated with spherocytic hemolysis.";
Acta Haematol. 100:200-203(1998).
[54]
VARIANTS BLOOD GROUPS BOW; BP(A); ELO; HG(A); MO(A); VG(A) AND WU.
PubMed=9845551;
Jarolim P., Rubin H.L., Zakova D., Storry J., Reid M.E.;
"Characterization of seven low incidence blood group antigens carried
by erythrocyte band 3 protein.";
Blood 92:4836-4843(1998).
[55]
VARIANT DRTA-HA ASP-701.
PubMed=9854053; DOI=10.1172/JCI4836;
Tanphaichitr V.S., Sumboonnanonda A., Ideguchi H., Shayakul C.,
Brugnara C., Takao M., Veerakul G., Alper S.L.;
"Novel AE1 mutations in recessive distal renal tubular acidosis: loss-
of-function is rescued by glycophorin A.";
J. Clin. Invest. 102:2173-2179(1998).
[56]
VARIANTS AD-DRTA HIS-589 AND SER-589.
PubMed=9600966; DOI=10.1073/pnas.95.11.6337;
Karet F.E., Gainza F.J., Gyory A.Z., Unwin R.J., Wrong O.,
Tanner M.J.A., Nayir A., Alpay H., Santos F., Hulton S.A.,
Bakkaloglu A., Ozen S., Cunningham M.J., di Pietro A., Walker W.G.,
Lifton R.P.;
"Mutations in the chloride-bicarbonate exchanger gene AE1 cause
autosomal dominant but not autosomal recessive distal renal tubular
acidosis.";
Proc. Natl. Acad. Sci. U.S.A. 95:6337-6342(1998).
[57]
VARIANTS BLOOD GROUP WU.
PubMed=9709782; DOI=10.1046/j.1537-2995.1998.38898375513.x;
Zelinski T., McManus K., Punter F., Moulds M., Coghlan G.;
"A Gly565-->Ala substitution in human erythroid band 3 accounts for
the Wu blood group polymorphism.";
Transfusion 38:745-748(1998).
[58]
VARIANT SPH4 HIS-490.
PubMed=10580570;
Lima P.R.M., Sales T.S.I., Costa F.F., Saad S.T.O.;
"Arginine 490 is a hot spot for mutation in the band 3 gene in
hereditary spherocytosis.";
Eur. J. Haematol. 63:360-361(1999).
[59]
VARIANTS DRTA-HA ASP-701 AND VAL-850 DEL, VARIANT AD-DRTA ASP-858,
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=10926824; DOI=10.1042/bj3500041;
Bruce L.J., Wrong O., Toye A.M., Young M.T., Ogle G., Ismail Z.,
Sinha A.K., McMaster P., Hwaihwanje I., Nash G.B., Hart S., Lavu E.,
Palmer R., Othman A., Unwin R.J., Tanner M.J.A.;
"Band 3 mutations, renal tubular acidosis and South-East Asian
ovalocytosis in Malaysia and Papua New Guinea: loss of up to 95% band
3 transport in red cells.";
Biochem. J. 350:41-51(2000).
[60]
VARIANT SPH4 MET-488.
PubMed=10942416;
Ribeiro M.L., Alloisio N., Almeida H., Gomes C., Texier P., Lemos C.,
Mimoso G., Morle L., Bey-Cabet F., Rudigoz R.-C., Delaunay J.,
Tamagnini G.;
"Severe hereditary spherocytosis and distal renal tubular acidosis
associated with the total absence of band 3.";
Blood 96:1602-1604(2000).
[61]
VARIANTS SPH4 ARG-130; ARG-455; ARG-714; TRP-760; GLN-760; HIS-808;
ARG-837 AND MET-837, AND VARIANTS ALA-38; GLU-56; ASP-72 AND LEU-854.
PubMed=10745622;
Yawata Y., Kanzaki A., Yawata A., Doerfler W., Oezcan R., Eber S.W.;
"Characteristic features of the genotype and phenotype of hereditary
spherocytosis in the Japanese population.";
Int. J. Hematol. 71:118-135(2000).
[62]
CHARACTERIZATION OF VARIANTS PRO-707; GLN-760; TRP-760; CYS-808;
PRO-834; MET-837 AND TRP-870.
PubMed=11208088; DOI=10.1034/j.1600-0854.2000.011208.x;
Quilty J.A., Reithmeier R.A.;
"Trafficking and folding defects in hereditary spherocytosis mutants
of the human red cell anion exchanger.";
Traffic 1:987-998(2000).
[63]
VARIANTS BLOOD GROUP NFLD+ ASP-429 AND ALA-561, AND VARIANT BLOOD
GROUP BOW+ SER-561.
PubMed=10738034; DOI=10.1046/j.1537-2995.2000.40030325.x;
McManus K., Pongoski J., Coghlan G., Zelinski T.;
"Amino acid substitutions in human erythroid protein band 3 account
for the low-incidence antigens NFLD and BOW.";
Transfusion 40:325-329(2000).
[64]
VARIANT BLOOD GROUP FR(A+) LYS-480.
PubMed=11061863; DOI=10.1046/j.1537-2995.2000.40101246.x;
McManus K., Lupe K., Coghlan G., Zelinski T.;
"An amino acid substitution in the putative second extracellular loop
of RBC band 3 accounts for the Froese blood group polymorphism.";
Transfusion 40:1246-1249(2000).
[65]
VARIANTS BLOOD GROUP SW(A+) GLN-646 AND TRP-646.
PubMed=11155072; DOI=10.1159/000056733;
Zelinski T., Rusnak A., McManus K., Coghlan G.;
"Distinctive Swann blood group genotypes: molecular investigations.";
Vox Sang. 79:215-218(2000).
[66]
VARIANTS SPH4 LYS-90 AND TRP-870.
PubMed=11380459; DOI=10.1046/j.1365-2141.2001.02800.x;
Bracher N.A., Lyons C.A., Wessels G., Mansvelt E., Coetzer T.L.;
"Band 3 Cape Town (E90K) causes severe hereditary spherocytosis in
combination with band 3 Prague III.";
Br. J. Haematol. 113:689-693(2001).
[67]
VARIANT DRTA-HA PRO-602, AND VARIANT DRTA-NRC PRO-773.
PubMed=15211439; DOI=10.1053/j.ajkd.2004.03.033;
Sritippayawan S., Sumboonnanonda A., Vasuvattakul S., Keskanokwong T.,
Sawasdee N., Paemanee A., Thuwajit P., Wilairat P., Nimmannit S.,
Malasit P., Yenchitsomanus P.T.;
"Novel compound heterozygous SLC4A1 mutations in Thai patients with
autosomal recessive distal renal tubular acidosis.";
Am. J. Kidney Dis. 44:64-70(2004).
[68]
VARIANT AD-DRTA ARG-609, FUNCTION, SUBCELLULAR LOCATION, AND
CHARACTERIZATION OF VARIANT AD-DRTA ARG-609.
PubMed=14734552; DOI=10.1074/jbc.M400188200;
Rungroj N., Devonald M.A.J., Cuthbert A.W., Reimann F.,
Akkarapatumwong V., Yenchitsomanus P.-T., Bennett W.M., Karet F.E.;
"A novel missense mutation in AE1 causing autosomal dominant distal
renal tubular acidosis retains normal transport function but is
mistargeted in polarized epithelial cells.";
J. Biol. Chem. 279:13833-13838(2004).
[69]
VARIANT SPH4 LYS-663.
PubMed=15813913; DOI=10.1111/j.1600-0609.2004.00405.x;
Lima P.R.M., Baratti M.O., Chiattone M.L., Costa F.F., Saad S.T.O.;
"Band 3Tambau: a de novo mutation in the AE1 gene associated with
hereditary spherocytosis. Implications for anion exchange and
insertion into the red blood cell membrane.";
Eur. J. Haematol. 74:396-401(2005).
[70]
INVOLVEMENT IN CHC AND SPH4, VARIANT GLU-56, VARIANTS CHC PRO-687;
PRO-731 AND ARG-734, VARIANTS SPH4 TYR-705 AND GLN-760,
CHARACTERIZATION OF VARIANTS CHC PRO-687; PRO-731 AND ARG-734, AND
CHARACTERIZATION OF VARIANTS SPH4 TYR-705 AND GLN-760.
PubMed=16227998; DOI=10.1038/ng1656;
Bruce L.J., Robinson H.C., Guizouarn H., Borgese F., Harrison P.,
King M.-J., Goede J.S., Coles S.E., Gore D.M., Lutz H.U.,
Ficarella R., Layton D.M., Iolascon A., Ellory J.C., Stewart G.W.;
"Monovalent cation leaks in human red cells caused by single amino-
acid substitutions in the transport domain of the band 3 chloride-
bicarbonate exchanger, AE1.";
Nat. Genet. 37:1258-1263(2005).
[71]
CHARACTERIZATION OF VARIANT DRTA-HA ASP-701, CHARACTERIZATION OF
VARIANT AD-DRTA ASP-858, SUBUNIT, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=20151848; DOI=10.3109/09687681003588020;
Ungsupravate D., Sawasdee N., Khositseth S., Udomchaiprasertkul W.,
Khoprasert S., Li J., Reithmeier R.A., Yenchitsomanus P.T.;
"Impaired trafficking and intracellular retention of mutant kidney
anion exchanger 1 proteins (G701D and A858D) associated with distal
renal tubular acidosis.";
Mol. Membr. Biol. 27:92-103(2010).
[72]
VARIANT ILE-862.
PubMed=21849667; DOI=10.1152/ajpcell.00054.2011;
Stewart A.K., Shmukler B.E., Vandorpe D.H., Rivera A., Heneghan J.F.,
Li X., Hsu A., Karpatkin M., O'Neill A.F., Bauer D.E., Heeney M.M.,
John K., Kuypers F.A., Gallagher P.G., Lux S.E., Brugnara C.,
Westhoff C.M., Alper S.L.;
"Loss-of-function and gain-of-function phenotypes of stomatocytosis
mutant RhAG F65S.";
Am. J. Physiol. 301:C1325-C1343(2011).
-!- FUNCTION: Functions both as a transporter that mediates
electroneutral anion exchange across the cell membrane and as a
structural protein. Major integral membrane glycoprotein of the
erythrocyte membrane; required for normal flexibility and
stability of the erythrocyte membrane and for normal erythrocyte
shape via the interactions of its cytoplasmic domain with
cytoskeletal proteins, glycolytic enzymes, and hemoglobin.
Functions as a transporter that mediates the 1:1 exchange of
inorganic anions across the erythrocyte membrane. Mediates
chloride-bicarbonate exchange in the kidney, and is required for
normal acidification of the urine. {ECO:0000269|PubMed:10926824,
ECO:0000269|PubMed:14734552, ECO:0000269|PubMed:1538405,
ECO:0000269|PubMed:20151848, ECO:0000269|PubMed:24121512}.
-!- ENZYME REGULATION: Phenyl isothiocyanate inhibits anion transport
in vitro.
-!- SUBUNIT: A dimer in solution, but in its membrane environment, it
exists primarily as a mixture of dimers and tetramers and spans
the membrane asymmetrically. Interacts (via cytoplasmic N-terminal
domain) with ANK1 (via N-terminal ANK repeats); tetramer formation
is critical for ankyrin association. Interacts with STOM. Isoform
2 interacts with TM139 (PubMed:26049106).
{ECO:0000269|PubMed:11049968, ECO:0000269|PubMed:20151848,
ECO:0000269|PubMed:23219802, ECO:0000269|PubMed:26049106,
ECO:0000269|PubMed:7665627}.
-!- INTERACTION:
P05026:ATP1B1; NbExp=8; IntAct=EBI-7576138, EBI-714630;
O95393:BMP10; NbExp=4; IntAct=EBI-7576138, EBI-3922513;
A5K5E5:PVX_088820 (xeno); NbExp=8; IntAct=EBI-7576138, EBI-11621504;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10926824,
ECO:0000269|PubMed:24121512, ECO:0000269|PubMed:26542571,
ECO:0000269|PubMed:7506871}; Multi-pass membrane protein
{ECO:0000269|PubMed:26542571}. Basolateral cell membrane
{ECO:0000269|PubMed:7506871}; Multi-pass membrane protein
{ECO:0000269|PubMed:7506871}. Note=Detected in the erythrocyte
cell membrane and on the basolateral membrane of alpha-
intercalated cells in the collecting duct in the kidney.
{ECO:0000269|PubMed:7506871}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=eAE1, Erythrocyte;
IsoId=P02730-1; Sequence=Displayed;
Name=2 {ECO:0000269|PubMed:7506871}; Synonyms=kAE1, Kidney;
IsoId=P02730-2; Sequence=VSP_057833;
-!- TISSUE SPECIFICITY: Detected in erythrocytes (at protein level)
(PubMed:7506871, PubMed:26542571). Isoform 2 is expressed in
kidney (at protein level) (PubMed:7506871).
{ECO:0000269|PubMed:10926824, ECO:0000269|PubMed:1538405,
ECO:0000269|PubMed:23219802, ECO:0000269|PubMed:26542571,
ECO:0000269|PubMed:7506871}.
-!- PTM: Phosphorylated on Tyr-8 and Tyr-21 most likely by SYK. PP1-
resistant phosphorylation that precedes Tyr-359 and Tyr-904
phosphorylation. {ECO:0000269|PubMed:10942405,
ECO:0000269|PubMed:1998697}.
-!- PTM: Phosphorylated on Tyr-359 and Tyr-904 most likely by LYN.
PP1-inhibited phosphorylation that follows Tyr-8 and Tyr-21
phosphorylation. {ECO:0000269|PubMed:10942405,
ECO:0000269|PubMed:1998697}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:26542571}.
-!- POLYMORPHISM: SLC4A1 is responsible for the Diego blood group
system. The molecular basis of the Di(a)=Di1/Di(b)/Di2 blood group
antigens is a single variation in position 854; Leu-854
corresponds to Di(a) and Pro-854 to Di(b). The molecular basis of
the Wr(a)=Di3/Wr(b)/Di4 blood group antigens is a single variation
in position 658; Lys-658 corresponds to Wr(a) and Glu-658 to
Wr(b). The blood group antigens Wd(a)=Di5 (Waldner-type) has Met-
557; Rb(a)=Di6 has Leu-548 and WARR=Di7 has Ile-552.
-!- POLYMORPHISM: SLC4A1 is responsible for the Swann blood group
system (SW) [MIM:601550]. Sw(a+) has a Gln or a Trp at position
646 and Sw(a-) has an Arg.
-!- POLYMORPHISM: SLC4A1 is responsible for the Froese blood group
system (FR) [MIM:601551]. FR(a+) has a Lys at position 480 and
FR(a-) has a Glu.
-!- POLYMORPHISM: Genetic variations in SLC4A1 are involved in
resistance to malaria [MIM:611162].
-!- DISEASE: Ovalocytosis, Southeast Asian (SAO) [MIM:166900]: A
hereditary hematologic disorder characterized by ovalocytic
erythrocytes that are rigid and exhibit reduced expression of many
erythrocyte antigens. Clinical manifestations include mild
hemolysis, intermittent jaundice and gallstones. However, the
disorder is most often asymptomatic. {ECO:0000269|PubMed:1538405,
ECO:0000269|PubMed:1722314}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Spherocytosis 4 (SPH4) [MIM:612653]: Spherocytosis is a
hematologic disorder leading to chronic hemolytic anemia and
characterized by numerous abnormally shaped erythrocytes which are
generally spheroidal. {ECO:0000269|PubMed:10580570,
ECO:0000269|PubMed:10745622, ECO:0000269|PubMed:10942416,
ECO:0000269|PubMed:11380459, ECO:0000269|PubMed:1378323,
ECO:0000269|PubMed:15813913, ECO:0000269|PubMed:16227998,
ECO:0000269|PubMed:7530501, ECO:0000269|PubMed:8547122,
ECO:0000269|PubMed:8640229, ECO:0000269|PubMed:8943874,
ECO:0000269|PubMed:9012689, ECO:0000269|PubMed:9207478,
ECO:0000269|PubMed:9233560, ECO:0000269|PubMed:9973643}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Renal tubular acidosis, distal, autosomal dominant (AD-
dRTA) [MIM:179800]: An autosomal dominant disease characterized by
reduced ability to acidify urine, variable hyperchloremic
hypokalemic metabolic acidosis, nephrocalcinosis, and
nephrolithiasis. It is due to functional failure of alpha-
intercalated cells of the cortical collecting duct of the distal
nephron, where vectorial proton transport is required for urinary
acidification. Note=The disease is caused by mutations affecting
the gene represented in this entry.
-!- DISEASE: Renal tubular acidosis, distal, with hemolytic anemia
(dRTA-HA) [MIM:611590]: A disease characterized by the association
of hemolytic anemia with distal renal tubular acidosis, the
reduced ability to acidify urine resulting in variable
hyperchloremic hypokalemic metabolic acidosis, nephrocalcinosis,
and nephrolithiasis. {ECO:0000269|PubMed:10926824,
ECO:0000269|PubMed:15211439, ECO:0000269|PubMed:9854053}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Renal tubular acidosis, distal, with normal red cell
morphology (dRTA-NRC) [MIM:611590]: A disease characterized by
reduced ability to acidify urine, variable hyperchloremic
hypokalemic metabolic acidosis, nephrocalcinosis, and
nephrolithiasis. It is due to functional failure of alpha-
intercalated cells of the cortical collecting duct of the distal
nephron, where vectorial proton transport is required for urinary
acidification. {ECO:0000269|PubMed:15211439}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- DISEASE: Cryohydrocytosis (CHC) [MIM:185020]: An autosomal
dominant disorder of red cell membrane permeability characterized
by cold-induced changes in cell volume, resulting in cold-
sensitive stomatocytosis, and increased erythrocyte osmotic
fragility and autohemolysis at 4 degrees Celsius. Patients present
with mild to moderate hemolytic anemia, splenomegaly, fatigue, and
pseudohyperkalemia due to a potassium leak from the erythrocytes.
{ECO:0000269|PubMed:16227998}. Note=The disease is caused by
mutations affecting distinct genetic loci, including the gene
represented in this entry.
-!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Band 3 entry;
URL="https://en.wikipedia.org/wiki/Band_3";
-!- WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene
mutation database;
URL="https://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=diego";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/slc4a1/";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/SLC4A1ID42325ch17q21.html";
-----------------------------------------------------------------------
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EMBL; X12609; CAA31128.1; -; mRNA.
EMBL; M27819; AAA35514.1; -; mRNA.
EMBL; DQ419529; ABD74692.1; -; mRNA.
EMBL; GQ981383; ADN39420.1; -; mRNA.
EMBL; GQ981384; ADN39421.1; -; mRNA.
EMBL; DQ072115; AAY57324.1; -; Genomic_DNA.
EMBL; CH471178; EAW51614.1; -; Genomic_DNA.
EMBL; BC096106; AAH96106.1; -; mRNA.
EMBL; BC096107; AAH96107.1; -; mRNA.
EMBL; BC099628; AAH99628.1; -; mRNA.
EMBL; BC099629; AAH99629.1; -; mRNA.
EMBL; BC101570; AAI01571.1; -; mRNA.
EMBL; BC101574; AAI01575.1; -; mRNA.
EMBL; S68680; AAC60608.2; -; mRNA.
CCDS; CCDS11481.1; -. [P02730-1]
PIR; A36218; B3HU.
RefSeq; NP_000333.1; NM_000342.3. [P02730-1]
RefSeq; XP_005257650.1; XM_005257593.4. [P02730-2]
UniGene; Hs.210751; -.
UniGene; Hs.443948; -.
PDB; 1BH7; NMR; -; A=803-835.
PDB; 1BNX; NMR; -; A=389-430.
PDB; 1BTQ; NMR; -; A=405-424.
PDB; 1BTR; NMR; -; A=405-424.
PDB; 1BTS; NMR; -; A=436-456.
PDB; 1BTT; NMR; -; A=436-456.
PDB; 1BZK; NMR; -; A=389-430.
PDB; 1HYN; X-ray; 2.60 A; P/Q/R/S=1-379.
PDB; 2BTA; NMR; -; A=1-15.
PDB; 2BTB; NMR; -; A=1-15.
PDB; 3BTB; NMR; -; A=1-15.
PDB; 4KY9; X-ray; 2.23 A; A/P=51-356.
PDB; 4YZF; X-ray; 3.50 A; A/B/C/D=1-911.
PDBsum; 1BH7; -.
PDBsum; 1BNX; -.
PDBsum; 1BTQ; -.
PDBsum; 1BTR; -.
PDBsum; 1BTS; -.
PDBsum; 1BTT; -.
PDBsum; 1BZK; -.
PDBsum; 1HYN; -.
PDBsum; 2BTA; -.
PDBsum; 2BTB; -.
PDBsum; 3BTB; -.
PDBsum; 4KY9; -.
PDBsum; 4YZF; -.
ProteinModelPortal; P02730; -.
SMR; P02730; -.
BioGrid; 112412; 12.
DIP; DIP-42428N; -.
ELM; P02730; -.
IntAct; P02730; 9.
MINT; MINT-1344291; -.
STRING; 9606.ENSP00000262418; -.
MoonProt; P02730; -.
TCDB; 2.A.31.1.1; the anion exchanger (ae) family.
iPTMnet; P02730; -.
PhosphoSitePlus; P02730; -.
SwissPalm; P02730; -.
BioMuta; SLC4A1; -.
DMDM; 114787; -.
EPD; P02730; -.
PaxDb; P02730; -.
PeptideAtlas; P02730; -.
PRIDE; P02730; -.
Ensembl; ENST00000262418; ENSP00000262418; ENSG00000004939. [P02730-1]
GeneID; 6521; -.
KEGG; hsa:6521; -.
UCSC; uc002igf.5; human. [P02730-1]
CTD; 6521; -.
DisGeNET; 6521; -.
GeneCards; SLC4A1; -.
HGNC; HGNC:11027; SLC4A1.
HPA; CAB034438; -.
HPA; HPA015584; -.
HPA; HPA063911; -.
MalaCards; SLC4A1; -.
MIM; 109270; gene+phenotype.
MIM; 110500; phenotype.
MIM; 112010; phenotype.
MIM; 112050; phenotype.
MIM; 130600; phenotype.
MIM; 166900; phenotype.
MIM; 179800; phenotype.
MIM; 185020; phenotype.
MIM; 601550; phenotype.
MIM; 601551; phenotype.
MIM; 611162; phenotype.
MIM; 611590; phenotype.
MIM; 612653; phenotype.
neXtProt; NX_P02730; -.
OpenTargets; ENSG00000004939; -.
Orphanet; 93608; Autosomal dominant distal renal tubular acidosis.
Orphanet; 93610; Distal renal tubular acidosis with anemia.
Orphanet; 398088; Hereditary cryohydrocytosis with normal stomatin.
Orphanet; 822; Hereditary spherocytosis.
Orphanet; 98868; Southeast Asian ovalocytosis.
PharmGKB; PA35895; -.
eggNOG; KOG1172; Eukaryota.
eggNOG; ENOG410XPHD; LUCA.
GeneTree; ENSGT00760000119021; -.
HOVERGEN; HBG004326; -.
InParanoid; P02730; -.
KO; K06573; -.
OMA; WSLLELQ; -.
OrthoDB; EOG091G01FT; -.
PhylomeDB; P02730; -.
TreeFam; TF313630; -.
Reactome; R-HSA-1237044; Erythrocytes take up carbon dioxide and release oxygen.
Reactome; R-HSA-1247673; Erythrocytes take up oxygen and release carbon dioxide.
Reactome; R-HSA-425381; Bicarbonate transporters.
SIGNOR; P02730; -.
ChiTaRS; SLC4A1; human.
EvolutionaryTrace; P02730; -.
GeneWiki; Band_3; -.
GenomeRNAi; 6521; -.
PMAP-CutDB; P02730; -.
PRO; PR:P02730; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000004939; -.
ExpressionAtlas; P02730; baseline and differential.
Genevisible; P02730; HS.
GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
GO; GO:0030863; C:cortical cytoskeleton; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0030018; C:Z disc; ISS:UniProtKB.
GO; GO:0008509; F:anion transmembrane transporter activity; TAS:ProtInc.
GO; GO:0015301; F:anion:anion antiporter activity; IDA:UniProtKB.
GO; GO:0030506; F:ankyrin binding; IPI:BHF-UCL.
GO; GO:0015106; F:bicarbonate transmembrane transporter activity; IDA:UniProtKB.
GO; GO:0015108; F:chloride transmembrane transporter activity; ISS:UniProtKB.
GO; GO:0005452; F:inorganic anion exchanger activity; IDA:UniProtKB.
GO; GO:0043495; F:protein anchor; TAS:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
GO; GO:0008510; F:sodium:bicarbonate symporter activity; IBA:GO_Central.
GO; GO:0006820; P:anion transport; IDA:UniProtKB.
GO; GO:0015701; P:bicarbonate transport; IDA:UniProtKB.
GO; GO:0006873; P:cellular ion homeostasis; TAS:ProtInc.
GO; GO:0006821; P:chloride transport; ISS:UniProtKB.
GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
Gene3D; 3.40.930.10; -; 1.
InterPro; IPR001717; Anion_exchange.
InterPro; IPR002977; Anion_exchange_1.
InterPro; IPR018241; Anion_exchange_CS.
InterPro; IPR013769; Band3_cytoplasmic_dom.
InterPro; IPR011531; HCO3_transpt_C.
InterPro; IPR003020; HCO3_transpt_euk.
InterPro; IPR016152; PTrfase/Anion_transptr.
PANTHER; PTHR11453; PTHR11453; 1.
Pfam; PF07565; Band_3_cyto; 1.
Pfam; PF00955; HCO3_cotransp; 2.
PRINTS; PR00165; ANIONEXCHNGR.
PRINTS; PR01187; ANIONEXHNGR1.
PRINTS; PR01231; HCO3TRNSPORT.
SUPFAM; SSF55804; SSF55804; 1.
TIGRFAMs; TIGR00834; ae; 1.
PROSITE; PS00219; ANION_EXCHANGER_1; 1.
PROSITE; PS00220; ANION_EXCHANGER_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Anion exchange;
Blood group antigen; Cell membrane; Complete proteome;
Direct protein sequencing; Disease mutation; Elliptocytosis;
Glycoprotein; Hereditary hemolytic anemia; Ion transport; Lipoprotein;
Membrane; Palmitate; Phosphoprotein; Polymorphism; Reference proteome;
Transmembrane; Transmembrane helix; Transport.
CHAIN 1 911 Band 3 anion transport protein.
/FTId=PRO_0000079209.
TOPO_DOM 1 403 Cytoplasmic.
{ECO:0000269|PubMed:26542571}.
TRANSMEM 404 427 Helical; Name=1.
{ECO:0000269|PubMed:26542571}.
TOPO_DOM 428 435 Extracellular.
{ECO:0000269|PubMed:26542571}.
TRANSMEM 436 456 Helical; Name=2.
{ECO:0000269|PubMed:26542571}.
TOPO_DOM 457 459 Cytoplasmic.
{ECO:0000269|PubMed:26542571}.
TRANSMEM 460 476 Discontinuously helical; Name=3.
{ECO:0000269|PubMed:26542571}.
TOPO_DOM 477 485 Extracellular.
{ECO:0000269|PubMed:26542571}.
TRANSMEM 486 506 Helical; Name=4.
{ECO:0000269|PubMed:26542571}.
TOPO_DOM 507 518 Cytoplasmic.
{ECO:0000269|PubMed:26542571}.
TRANSMEM 519 541 Helical; Name=5.
{ECO:0000269|PubMed:26542571}.
TOPO_DOM 542 570 Extracellular.
{ECO:0000269|PubMed:26542571}.
TRANSMEM 571 591 Helical; Name=6.
{ECO:0000269|PubMed:26542571}.
TOPO_DOM 592 602 Cytoplasmic.
{ECO:0000269|PubMed:26542571}.
TRANSMEM 603 623 Helical; Name=7.
{ECO:0000269|PubMed:26542571}.
TOPO_DOM 624 663 Extracellular.
{ECO:0000269|PubMed:26542571}.
TRANSMEM 664 684 Helical; Name=8.
{ECO:0000269|PubMed:26542571}.
TOPO_DOM 685 700 Cytoplasmic.
{ECO:0000269|PubMed:26542571}.
TRANSMEM 701 719 Helical; Name=9.
{ECO:0000269|PubMed:26542571}.
TRANSMEM 720 737 Discontinuously helical; Name=10.
{ECO:0000269|PubMed:26542571}.
TOPO_DOM 738 760 Cytoplasmic.
{ECO:0000269|PubMed:26542571}.
TRANSMEM 761 781 Helical; Name=11.
{ECO:0000269|PubMed:26542571}.
TRANSMEM 782 800 Helical; Name=12.
{ECO:0000269|PubMed:26542571}.
TOPO_DOM 801 838 Cytoplasmic.
{ECO:0000269|PubMed:26542571}.
INTRAMEM 839 869 Discontinuously helical.
{ECO:0000269|PubMed:26542571}.
TOPO_DOM 870 911 Cytoplasmic.
{ECO:0000269|PubMed:26542571}.
REGION 55 290 Globular.
REGION 176 185 Interaction with ANK1. {ECO:0000305}.
REGION 304 357 Dimerization arm.
REGION 559 630 Involved in anion transport.
SITE 590 590 Important for anion transport.
SITE 681 681 Important for anion-proton cotransport.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000269|PubMed:2790053,
ECO:0000269|PubMed:701248}.
MOD_RES 8 8 Phosphotyrosine.
{ECO:0000269|PubMed:10942405,
ECO:0000269|PubMed:1998697}.
MOD_RES 21 21 Phosphotyrosine.
{ECO:0000269|PubMed:10942405,
ECO:0000269|PubMed:1998697}.
MOD_RES 46 46 Phosphotyrosine.
{ECO:0000269|PubMed:1998697}.
MOD_RES 185 185 Phosphoserine.
{ECO:0000250|UniProtKB:P23562}.
MOD_RES 350 350 Phosphoserine.
{ECO:0000250|UniProtKB:P04919}.
MOD_RES 359 359 Phosphotyrosine.
{ECO:0000269|PubMed:10942405}.
MOD_RES 904 904 Phosphotyrosine.
{ECO:0000269|PubMed:10942405}.
LIPID 843 843 S-palmitoyl cysteine.
{ECO:0000269|PubMed:1885574}.
CARBOHYD 642 642 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:10861210,
ECO:0000269|PubMed:24121512}.
VAR_SEQ 1 65 Missing (in isoform 2).
{ECO:0000269|PubMed:7506871}.
/FTId=VSP_057833.
VARIANT 27 27 P -> H. {ECO:0000269|PubMed:15489334}.
/FTId=VAR_058035.
VARIANT 38 38 D -> A (in dbSNP:rs5035).
{ECO:0000269|PubMed:10745622,
ECO:0000269|PubMed:16252102,
ECO:0000269|PubMed:9012689,
ECO:0000269|Ref.5}.
/FTId=VAR_014612.
VARIANT 40 40 E -> K (found in patients with hemolytic
anemia; unknown pathological
significance; Montefiore;
dbSNP:rs45562031).
{ECO:0000269|PubMed:8471774,
ECO:0000269|PubMed:8640229}.
/FTId=VAR_000798.
VARIANT 45 45 D -> E (in dbSNP:rs34700496).
/FTId=VAR_036693.
VARIANT 56 56 K -> E (in Di(a)/Memphis-II antigen;
dbSNP:rs5036).
{ECO:0000269|PubMed:10745622,
ECO:0000269|PubMed:16227998,
ECO:0000269|PubMed:1678289,
ECO:0000269|PubMed:1722314,
ECO:0000269|PubMed:8206915,
ECO:0000269|Ref.5}.
/FTId=VAR_000799.
VARIANT 68 68 E -> K (in dbSNP:rs13306787).
/FTId=VAR_039290.
VARIANT 72 72 E -> D (in dbSNP:rs13306788).
{ECO:0000269|PubMed:10745622}.
/FTId=VAR_058036.
VARIANT 73 73 L -> M (in dbSNP:rs781490287).
{ECO:0000269|PubMed:9012689}.
/FTId=VAR_039291.
VARIANT 90 90 E -> K (in SPH4; Cape Town;
dbSNP:rs28929480).
{ECO:0000269|PubMed:11380459}.
/FTId=VAR_013784.
VARIANT 112 112 R -> S (in dbSNP:rs5037).
/FTId=VAR_014613.
VARIANT 130 130 G -> R (in SPH4; Fukoka;
dbSNP:rs121912749).
{ECO:0000269|PubMed:10745622}.
/FTId=VAR_013785.
VARIANT 147 147 P -> S (in SPH4; Mondego).
{ECO:0000269|PubMed:9207478}.
/FTId=VAR_013786.
VARIANT 285 285 A -> D (in SPH4; Boston).
{ECO:0000269|PubMed:8943874}.
/FTId=VAR_013787.
VARIANT 327 327 P -> R (in SPH4; Tuscaloosa;
dbSNP:rs28931583).
{ECO:0000269|PubMed:1378323}.
/FTId=VAR_000800.
VARIANT 400 408 Missing (in SAO; increased rigidity of
the erythrocyte membrane leading to
increased resistance to shear stress and
increased resistance to P.falciparum).
{ECO:0000269|PubMed:1538405,
ECO:0000269|PubMed:1722314}.
/FTId=VAR_000801.
VARIANT 429 429 E -> D (in NFLD+ antigen).
{ECO:0000269|PubMed:10738034}.
/FTId=VAR_058037.
VARIANT 432 432 R -> W (in ELO antigen;
dbSNP:rs373768879).
/FTId=VAR_013788.
VARIANT 442 442 I -> F (in dbSNP:rs5018).
/FTId=VAR_014614.
VARIANT 455 455 G -> E (in SPH4; Benesov).
{ECO:0000269|PubMed:8943874}.
/FTId=VAR_013789.
VARIANT 455 455 G -> R (in SPH4; Yamagata).
{ECO:0000269|PubMed:10745622}.
/FTId=VAR_058038.
VARIANT 480 480 E -> K (in FR(a+) antigen;
dbSNP:rs121912756).
{ECO:0000269|PubMed:11061863}.
/FTId=VAR_013790.
VARIANT 488 488 V -> M (in SPH4; Coimbra; also in AR-
dRTA; dbSNP:rs28931584).
{ECO:0000269|PubMed:10942416,
ECO:0000269|PubMed:9207478}.
/FTId=VAR_013791.
VARIANT 490 490 R -> C (in SPH4; Bicetre I).
{ECO:0000269|PubMed:9233560}.
/FTId=VAR_013792.
VARIANT 490 490 R -> H (in SPH4; Pinhal).
{ECO:0000269|PubMed:10580570}.
/FTId=VAR_058039.
VARIANT 508 508 E -> K (in dbSNP:rs45568837).
{ECO:0000269|Ref.5}.
/FTId=VAR_025090.
VARIANT 518 518 R -> C (in SPH4; Dresden;
dbSNP:rs868742796).
{ECO:0000269|PubMed:8640229}.
/FTId=VAR_000802.
VARIANT 548 548 P -> L (in RB(A) antigen;
dbSNP:rs879202054).
/FTId=VAR_000803.
VARIANT 551 551 K -> N (in TR(A) antigen).
/FTId=VAR_013793.
VARIANT 552 552 T -> I (in WARR antigen).
/FTId=VAR_000804.
VARIANT 555 555 Y -> H (in VG(a) antigen).
/FTId=VAR_013794.
VARIANT 557 557 V -> M (in WD(a) antigen;
dbSNP:rs121912743).
/FTId=VAR_000805.
VARIANT 561 561 P -> A (in NFLD+ antigen).
{ECO:0000269|PubMed:10738034}.
/FTId=VAR_058040.
VARIANT 561 561 P -> S (in BOW antigen).
{ECO:0000269|PubMed:10738034}.
/FTId=VAR_013795.
VARIANT 565 565 G -> A (in WU antigen;
dbSNP:rs551784583).
/FTId=VAR_013796.
VARIANT 566 566 P -> A (in KREP antigen).
/FTId=VAR_013797.
VARIANT 566 566 P -> S (in PN(a) antigen).
/FTId=VAR_013798.
VARIANT 569 569 N -> K (in BP(a) antigen).
/FTId=VAR_013799.
VARIANT 586 586 M -> L (in dbSNP:rs5019).
/FTId=VAR_014615.
VARIANT 589 589 R -> C (in AD-dRTA; reduced red cell
sulfate transport and altered
glycosylation of the red cell band 3 N-
glycan chain; dbSNP:rs121912745).
{ECO:0000269|PubMed:9312167}.
/FTId=VAR_015104.
VARIANT 589 589 R -> H (in AD-dRTA; dbSNP:rs121912744).
{ECO:0000269|PubMed:9312167,
ECO:0000269|PubMed:9600966}.
/FTId=VAR_015105.
VARIANT 589 589 R -> S (in AD-dRTA; dbSNP:rs121912745).
{ECO:0000269|PubMed:9600966}.
/FTId=VAR_015106.
VARIANT 602 602 R -> P (in dRTA-HA; dbSNP:rs121912754).
{ECO:0000269|PubMed:15211439}.
/FTId=VAR_039292.
VARIANT 609 609 G -> R (in AD-dRTA; detected subapically
and at the apical membrane as well as at
the basolateral membrane in contrast to
the normal basolateral appearance of
wild-type protein; dbSNP:rs878853002).
{ECO:0000269|PubMed:14734552}.
/FTId=VAR_058041.
VARIANT 613 613 S -> F (in AD-dRTA; markedly increased
red cell sulfate transport but almost
normal red cell iodide transport;
dbSNP:rs121912746).
{ECO:0000269|PubMed:9312167}.
/FTId=VAR_015107.
VARIANT 646 646 R -> Q (in SW(a+) antigen;
dbSNP:rs121912757).
{ECO:0000269|PubMed:11155072}.
/FTId=VAR_013800.
VARIANT 646 646 R -> W (in SW(a+) antigen;
dbSNP:rs121912758).
{ECO:0000269|PubMed:11155072}.
/FTId=VAR_013801.
VARIANT 656 656 R -> C (in HG(a) antigen;
dbSNP:rs372514760).
/FTId=VAR_013802.
VARIANT 656 656 R -> H (in MO(a) antigen;
dbSNP:rs758868427).
/FTId=VAR_013803.
VARIANT 658 658 E -> K (in WR(a) antigen;
dbSNP:rs75731670).
{ECO:0000269|PubMed:7812009}.
/FTId=VAR_000806.
VARIANT 663 663 M -> K (in SPH4; Tambau).
{ECO:0000269|PubMed:15813913}.
/FTId=VAR_058042.
VARIANT 663 663 Missing (in SPH4; Osnabruck II).
{ECO:0000269|PubMed:8640229}.
/FTId=VAR_000807.
VARIANT 687 687 L -> P (in CHC; Blackburn; induces
abnormal cations sodium and potassium
fluxes; decreases anion chloride
transport; dbSNP:rs863225463).
{ECO:0000269|PubMed:16227998}.
/FTId=VAR_039293.
VARIANT 688 688 I -> V (in dbSNP:rs5022).
/FTId=VAR_014616.
VARIANT 690 690 S -> G (in dbSNP:rs5023).
/FTId=VAR_014617.
VARIANT 701 701 G -> D (in dRTA-HA; impairs expression at
the cell membrane; dbSNP:rs121912748).
{ECO:0000269|PubMed:10926824,
ECO:0000269|PubMed:20151848,
ECO:0000269|PubMed:9854053}.
/FTId=VAR_015171.
VARIANT 705 705 D -> Y (in SPH4; Horam; induces abnormal
cations sodium and potassium fluxes;
decreases anion chloride transport).
{ECO:0000269|PubMed:16227998}.
/FTId=VAR_039294.
VARIANT 707 707 L -> P (in SPH4; Most).
{ECO:0000269|PubMed:11208088,
ECO:0000269|PubMed:8943874}.
/FTId=VAR_013804.
VARIANT 714 714 G -> R (in SPH4; Okinawa).
{ECO:0000269|PubMed:10745622}.
/FTId=VAR_013805.
VARIANT 731 731 S -> P (in CHC; Hemel; induces abnormal
cations sodium and potassium fluxes;
decreases anion chloride transport;
dbSNP:rs863225461).
{ECO:0000269|PubMed:16227998}.
/FTId=VAR_039295.
VARIANT 734 734 H -> R (in CHC; Hurstpierpont; induces
abnormal cations sodium and potassium
fluxes; decreases anion chloride
transport; dbSNP:rs863225462).
{ECO:0000269|PubMed:16227998}.
/FTId=VAR_039296.
VARIANT 760 760 R -> Q (in SPH4; Prague II; induces
abnormal cations sodium and potassium
fluxes; decreases anion chloride
transport; dbSNP:rs121912755).
{ECO:0000269|PubMed:10745622,
ECO:0000269|PubMed:11208088,
ECO:0000269|PubMed:16227998,
ECO:0000269|PubMed:7530501}.
/FTId=VAR_013806.
VARIANT 760 760 R -> W (in SPH4; Hradec Kralove;
dbSNP:rs373916826).
{ECO:0000269|PubMed:10745622,
ECO:0000269|PubMed:11208088,
ECO:0000269|PubMed:7530501}.
/FTId=VAR_013807.
VARIANT 771 771 G -> D (in SPH4; Chur;
dbSNP:rs121912741).
{ECO:0000269|PubMed:8547122}.
/FTId=VAR_013808.
VARIANT 773 773 S -> P (in dRTA-NRC; dbSNP:rs121912753).
{ECO:0000269|PubMed:15211439}.
/FTId=VAR_039297.
VARIANT 783 783 I -> N (in SPH4; Napoli II).
{ECO:0000269|PubMed:9012689}.
/FTId=VAR_013809.
VARIANT 808 808 R -> C (in SPH4; Jablonec).
{ECO:0000269|PubMed:11208088,
ECO:0000269|PubMed:7530501}.
/FTId=VAR_013810.
VARIANT 808 808 R -> H (in SPH4; Nara;
dbSNP:rs866727908).
{ECO:0000269|PubMed:10745622}.
/FTId=VAR_013811.
VARIANT 832 832 R -> H (in dbSNP:rs5025).
/FTId=VAR_014618.
VARIANT 834 834 H -> P (in SPH4; Birmingham).
{ECO:0000269|PubMed:11208088,
ECO:0000269|PubMed:8943874}.
/FTId=VAR_013812.
VARIANT 837 837 T -> A (in SPH4; Tokyo;
dbSNP:rs121912750).
{ECO:0000269|PubMed:9973643}.
/FTId=VAR_013813.
VARIANT 837 837 T -> M (in SPH4; Philadelphia).
{ECO:0000269|PubMed:10745622,
ECO:0000269|PubMed:11208088,
ECO:0000269|PubMed:8943874,
ECO:0000269|PubMed:9233560}.
/FTId=VAR_013814.
VARIANT 837 837 T -> R (in SPH4; Nagoya).
{ECO:0000269|PubMed:10745622}.
/FTId=VAR_058043.
VARIANT 850 850 Missing (in dRTA-HA).
{ECO:0000269|PubMed:10926824}.
/FTId=VAR_015109.
VARIANT 854 854 P -> L (in Di(a)/Memphis-II antigen;
dbSNP:rs2285644).
{ECO:0000269|PubMed:10745622,
ECO:0000269|PubMed:8206915}.
/FTId=VAR_000808.
VARIANT 858 858 A -> D (in AD-dRTA; impairs expression at
the cell membrane; dbSNP:rs121912751).
{ECO:0000269|PubMed:10926824,
ECO:0000269|PubMed:20151848}.
/FTId=VAR_015108.
VARIANT 862 862 V -> I (polymorphism; dbSNP:rs5026).
{ECO:0000269|PubMed:21849667,
ECO:0000269|Ref.5}.
/FTId=VAR_014619.
VARIANT 868 868 P -> L (in acanthocytosis; slightly
increases transporter activity; impairs
expression at the cell membrane;
dbSNP:rs121912759).
{ECO:0000269|PubMed:24121512,
ECO:0000269|PubMed:8343110}.
/FTId=VAR_013815.
VARIANT 870 870 R -> W (in SPH4; Prague III;
dbSNP:rs28931585).
{ECO:0000269|PubMed:11208088,
ECO:0000269|PubMed:11380459,
ECO:0000269|PubMed:7530501}.
/FTId=VAR_013816.
MUTAGEN 85 85 E->A,R: Impairs expression at the cell
membrane. {ECO:0000269|PubMed:24121512}.
MUTAGEN 283 283 R->A,E,S: Impairs expression at the cell
membrane. {ECO:0000269|PubMed:24121512}.
MUTAGEN 642 642 N->D: Loss of N-glycosylation site.
{ECO:0000269|PubMed:24121512}.
MUTAGEN 681 681 E->Q: Impairs expression at the cell
membrane. {ECO:0000269|PubMed:24121512}.
CONFLICT 11 11 M -> D (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 68 68 E -> EE (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 759 759 Q -> H (in Ref. 3; ABD74692).
{ECO:0000305}.
STRAND 9 12 {ECO:0000244|PDB:2BTA}.
STRAND 58 66 {ECO:0000244|PDB:4KY9}.
STRAND 68 70 {ECO:0000244|PDB:4KY9}.
STRAND 73 88 {ECO:0000244|PDB:4KY9}.
STRAND 90 92 {ECO:0000244|PDB:4KY9}.
HELIX 104 115 {ECO:0000244|PDB:4KY9}.
STRAND 118 123 {ECO:0000244|PDB:4KY9}.
HELIX 128 141 {ECO:0000244|PDB:4KY9}.
HELIX 147 149 {ECO:0000244|PDB:4KY9}.
HELIX 150 157 {ECO:0000244|PDB:4KY9}.
HELIX 164 169 {ECO:0000244|PDB:4KY9}.
STRAND 173 175 {ECO:0000244|PDB:1HYN}.
STRAND 188 190 {ECO:0000244|PDB:4KY9}.
HELIX 195 200 {ECO:0000244|PDB:4KY9}.
HELIX 212 219 {ECO:0000244|PDB:1HYN}.
STRAND 226 234 {ECO:0000244|PDB:4KY9}.
STRAND 241 251 {ECO:0000244|PDB:4KY9}.
STRAND 256 258 {ECO:0000244|PDB:1HYN}.
STRAND 262 270 {ECO:0000244|PDB:4KY9}.
HELIX 278 290 {ECO:0000244|PDB:4KY9}.
HELIX 292 300 {ECO:0000244|PDB:4KY9}.
HELIX 304 316 {ECO:0000244|PDB:4KY9}.
STRAND 319 321 {ECO:0000244|PDB:4KY9}.
HELIX 329 332 {ECO:0000244|PDB:4KY9}.
HELIX 333 335 {ECO:0000244|PDB:4KY9}.
HELIX 336 347 {ECO:0000244|PDB:4KY9}.
STRAND 349 351 {ECO:0000244|PDB:1HYN}.
HELIX 383 393 {ECO:0000244|PDB:4YZF}.
TURN 394 400 {ECO:0000244|PDB:4YZF}.
HELIX 403 430 {ECO:0000244|PDB:4YZF}.
TURN 431 433 {ECO:0000244|PDB:4YZF}.
HELIX 437 454 {ECO:0000244|PDB:4YZF}.
HELIX 466 481 {ECO:0000244|PDB:4YZF}.
HELIX 486 506 {ECO:0000244|PDB:4YZF}.
HELIX 509 515 {ECO:0000244|PDB:4YZF}.
HELIX 518 546 {ECO:0000244|PDB:4YZF}.
HELIX 570 593 {ECO:0000244|PDB:4YZF}.
STRAND 594 597 {ECO:0000244|PDB:4YZF}.
HELIX 599 607 {ECO:0000244|PDB:4YZF}.
HELIX 609 623 {ECO:0000244|PDB:4YZF}.
STRAND 655 657 {ECO:0000244|PDB:4YZF}.
HELIX 663 666 {ECO:0000244|PDB:4YZF}.
HELIX 668 689 {ECO:0000244|PDB:4YZF}.
HELIX 703 718 {ECO:0000244|PDB:4YZF}.
HELIX 728 735 {ECO:0000244|PDB:4YZF}.
HELIX 761 780 {ECO:0000244|PDB:4YZF}.
HELIX 785 799 {ECO:0000244|PDB:4YZF}.
HELIX 804 813 {ECO:0000244|PDB:4YZF}.
HELIX 823 827 {ECO:0000244|PDB:4YZF}.
TURN 828 831 {ECO:0000244|PDB:4YZF}.
HELIX 832 850 {ECO:0000244|PDB:4YZF}.
HELIX 854 858 {ECO:0000244|PDB:4YZF}.
HELIX 859 873 {ECO:0000244|PDB:4YZF}.
TURN 875 877 {ECO:0000244|PDB:4YZF}.
TURN 880 882 {ECO:0000244|PDB:4YZF}.
HELIX 883 886 {ECO:0000244|PDB:4YZF}.
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


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CSB-EL021667RA Rat solute carrier family 4, anion exchanger, member 2 (erythrocyte membrane protein band 3-like 1) (SLC4A2) ELISA kit, Species Rat, Sample Type serum, plasma 96T
EIAAB36841 Anion exchange transporter,Bos taurus,Bovine,SLC26A8,Solute carrier family 26 member 8,Testis anion transporter 1
EIAAB36842 Anion exchange transporter,Mouse,Mus musculus,Slc26a8,Solute carrier family 26 member 8,Tat1,Testis anion transporter 1
EIAAB36843 Anion exchange transporter,Homo sapiens,Human,SLC26A8,Solute carrier family 26 member 8,TAT1,Testis anion transporter 1
SLC4A1 SLC4A1 Gene solute carrier family 4, anion exchanger, member 1 (erythrocyte membrane protein band 3, Diego blood group)
CSB-EL021663RA Rat solute carrier family 4, anion exchanger, member 1 (erythrocyte membrane protein band 3, Diego blood group) (SLC4A1) ELISA kit, Species Rat, Sample Type serum, plasma 96T
EIAAB39171 Homo sapiens,Human,OATP5A1,OATPRP4,OATP-RP4,Organic anion transporter polypeptide-related protein 4,SLC21A15,SLCO5A1,Solute carrier family 21 member 15,Solute carrier organic anion transporter family
CSB-EL021667GU Guinea pig solute carrier family 4, anion exchanger, member 2 (erythrocyte membrane protein band 3-like 1) (SLC4A2) ELISA kit, Species Guinea pig, Sample Type serum, plasma 96T
CSB-EL021667MO Mouse solute carrier family 4, anion exchanger, member 2 (erythrocyte membrane protein band 3-like 1) (SLC4A2) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL021667HO Horse solute carrier family 4, anion exchanger, member 2 (erythrocyte membrane protein band 3-like 1) (SLC4A2) ELISA kit, Species Horse, Sample Type serum, plasma 96T
CSB-EL021667HU Human solute carrier family 4, anion exchanger, member 2 (erythrocyte membrane protein band 3-like 1) (SLC4A2) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL021667RB Rabbit solute carrier family 4, anion exchanger, member 2 (erythrocyte membrane protein band 3-like 1) (SLC4A2) ELISA kit, Species Rabbit, Sample Type serum, plasma 96T
EIAAB36715 Kidney-specific transport protein,mNKT,Mouse,mROAT1,Mus musculus,Nkt,Novel kidney transcript,Oat1,Organic anion transporter 1,Renal organic anion transporter 1,Slc22a6,Solute carrier family 22 member
EIAAB39139 Mouse,Mus musculus,OATP-1,Oatp1a1,Slc21a1,Slco1a1,Sodium-independent organic anion-transporting polypeptide 1,Solute carrier family 21 member 1,Solute carrier organic anion transporter family member 1
EIAAB39146 Kidney-specific organic anion-transporting polypeptide 5,Mouse,Mus musculus,Oatp5,OATP-5,Slc21a13,Slco1a6,Solute carrier family 21 member 13,Solute carrier organic anion transporter family member 1A6
EIAAB39147 Kidney-specific organic anion-transporting polypeptide 5,Oatp5,OATP-5,Rat,Rattus norvegicus,Slc21a13,Slco1a6,Solute carrier family 21 member 13,Solute carrier organic anion transporter family member 1
EIAAB39143 Mouse,Mus musculus,Oatp1a4,Oatp2,Slc21a5,Slco1a4,Sodium-independent organic anion-transporting polypeptide 2,Solute carrier family 21 member 5,Solute carrier organic anion transporter family member 1A
CSB-EL021663HU Human solute carrier family 4, anion exchanger, member 1 (erythrocyte membrane protein band 3, Diego blood group) (SLC4A1) ELISA kit, Species Human, Sample Type serum, plasma 96T


 

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