| |
|---|---|
| Accession Number: | P02730 |
| Protein Name: | B3AT aka SLC4A1 aka AE1 aka EPB3 aka DI |
| Length: | 911 |
| Molecular Weight: | 101792.00 |
| Species: | Homo sapiens (Human) [9606] |
| Number of TMSs: | 14 |
| Location1 / Topology2 / Orientation3: | Membrane1 / Multi-pass membrane protein2 |
| Substrate | anion, inorganic anion, chloride, sodium(1+), potassium(1+), organic anion, hydrogencarbonate, phospholipid |
Cross database links:
| RefSeq: | NP_000333.1 |
|---|---|
| Entrez Gene ID: | 6521 |
| Pfam: | PF07565 PF00955 |
| OMIM: |
109270 gene+phenotype 110500 phenotype 112010 phenotype 112050 phenotype 130600 phenotype 179800 phenotype 601550 phenotype 601551 phenotype 611590 phenotype 612653 phenotype |
| KEGG: | hsa:6521 hsa:6521 |
Gene Ontology
GO:0016323
C:basolateral plasma membrane
GO:0030863
C:cortical cytoskeleton
GO:0005887
C:integral to plasma membrane
GO:0030506
F:ankyrin binding
GO:0005452
F:inorganic anion exchanger activity
GO:0043495
F:protein anchor
GO:0042803
F:protein homodimerization activity
GO:0006820
P:anion transport
GO:0006873
P:cellular ion homeostasis
GO:0030018
C:Z disc
GO:0015301
F:anion:anion antiporter activity
GO:0015108
F:chloride transmembrane transporter activity
GO:0015701
P:bicarbonate transport
| |
References (117)[1] “The complete amino acid sequence of the human erythrocyte membrane anion-transport protein deduced from the cDNA sequence.” Tanner M.J.A.et.al. 3223947 [2] “Cloning and characterization of band 3, the human erythrocyte anion-exchange protein (AE1).” Lux S.E.et.al. 2594752 [3] “Recessive distal renal tubular acidosis in Sarawak caused by AE1 mutations.” Choo K.E.et.al. 16252102 [4] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).” The MGC Project Teamet.al. 15489334 [5] “Primary structure of the cytoplasmic domain of human erythrocyte protein band 3. Comparison with its sequence in the mouse.” Yannoukakos D.et.al. 2790053 [6] “Amino acid sequence of the N alpha-terminal 201 residues of human erythrocyte membrane band 3.” Kaul R.K.et.al. 6345535 [7] “Orientation of the band 3 polypeptide from human erythrocyte membranes. Identification of NH2-terminal sequence and site of carbohydrate attachment.” Drickamer L.K.et.al. 701248 [8] “Anion exchanger 1 in human kidney and oncocytoma differs from erythroid AE1 in its NH2 terminus.” Kollert-Jons A.et.al. 7506871 [9] “The human erythrocyte anion-transport protein. Partial amino acid sequence, conformation and a possible molecular mechanism for anion exchange.” Brock C.J.et.al. 6615451 [10] “Anion-proton cotransport through the human red blood cell band 3 protein. Role of glutamate 681.” Jennings M.L.et.al. 1352774 [11] “Band 3 Chur: a variant associated with band 3-deficient hereditary spherocytosis and substitution in a highly conserved position of transmembrane segment 11.” Maillet P.et.al. 8547122 [12] “Localization of the pyridoxal phosphate binding site at the COOH-terminal region of erythrocyte band 3 protein.” Kawano Y.et.al. 3372523 [13] “Phosphorylation sites in human erythrocyte band 3 protein.” Yannoukakos D.et.al. 1998697 [14] “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.” Okubo K.et.al. 1885574 [15] “Sequential phosphorylation of protein band 3 by Syk and Lyn tyrosine kinases in intact human erythrocytes: identification of primary and secondary phosphorylation sites.” Brunati A.M.et.al. 10942405 [16] “Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.” Rikova K.et.al. 18083107 [17] “Two-dimensional structure of the membrane domain of human band 3, the anion transport protein of the erythrocyte membrane.” Wang D.N.et.al. 8508760 [18] “Three-dimensional map of the dimeric membrane domain of the human erythrocyte anion exchanger, Band 3.” Wang D.N.et.al. 8045253 [19] “The solution structures of the first and second transmembrane-spanning segments of band 3.” Gargaro A.R.et.al. 8168533 [20] “Solution structure of a band 3 peptide inhibitor bound to aldolase: a proposed mechanism for regulating binding by tyrosine phosphorylation.” Schneider M.L.et.al. 8527430 [21] “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.” Eisenmesser E.Z.et.al. 9454576 [22] “Studies on the structure of a transmembrane region and a cytoplasmic loop of the human red cell anion exchanger.” Chambers E.J.et.al. 9765907 [23] “NMR solution structure of a cytoplasmic surface loop of the human red cell anion transporter, band 3.” Askin D.et.al. 9709005 [24] “Human erythrocyte band 3 polymorphism (band 3 Memphis): characterization of the structural modification (Lys 56-->Glu) by protein chemistry methods.” Yannoukakos D.et.al. 1678289 [25] “Deletion in erythrocyte band 3 gene in malaria-resistant Southeast Asian ovalocytosis.” Jarolim P.et.al. 1722314 [26] “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.” Jarolim P.et.al. 1378323 [27] “Basis of unique red cell membrane properties in hereditary ovalocytosis.” Schofield A.E.et.al. 1538405 [28] “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.” Bruce L.J.et.al. 8343110 [29] “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).” Rybicki A.C.et.al. 8471774 [30] “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.” Bruce L.J.et.al. 8206915 [31] “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.” Bruce L.J.et.al. 7812009 [32] “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.” Jarolim P.et.al. 7530501 [33] “Characterization of 13 novel band 3 gene defects in hereditary spherocytosis with band 3 deficiency.” Jarolim P.et.al. 8943874 [34] “Ankyrin-1 mutations are a major cause of dominant and recessive hereditary spherocytosis.” Eber S.W.et.al. 8640229 [35] “Modulation of clinical expression and band 3 deficiency in hereditary spherocytosis.” Alloisio N.et.al. 9207478 [36] “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.” Miraglia del Giudice E.et.al. 9012689 [37] “Heterogenous band 3 deficiency in hereditary spherocytosis related to different band 3 gene defects.” Dhermy D.et.al. 9233560 [38] “Familial distal renal tubular acidosis is associated with mutations in the red cell anion exchanger (Band 3, AE1) gene.” Bruce L.J.et.al. 9312167 [39] “Blood group antigens Rb(a), Tr(a), and Wd(a) are located in the third ectoplasmic loop of erythroid band 3.” Jarolim P.et.al. 9191821 [40] “Band 3 Tokyo: Thr837-->Ala837 substitution in erythrocyte band 3 protein associated with spherocytic hemolysis.” Iwase S.et.al. 9973643 [41] “Characterization of seven low incidence blood group antigens carried by erythrocyte band 3 protein.” Jarolim P.et.al. 9845551 [42] “Novel AE1 mutations in recessive distal renal tubular acidosis: loss-of-function is rescued by glycophorin A.” Tanphaichitr V.S.et.al. 9854053 [43] “Mutations in the chloride-bicarbonate exchanger gene AE1 cause autosomal dominant but not autosomal recessive distal renal tubular acidosis.” Karet F.E.et.al. 9600966 [44] “A Gly565-->Ala substitution in human erythroid band 3 accounts for the Wu blood group polymorphism.” Zelinski T.et.al. 9709782 [45] “Arginine 490 is a hot spot for mutation in the band 3 gene in hereditary spherocytosis.” Lima P.R.M.et.al. 10580570 [46] “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.” Bruce L.J.et.al. 10926824 [47] “Severe hereditary spherocytosis and distal renal tubular acidosis associated with the total absence of band 3.” Ribeiro M.L.et.al. 10942416 [48] “Characteristic features of the genotype and phenotype of hereditary spherocytosis in the Japanese population.” Yawata Y.et.al. 10745622 [49] “Trafficking and folding defects in hereditary spherocytosis mutants of the human red cell anion exchanger.” Quilty J.A.et.al. 11208088 [50] “Amino acid substitutions in human erythroid protein band 3 account for the low-incidence antigens NFLD and BOW.” McManus K.et.al. 10738034 [51] “An amino acid substitution in the putative second extracellular loop of RBC band 3 accounts for the Froese blood group polymorphism.” McManus K.et.al. 11061863 [52] “Distinctive Swann blood group genotypes: molecular investigations.” Zelinski T.et.al. 11155072 [53] “Band 3 Cape Town (E90K) causes severe hereditary spherocytosis in combination with band 3 Prague III.” Bracher N.A.et.al. 11380459 [54] “Novel compound heterozygous SLC4A1 mutations in Thai patients with autosomal recessive distal renal tubular acidosis.” Sritippayawan S.et.al. 15211439 [55] “A novel missense mutation in AE1 causing autosomal dominant distal renal tubular acidosis retains normal transport function but is mistargeted in polarized epithelial cells.” Rungroj N.et.al. 14734552 [56] “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.” Lima P.R.M.et.al. 15813913 [57] “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.” Bruce L.J.et.al. 16227998 [58] “The complete amino acid sequence of the human erythrocyte membrane anion-transport protein deduced from the cDNA sequence.” Tanner M.J.A.et.al. 3223947 [59] “Cloning and characterization of band 3, the human erythrocyte anion-exchange protein (AE1).” Lux S.E.et.al. 2594752 [60] “Recessive distal renal tubular acidosis in Sarawak caused by AE1 mutations.” Choo K.E.et.al. 16252102 [61] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).” The MGC Project Teamet.al. 15489334 [62] “Primary structure of the cytoplasmic domain of human erythrocyte protein band 3. Comparison with its sequence in the mouse.” Yannoukakos D.et.al. 2790053 [63] “Amino acid sequence of the N alpha-terminal 201 residues of human erythrocyte membrane band 3.” Kaul R.K.et.al. 6345535 [64] “Orientation of the band 3 polypeptide from human erythrocyte membranes. Identification of NH2-terminal sequence and site of carbohydrate attachment.” Drickamer L.K.et.al. 701248 [65] “Anion exchanger 1 in human kidney and oncocytoma differs from erythroid AE1 in its NH2 terminus.” Kollert-Jons A.et.al. 7506871 [66] “A structural study of the membrane domain of band 3 by tryptic digestion. Conformational change of band 3 in situ induced by alkali treatment.” Kang D.et.al. 1527044 [67] “The human erythrocyte anion-transport protein. Partial amino acid sequence, conformation and a possible molecular mechanism for anion exchange.” Brock C.J.et.al. 6615451 [68] “Anion-proton cotransport through the human red blood cell band 3 protein. Role of glutamate 681.” Jennings M.L.et.al. 1352774 [69] “Band 3 Chur: a variant associated with band 3-deficient hereditary spherocytosis and substitution in a highly conserved position of transmembrane segment 11.” Maillet P.et.al. 8547122 [70] “Localization of the pyridoxal phosphate binding site at the COOH-terminal region of erythrocyte band 3 protein.” Kawano Y.et.al. 3372523 [71] “Phosphorylation sites in human erythrocyte band 3 protein.” Yannoukakos D.et.al. 1998697 [72] “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.” Okubo K.et.al. 1885574 [73] “The ANK repeats of erythrocyte ankyrin form two distinct but cooperative binding sites for the erythrocyte anion exchanger.” Michaely P.et.al. 7665627 [74] “Sequential phosphorylation of protein band 3 by Syk and Lyn tyrosine kinases in intact human erythrocytes: identification of primary and secondary phosphorylation sites.” Brunati A.M.et.al. 10942405 [75] “Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.” Rikova K.et.al. 18083107 [76] “Initial characterization of the human central proteome.” Burkard T.R.et.al. 21269460 [77] “Two-dimensional structure of the membrane domain of human band 3, the anion transport protein of the erythrocyte membrane.” Wang D.N.et.al. 8508760 [78] “Three-dimensional map of the dimeric membrane domain of the human erythrocyte anion exchanger, Band 3.” Wang D.N.et.al. 8045253 [79] “The solution structures of the first and second transmembrane-spanning segments of band 3.” Gargaro A.R.et.al. 8168533 [80] “Solution structure of a band 3 peptide inhibitor bound to aldolase: a proposed mechanism for regulating binding by tyrosine phosphorylation.” Schneider M.L.et.al. 8527430 [81] “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.” Eisenmesser E.Z.et.al. 9454576 [82] “Studies on the structure of a transmembrane region and a cytoplasmic loop of the human red cell anion exchanger.” Chambers E.J.et.al. 9765907 [83] “NMR solution structure of a cytoplasmic surface loop of the human red cell anion transporter, band 3.” Askin D.et.al. 9709005 [84] “Human erythrocyte band 3 polymorphism (band 3 Memphis): characterization of the structural modification (Lys 56-->Glu) by protein chemistry methods.” Yannoukakos D.et.al. 1678289 [85] “Deletion in erythrocyte band 3 gene in malaria-resistant Southeast Asian ovalocytosis.” Jarolim P.et.al. 1722314 [86] “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.” Jarolim P.et.al. 1378323 [87] “Basis of unique red cell membrane properties in hereditary ovalocytosis.” Schofield A.E.et.al. 1538405 [88] “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.” Bruce L.J.et.al. 8343110 [89] “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).” Rybicki A.C.et.al. 8471774 [90] “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.” Bruce L.J.et.al. 8206915 [91] “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.” Bruce L.J.et.al. 7812009 [92] “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.” Jarolim P.et.al. 7530501 [93] “Characterization of 13 novel band 3 gene defects in hereditary spherocytosis with band 3 deficiency.” Jarolim P.et.al. 8943874 [94] “Ankyrin-1 mutations are a major cause of dominant and recessive hereditary spherocytosis.” Eber S.W.et.al. 8640229 [95] “Modulation of clinical expression and band 3 deficiency in hereditary spherocytosis.” Alloisio N.et.al. 9207478 [96] “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.” Miraglia del Giudice E.et.al. 9012689 [97] “Heterogenous band 3 deficiency in hereditary spherocytosis related to different band 3 gene defects.” Dhermy D.et.al. 9233560 [98] “Familial distal renal tubular acidosis is associated with mutations in the red cell anion exchanger (Band 3, AE1) gene.” Bruce L.J.et.al. 9312167 [99] “Blood group antigens Rb(a), Tr(a), and Wd(a) are located in the third ectoplasmic loop of erythroid band 3.” Jarolim P.et.al. 9191821 [100] “Band 3 Tokyo: Thr837-->Ala837 substitution in erythrocyte band 3 protein associated with spherocytic hemolysis.” Iwase S.et.al. 9973643 [101] “Characterization of seven low incidence blood group antigens carried by erythrocyte band 3 protein.” Jarolim P.et.al. 9845551 [102] “Novel AE1 mutations in recessive distal renal tubular acidosis: loss-of-function is rescued by glycophorin A.” Tanphaichitr V.S.et.al. 9854053 [103] “Mutations in the chloride-bicarbonate exchanger gene AE1 cause autosomal dominant but not autosomal recessive distal renal tubular acidosis.” Karet F.E.et.al. 9600966 [104] “A Gly565-->Ala substitution in human erythroid band 3 accounts for the Wu blood group polymorphism.” Zelinski T.et.al. 9709782 [105] “Arginine 490 is a hot spot for mutation in the band 3 gene in hereditary spherocytosis.” Lima P.R.M.et.al. 10580570 [106] “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.” Bruce L.J.et.al. 10926824 [107] “Severe hereditary spherocytosis and distal renal tubular acidosis associated with the total absence of band 3.” Ribeiro M.L.et.al. 10942416 [108] “Characteristic features of the genotype and phenotype of hereditary spherocytosis in the Japanese population.” Yawata Y.et.al. 10745622 [109] “Trafficking and folding defects in hereditary spherocytosis mutants of the human red cell anion exchanger.” Quilty J.A.et.al. 11208088 [110] “Amino acid substitutions in human erythroid protein band 3 account for the low-incidence antigens NFLD and BOW.” McManus K.et.al. 10738034 [111] “An amino acid substitution in the putative second extracellular loop of RBC band 3 accounts for the Froese blood group polymorphism.” McManus K.et.al. 11061863 [112] “Distinctive Swann blood group genotypes: molecular investigations.” Zelinski T.et.al. 11155072 [113] “Band 3 Cape Town (E90K) causes severe hereditary spherocytosis in combination with band 3 Prague III.” Bracher N.A.et.al. 11380459 [114] “Novel compound heterozygous SLC4A1 mutations in Thai patients with autosomal recessive distal renal tubular acidosis.” Sritippayawan S.et.al. 15211439 [115] “A novel missense mutation in AE1 causing autosomal dominant distal renal tubular acidosis retains normal transport function but is mistargeted in polarized epithelial cells.” Rungroj N.et.al. 14734552 [116] “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.” Lima P.R.M.et.al. 15813913 [117] “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.” Bruce L.J.et.al. 16227998
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1: MEELQDDYED MMEENLEQEE YEDPDIPESQ MEEPAAHDTE ATATDYHTTS HPGTHKVYVE 61: LQELVMDEKN QELRWMEAAR WVQLEENLGE NGAWGRPHLS HLTFWSLLEL RRVFTKGTVL 121: LDLQETSLAG VANQLLDRFI FEDQIRPQDR EELLRALLLK HSHAGELEAL GGVKPAVLTR 181: SGDPSQPLLP QHSSLETQLF CEQGDGGTEG HSPSGILEKI PPDSEATLVL VGRADFLEQP 241: VLGFVRLQEA AELEAVELPV PIRFLFVLLG PEAPHIDYTQ LGRAAATLMS ERVFRIDAYM 301: AQSRGELLHS LEGFLDCSLV LPPTDAPSEQ ALLSLVPVQR ELLRRRYQSS PAKPDSSFYK 361: GLDLNGGPDD PLQQTGQLFG GLVRDIRRRY PYYLSDITDA FSPQVLAAVI FIYFAALSPA 421: ITFGGLLGEK TRNQMGVSEL LISTAVQGIL FALLGAQPLL VVGFSGPLLV FEEAFFSFCE 481: TNGLEYIVGR VWIGFWLILL VVLVVAFEGS FLVRFISRYT QEIFSFLISL IFIYETFSKL 541: IKIFQDHPLQ KTYNYNVLMV PKPQGPLPNT ALLSLVLMAG TFFFAMMLRK FKNSSYFPGK 601: LRRVIGDFGV PISILIMVLV DFFIQDTYTQ KLSVPDGFKV SNSSARGWVI HPLGLRSEFP 661: IWMMFASALP ALLVFILIFL ESQITTLIVS KPERKMVKGS GFHLDLLLVV GMGGVAALFG 721: MPWLSATTVR SVTHANALTV MGKASTPGAA AQIQEVKEQR ISGLLVAVLV GLSILMEPIL 781: SRIPLAVLFG IFLYMGVTSL SGIQLFDRIL LLFKPPKYHP DVPYVKRVKT WRMHLFTGIQ 841: IICLAVLWVV KSTPASLALP FVLILTVPLR RVLLPLIFRN VELQCLDADD AKATFDEEEG 901: RDEYDEVAMP V