B3AT_MOUSE
ID B3AT_MOUSE Reviewed; 929 AA.
AC P04919;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 197.
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=MEB3;
DE AltName: Full=Solute carrier family 4 member 1;
DE AltName: CD_antigen=CD233;
GN Name=Slc4a1; Synonyms=Ae1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2410791; DOI=10.1038/316234a0;
RA Kopito R.R., Lodish H.F.;
RT "Primary structure and transmembrane orientation of the murine anion
RT exchange protein.";
RL Nature 316:234-238(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3840489; DOI=10.1002/jcb.240290102;
RA Kopito R.R., Lodish H.F.;
RT "Structure of the murine anion exchange protein.";
RL J. Cell. Biochem. 29:1-17(1985).
RN [3]
RP PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3036795; DOI=10.1016/s0021-9258(18)47522-9;
RA Kopito R.R., Andersson M., Lodish H.F.;
RT "Structure and organization of the murine band 3 gene.";
RL J. Biol. Chem. 262:8035-8040(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE.
RA Kopito R.R.;
RL Submitted (JUL-1987) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Limb;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-929.
RX PubMed=3015590; DOI=10.1002/j.1460-2075.1986.tb04348.x;
RA Demuth D.R., Showe L.C., Ballantine M., Palumbo A., Fraser P.J., Cioe L.,
RA Rovera G., Curtis P.J.;
RT "Cloning and structural characterization of a human non-erythroid band 3-
RT like protein.";
RL EMBO J. 5:1205-1214(1986).
RN [7]
RP PROTEIN SEQUENCE OF 33-47; 360-375; 382-395 AND 578-590, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=2713407; DOI=10.1016/0005-2736(89)90315-5;
RA Raida M., Wendel J., Kojro E., Fahrenholz F., Fasold H., Legrum B.,
RA Passow H.;
RT "Major proteolytic fragments of the murine band 3 protein as obtained after
RT in situ proteolysis.";
RL Biochim. Biophys. Acta 980:291-298(1989).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=9490702;
RA Hassoun H., Hanada T., Lutchman M., Sahr K.E., Palek J., Hanspal M.,
RA Chishti A.H.;
RT "Complete deficiency of glycophorin A in red blood cells from mice with
RT targeted inactivation of the band 3 (AE1) gene.";
RL Blood 91:2146-2151(1998).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-363 AND THR-374, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:0000250|UniProtKB:P02730}.
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 TMEM139. {ECO:0000250|UniProtKB:P02730}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2713407};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P02730}. Basolateral
CC cell membrane {ECO:0000250|UniProtKB:P02730}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:P02730}. Note=Detected in the
CC erythrocyte cell membrane and on the basolateral membrane of alpha-
CC intercalated cells in the collecting duct in the kidney.
CC {ECO:0000250|UniProtKB:P02730}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Erythrocyte;
CC IsoId=P04919-1; Sequence=Displayed;
CC Name=2; Synonyms=Kidney;
CC IsoId=P04919-2; Sequence=VSP_000454;
CC -!- TISSUE SPECIFICITY: Detected in erythrocytes (at protein level).
CC {ECO:0000269|PubMed:2713407}.
CC -!- DISRUPTION PHENOTYPE: Gypa is not incorporated in the erythrocyte
CC membrane. {ECO:0000269|PubMed:9490702}.
CC -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
CC {ECO:0000305}.
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DR EMBL; X02677; CAA26506.1; -; mRNA.
DR EMBL; M29379; AAA37187.1; -; mRNA.
DR EMBL; J02756; AAA37278.1; -; Genomic_DNA.
DR EMBL; BC052419; AAH52419.1; -; mRNA.
DR EMBL; BC053429; AAH53429.1; -; mRNA.
DR EMBL; X03917; CAA27555.1; -; mRNA.
DR CCDS; CCDS25496.1; -. [P04919-1]
DR PIR; A25314; A25314.
DR RefSeq; NP_035533.1; NM_011403.2. [P04919-1]
DR AlphaFoldDB; P04919; -.
DR SMR; P04919; -.
DR BioGRID; 203312; 3.
DR IntAct; P04919; 2.
DR STRING; 10090.ENSMUSP00000006749; -.
DR ChEMBL; CHEMBL4523166; -.
DR GlyGen; P04919; 1 site.
DR iPTMnet; P04919; -.
DR PhosphoSitePlus; P04919; -.
DR CPTAC; non-CPTAC-3692; -.
DR jPOST; P04919; -.
DR MaxQB; P04919; -.
DR PaxDb; P04919; -.
DR PeptideAtlas; P04919; -.
DR PRIDE; P04919; -.
DR ProteomicsDB; 265187; -. [P04919-1]
DR ProteomicsDB; 265188; -. [P04919-2]
DR Antibodypedia; 2977; 317 antibodies from 35 providers.
DR DNASU; 20533; -.
DR Ensembl; ENSMUST00000006749; ENSMUSP00000006749; ENSMUSG00000006574. [P04919-1]
DR GeneID; 20533; -.
DR KEGG; mmu:20533; -.
DR UCSC; uc007lrp.2; mouse. [P04919-1]
DR CTD; 6521; -.
DR MGI; MGI:109393; Slc4a1.
DR VEuPathDB; HostDB:ENSMUSG00000006574; -.
DR eggNOG; KOG1172; Eukaryota.
DR GeneTree; ENSGT00940000157423; -.
DR HOGENOM; CLU_002289_1_0_1; -.
DR InParanoid; P04919; -.
DR OMA; VWGRPHL; -.
DR PhylomeDB; P04919; -.
DR TreeFam; TF313630; -.
DR Reactome; R-MMU-1237044; Erythrocytes take up carbon dioxide and release oxygen.
DR Reactome; R-MMU-1247673; Erythrocytes take up oxygen and release carbon dioxide.
DR Reactome; R-MMU-425381; Bicarbonate transporters.
DR BioGRID-ORCS; 20533; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Slc4a1; mouse.
DR PRO; PR:P04919; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P04919; protein.
DR Bgee; ENSMUSG00000006574; Expressed in fetal liver hematopoietic progenitor cell and 191 other tissues.
DR ExpressionAtlas; P04919; baseline and differential.
DR Genevisible; P04919; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0030863; C:cortical cytoskeleton; IDA:MGI.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0014704; C:intercalated disc; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0030018; C:Z disc; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0015301; F:anion:anion antiporter activity; IMP:MGI.
DR GO; GO:0030506; F:ankyrin binding; IPI:MGI.
DR GO; GO:0015106; F:bicarbonate transmembrane transporter activity; IDA:MGI.
DR GO; GO:0015108; F:chloride transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0030492; F:hemoglobin binding; IDA:MGI.
DR GO; GO:0005452; F:inorganic anion exchanger activity; ISS:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006820; P:anion transport; ISO:MGI.
DR GO; GO:0015701; P:bicarbonate transport; IDA:MGI.
DR GO; GO:0007596; P:blood coagulation; IMP:MGI.
DR GO; GO:0006821; P:chloride transport; IDA:UniProtKB.
DR GO; GO:0048821; P:erythrocyte development; IMP:MGI.
DR GO; GO:0050801; P:ion homeostasis; IBA:GO_Central.
DR GO; GO:1904539; P:negative regulation of glycolytic process through fructose-6-phosphate; IMP:MGI.
DR GO; GO:0051354; P:negative regulation of oxidoreductase activity; IMP:MGI.
DR GO; GO:0035811; P:negative regulation of urine volume; IMP:MGI.
DR GO; GO:0045852; P:pH elevation; IMP:MGI.
DR GO; GO:0017121; P:plasma membrane phospholipid scrambling; IMP:MGI.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; ISO:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:MGI.
DR GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
DR GO; GO:0014823; P:response to activity; ISO:MGI.
DR GO; GO:0046685; P:response to arsenic-containing substance; ISO:MGI.
DR GO; GO:0010037; P:response to carbon dioxide; ISO:MGI.
DR GO; GO:0042542; P:response to hydrogen peroxide; ISO:MGI.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
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 Acetylation; Alternative splicing; Anion exchange; Cell membrane;
KW Direct protein sequencing; Glycoprotein; Ion transport; Lipoprotein;
KW Membrane; Palmitate; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..929
FT /note="Band 3 anion transport protein"
FT /id="PRO_0000079210"
FT TOPO_DOM 1..422
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TRANSMEM 423..446
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TOPO_DOM 447..454
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TRANSMEM 455..475
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TOPO_DOM 476..478
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TRANSMEM 479..495
FT /note="Discontinuously helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TOPO_DOM 496..504
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TRANSMEM 505..525
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TOPO_DOM 526..537
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TRANSMEM 538..560
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TOPO_DOM 561..588
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TRANSMEM 589..609
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TOPO_DOM 610..620
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TRANSMEM 621..641
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TOPO_DOM 642..681
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TRANSMEM 682..702
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TOPO_DOM 703..718
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TRANSMEM 719..737
FT /note="Helical; Name=9"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TRANSMEM 738..755
FT /note="Discontinuously helical; Name=10"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TOPO_DOM 756..778
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TRANSMEM 779..799
FT /note="Helical; Name=11"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TRANSMEM 800..818
FT /note="Helical; Name=12"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TOPO_DOM 819..856
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT INTRAMEM 857..887
FT /note="Discontinuously helical"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT TOPO_DOM 888..929
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT REGION 46..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..303
FT /note="Globular"
FT /evidence="ECO:0000250"
FT REGION 190..199
FT /note="Interaction with ANK1"
FT /evidence="ECO:0000250"
FT REGION 317..370
FT /note="Dimerization arm"
FT /evidence="ECO:0000250"
FT REGION 366..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 31
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT MOD_RES 56
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23562"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23562"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 372
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT MOD_RES 374
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 922
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P02730"
FT LIPID 861
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 660
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT VAR_SEQ 1..79
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_000454"
FT CONFLICT 467
FT /note="G -> S (in Ref. 6; CAA27555)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 929 AA; 103136 MW; 5C0E281C394FB614 CRC64;
MGDMRDHEEV LEIPDRDSEE ELENIIGQIA YRDLTIPVTE MQDPEALPTE QTATDYVPSS
TSTPHPSSGQ VYVELQELMM DQRNQELQWV EAAHWIGLEE NLREDGVWGR PHLSYLTFWS
LLELQKVFSK GTFLLGLAET SLAGVANHLL DCFIYEDQIR PQDREELLRA LLLKRSHAED
LGNLEGVKPA VLTRSGGASE PLLPHQPSLE TQLYCGQAEG GSEGPSTSGT LKIPPDSETT
LVLVGRANFL EKPVLGFVRL KEAVPLEDLV LPEPVGFLLV LLGPEAPHVD YTQLGRAAAT
LMTERVFRIT ASMAHNREEL LRSLESFLDC SLVLPPTDAP SEKALLNLVP VQKELLRRRY
LPSPAKPDPN LYNTLDLNGG KGGPGDEDDP LRRTGRIFGG LIRDIRRRYP YYLSDITDAL
SPQVLAAVIF IYFAALSPAV TFGGLLGEKT RNLMGVSELL ISTAVQGILF ALLGAQPLLV
LGFSGPLLVF EEAFFSFCES NNLEYIVGRA WIGFWLILLV MLVVAFEGSF LVQYISRYTQ
EIFSFLISLI FIYETFSKLI KIFQDYPLQQ TYAPVVMKPK PQGPVPNTAL FSLVLMAGTF
LLAMTLRKFK NSTYFPGKLR RVIGDFGVPI SILIMVLVDS FIKGTYTQKL SVPDGLKVSN
SSARGWVIHP LGLYRLFPTW MMFASVLPAL LVFILIFLES QITTLIVSKP ERKMIKGSGF
HLDLLLVVGM GGVAALFGMP WLSATTVRSV THANALTVMG KASGPGAAAQ IQEVKEQRIS
GLLVSVLVGL SILMEPILSR IPLAVLFGIF LYMGVTSLSG IQLFDRILLL FKPPKYHPDV
PFVKRVKTWR MHLFTGIQII CLAVLWVVKS TPASLALPFV LILTVPLRRL ILPLIFRELE
LQCLDGDDAK VTFDEENGLD EYDEVPMPV
