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Band 3 anion transport protein (Anion exchange protein 1) (AE 1) (Anion exchanger 1) (MEB3) (Solute carrier family 4 member 1) (CD antigen CD233)

 B3AT_MOUSE              Reviewed;         929 AA.
P04919;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
13-AUG-1987, sequence version 1.
05-JUL-2017, entry version 170.
RecName: Full=Band 3 anion transport protein;
AltName: Full=Anion exchange protein 1;
Short=AE 1;
Short=Anion exchanger 1;
AltName: Full=MEB3;
AltName: Full=Solute carrier family 4 member 1;
AltName: CD_antigen=CD233;
Name=Slc4a1; Synonyms=Ae1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2410791; DOI=10.1038/316234a0;
Kopito R.R., Lodish H.F.;
"Primary structure and transmembrane orientation of the murine anion
exchange protein.";
Nature 316:234-238(1985).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3840489; DOI=10.1002/jcb.240290102;
Kopito R.R., Lodish H.F.;
"Structure of the murine anion exchange protein.";
J. Cell. Biochem. 29:1-17(1985).
[3]
PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3036795;
Kopito R.R., Andersson M., Lodish H.F.;
"Structure and organization of the murine band 3 gene.";
J. Biol. Chem. 262:8035-8040(1987).
[4]
NUCLEOTIDE SEQUENCE.
Kopito R.R.;
Submitted (JUL-1987) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Brain, and Limb;
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 11-929.
PubMed=3015590;
Demuth D.R., Showe L.C., Ballantine M., Palumbo A., Fraser P.J.,
Cioe L., Rovera G., Curtis P.J.;
"Cloning and structural characterization of a human non-erythroid band
3-like protein.";
EMBO J. 5:1205-1214(1986).
[7]
PROTEIN SEQUENCE OF 33-47; 360-375; 382-395 AND 578-590, TISSUE
SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=2713407; DOI=10.1016/0005-2736(89)90315-5;
Raida M., Wendel J., Kojro E., Fahrenholz F., Fasold H., Legrum B.,
Passow H.;
"Major proteolytic fragments of the murine band 3 protein as obtained
after in situ proteolysis.";
Biochim. Biophys. Acta 980:291-298(1989).
[8]
DISRUPTION PHENOTYPE.
PubMed=9490702;
Hassoun H., Hanada T., Lutchman M., Sahr K.E., Palek J., Hanspal M.,
Chishti A.H.;
"Complete deficiency of glycophorin A in red blood cells from mice
with targeted inactivation of the band 3 (AE1) gene.";
Blood 91:2146-2151(1998).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-363 AND THR-374,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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:0000250|UniProtKB:P02730}.
-!- 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 TMEM139. {ECO:0000250|UniProtKB:P02730}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2713407};
Multi-pass membrane protein {ECO:0000250|UniProtKB:P02730}.
Basolateral cell membrane {ECO:0000250|UniProtKB:P02730}; Multi-
pass membrane protein {ECO:0000250|UniProtKB:P02730}.
Note=Detected in the erythrocyte cell membrane and on the
basolateral membrane of alpha-intercalated cells in the collecting
duct in the kidney. {ECO:0000250|UniProtKB:P02730}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Erythrocyte;
IsoId=P04919-1; Sequence=Displayed;
Name=2; Synonyms=Kidney;
IsoId=P04919-2; Sequence=VSP_000454;
-!- TISSUE SPECIFICITY: Detected in erythrocytes (at protein level).
{ECO:0000269|PubMed:2713407}.
-!- DISRUPTION PHENOTYPE: Gypa is not incorporated in the erythrocyte
membrane. {ECO:0000269|PubMed:9490702}.
-!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X02677; CAA26506.1; -; mRNA.
EMBL; M29379; AAA37187.1; -; mRNA.
EMBL; J02756; AAA37278.1; -; Genomic_DNA.
EMBL; BC052419; AAH52419.1; -; mRNA.
EMBL; BC053429; AAH53429.1; -; mRNA.
EMBL; X03917; CAA27555.1; -; mRNA.
CCDS; CCDS25496.1; -. [P04919-1]
PIR; A25314; A25314.
RefSeq; NP_035533.1; NM_011403.2. [P04919-1]
UniGene; Mm.7248; -.
ProteinModelPortal; P04919; -.
BioGrid; 203312; 2.
IntAct; P04919; 4.
MINT; MINT-1861446; -.
STRING; 10090.ENSMUSP00000006749; -.
iPTMnet; P04919; -.
PhosphoSitePlus; P04919; -.
PaxDb; P04919; -.
PeptideAtlas; P04919; -.
PRIDE; P04919; -.
Ensembl; ENSMUST00000006749; ENSMUSP00000006749; ENSMUSG00000006574. [P04919-1]
GeneID; 20533; -.
KEGG; mmu:20533; -.
UCSC; uc007lrp.2; mouse. [P04919-1]
CTD; 6521; -.
MGI; MGI:109393; Slc4a1.
eggNOG; KOG1172; Eukaryota.
eggNOG; ENOG410XPHD; LUCA.
GeneTree; ENSGT00760000119021; -.
HOGENOM; HOG000280683; -.
HOVERGEN; HBG004326; -.
InParanoid; P04919; -.
KO; K06573; -.
OMA; WSLLELQ; -.
OrthoDB; EOG091G01FT; -.
PhylomeDB; P04919; -.
TreeFam; TF313630; -.
Reactome; R-MMU-1237044; Erythrocytes take up carbon dioxide and release oxygen.
Reactome; R-MMU-1247673; Erythrocytes take up oxygen and release carbon dioxide.
Reactome; R-MMU-425381; Bicarbonate transporters.
ChiTaRS; Slc4a1; mouse.
PRO; PR:P04919; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000006574; -.
ExpressionAtlas; P04919; baseline and differential.
Genevisible; P04919; MM.
GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
GO; GO:0072562; C:blood microparticle; ISO:MGI.
GO; GO:0030863; C:cortical cytoskeleton; IDA:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0030018; C:Z disc; ISS:UniProtKB.
GO; GO:0015301; F:anion:anion antiporter activity; ISS:UniProtKB.
GO; GO:0030506; F:ankyrin binding; ISO:MGI.
GO; GO:0015106; F:bicarbonate transmembrane transporter activity; ISS:UniProtKB.
GO; GO:0015108; F:chloride transmembrane transporter activity; IDA:UniProtKB.
GO; GO:0005452; F:inorganic anion exchanger activity; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0008510; F:sodium:bicarbonate symporter activity; IBA:GO_Central.
GO; GO:0006820; P:anion transport; ISO:MGI.
GO; GO:0015701; P:bicarbonate transport; ISS:UniProtKB.
GO; GO:0006821; P:chloride transport; IDA: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;
Acetylation; Alternative splicing; Anion exchange; Cell membrane;
Complete proteome; Direct protein sequencing; Glycoprotein;
Ion transport; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
Reference proteome; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 929 Band 3 anion transport protein.
/FTId=PRO_0000079210.
TOPO_DOM 1 422 Cytoplasmic.
{ECO:0000250|UniProtKB:P02730}.
TRANSMEM 423 446 Helical; Name=1.
{ECO:0000250|UniProtKB:P02730}.
TOPO_DOM 447 454 Extracellular.
{ECO:0000250|UniProtKB:P02730}.
TRANSMEM 455 475 Helical; Name=2.
{ECO:0000250|UniProtKB:P02730}.
TOPO_DOM 476 478 Cytoplasmic.
{ECO:0000250|UniProtKB:P02730}.
TRANSMEM 479 495 Discontinuously helical; Name=3.
{ECO:0000250|UniProtKB:P02730}.
TOPO_DOM 496 504 Extracellular.
{ECO:0000250|UniProtKB:P02730}.
TRANSMEM 505 525 Helical; Name=4.
{ECO:0000250|UniProtKB:P02730}.
TOPO_DOM 526 537 Cytoplasmic.
{ECO:0000250|UniProtKB:P02730}.
TRANSMEM 538 560 Helical; Name=5.
{ECO:0000250|UniProtKB:P02730}.
TOPO_DOM 561 588 Extracellular.
{ECO:0000250|UniProtKB:P02730}.
TRANSMEM 589 609 Helical; Name=6.
{ECO:0000250|UniProtKB:P02730}.
TOPO_DOM 610 620 Cytoplasmic.
{ECO:0000250|UniProtKB:P02730}.
TRANSMEM 621 641 Helical; Name=7.
{ECO:0000250|UniProtKB:P02730}.
TOPO_DOM 642 681 Extracellular.
{ECO:0000250|UniProtKB:P02730}.
TRANSMEM 682 702 Helical; Name=8.
{ECO:0000250|UniProtKB:P02730}.
TOPO_DOM 703 718 Cytoplasmic.
{ECO:0000250|UniProtKB:P02730}.
TRANSMEM 719 737 Helical; Name=9.
{ECO:0000250|UniProtKB:P02730}.
TRANSMEM 738 755 Discontinuously helical; Name=10.
{ECO:0000250|UniProtKB:P02730}.
TOPO_DOM 756 778 Cytoplasmic.
{ECO:0000250|UniProtKB:P02730}.
TRANSMEM 779 799 Helical; Name=11.
{ECO:0000250|UniProtKB:P02730}.
TRANSMEM 800 818 Helical; Name=12.
{ECO:0000250|UniProtKB:P02730}.
TOPO_DOM 819 856 Cytoplasmic.
{ECO:0000250|UniProtKB:P02730}.
INTRAMEM 857 887 Discontinuously helical.
{ECO:0000250|UniProtKB:P02730}.
TOPO_DOM 888 929 Cytoplasmic.
{ECO:0000250|UniProtKB:P02730}.
REGION 69 303 Globular. {ECO:0000250}.
REGION 190 199 Interaction with ANK1. {ECO:0000250}.
REGION 317 370 Dimerization arm. {ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P02730}.
MOD_RES 18 18 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 31 31 Phosphotyrosine.
{ECO:0000250|UniProtKB:P02730}.
MOD_RES 56 56 Phosphotyrosine.
{ECO:0000250|UniProtKB:P02730}.
MOD_RES 199 199 Phosphoserine.
{ECO:0000250|UniProtKB:P23562}.
MOD_RES 222 222 Phosphoserine.
{ECO:0000250|UniProtKB:P23562}.
MOD_RES 363 363 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 372 372 Phosphotyrosine.
{ECO:0000250|UniProtKB:P02730}.
MOD_RES 374 374 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 922 922 Phosphotyrosine.
{ECO:0000250|UniProtKB:P02730}.
LIPID 861 861 S-palmitoyl cysteine. {ECO:0000250}.
CARBOHYD 660 660 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
VAR_SEQ 1 79 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_000454.
CONFLICT 467 467 G -> S (in Ref. 6; CAA27555).
{ECO:0000305}.
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


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