B3A2_MOUSE
ID B3A2_MOUSE Reviewed; 1237 AA.
AC P13808; Q9ES09; Q9ES10; Q9ES11; Q9ES12; Q9ES13;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 25-MAY-2022, entry version 171.
DE RecName: Full=Anion exchange protein 2;
DE Short=AE 2;
DE Short=Anion exchanger 2;
DE AltName: Full=Band 3-related protein;
DE Short=B3RP;
DE AltName: Full=Non-erythroid band 3-like protein;
DE AltName: Full=Solute carrier family 4 member 2;
GN Name=Slc4a2; Synonyms=Ae2;
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] (ISOFORM A).
RX PubMed=3182834; DOI=10.1016/s0021-9258(18)37502-1;
RA Alper S.L., Kopito R.R., Libresco S.M., Lodish H.F.;
RT "Cloning and characterization of a murine band 3-related cDNA from kidney
RT and from a lymphoid cell line.";
RL J. Biol. Chem. 263:17092-17099(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, AND TISSUE
RP SPECIFICITY.
RX PubMed=11006093; DOI=10.1006/bbrc.2000.3439;
RA Lecanda J., Urtasun R., Medina J.F.;
RT "Molecular cloning and genomic organization of the mouse AE2 anion
RT exchanger gene.";
RL Biochem. Biophys. Res. Commun. 276:117-124(2000).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144; SER-170; SER-172 AND
RP THR-253, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, 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: Plasma membrane anion exchange protein of wide distribution.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=A;
CC IsoId=P13808-1; Sequence=Displayed;
CC Name=B1;
CC IsoId=P13808-2; Sequence=VSP_000458;
CC Name=B2;
CC IsoId=P13808-3; Sequence=VSP_000457;
CC Name=C1;
CC IsoId=P13808-4; Sequence=VSP_000460;
CC Name=C2;
CC IsoId=P13808-5; Sequence=VSP_000459, VSP_000461;
CC -!- TISSUE SPECIFICITY: Isoform a is widely expressed at similar levels in
CC all tissues examined. Isoforms B1 and B2 are predominantly expressed in
CC stomach although they are also detected at lower levels in other
CC tissues. Isoform C1 is stomach-specific. Isoform C2 is expressed at
CC slightly higher levels in lung and stomach than in other tissues.
CC {ECO:0000269|PubMed:11006093}.
CC -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
CC {ECO:0000305}.
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DR EMBL; J04036; AAA65505.1; -; mRNA.
DR EMBL; AF255774; AAG23154.1; -; Genomic_DNA.
DR EMBL; AF255774; AAG23155.1; -; Genomic_DNA.
DR EMBL; AF255774; AAG23156.1; -; Genomic_DNA.
DR EMBL; AF255774; AAG23158.1; -; Genomic_DNA.
DR EMBL; AF255774; AAG23157.1; -; Genomic_DNA.
DR CCDS; CCDS19119.1; -. [P13808-1]
DR PIR; A31789; A31789.
DR RefSeq; NP_001240821.1; NM_001253892.1.
DR RefSeq; NP_033233.2; NM_009207.3.
DR RefSeq; XP_006535713.1; XM_006535650.1.
DR RefSeq; XP_006535714.1; XM_006535651.3.
DR RefSeq; XP_006535718.1; XM_006535655.3.
DR RefSeq; XP_006535719.1; XM_006535656.3.
DR AlphaFoldDB; P13808; -.
DR SMR; P13808; -.
DR BioGRID; 203314; 6.
DR STRING; 10090.ENSMUSP00000078972; -.
DR GlyGen; P13808; 3 sites.
DR iPTMnet; P13808; -.
DR PhosphoSitePlus; P13808; -.
DR EPD; P13808; -.
DR jPOST; P13808; -.
DR MaxQB; P13808; -.
DR PaxDb; P13808; -.
DR PeptideAtlas; P13808; -.
DR PRIDE; P13808; -.
DR ProteomicsDB; 273516; -. [P13808-1]
DR ProteomicsDB; 273517; -. [P13808-2]
DR ProteomicsDB; 273518; -. [P13808-3]
DR ProteomicsDB; 273519; -. [P13808-4]
DR ProteomicsDB; 273520; -. [P13808-5]
DR DNASU; 20535; -.
DR GeneID; 20535; -.
DR KEGG; mmu:20535; -.
DR UCSC; uc008wrm.2; mouse. [P13808-1]
DR CTD; 6522; -.
DR MGI; MGI:109351; Slc4a2.
DR eggNOG; KOG1172; Eukaryota.
DR InParanoid; P13808; -.
DR OrthoDB; 265068at2759; -.
DR PhylomeDB; P13808; -.
DR TreeFam; TF313630; -.
DR Reactome; R-MMU-425381; Bicarbonate transporters.
DR BioGRID-ORCS; 20535; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Slc4a2; mouse.
DR PRO; PR:P13808; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P13808; protein.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015301; F:anion:anion antiporter activity; IBA:GO_Central.
DR GO; GO:0015108; F:chloride transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0005452; F:inorganic anion exchanger activity; IEA:InterPro.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0097186; P:amelogenesis; IDA:ARUK-UCL.
DR GO; GO:0015701; P:bicarbonate transport; IBA:GO_Central.
DR GO; GO:0006821; P:chloride transport; IDA:UniProtKB.
DR GO; GO:0050801; P:ion homeostasis; IBA:GO_Central.
DR GO; GO:0070175; P:positive regulation of enamel mineralization; IDA:ARUK-UCL.
DR GO; GO:0051453; P:regulation of intracellular pH; 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; IPR002978; Anion_exchange_2.
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 PANTHER; PTHR11453:SF14; PTHR11453:SF14; 1.
DR Pfam; PF07565; Band_3_cyto; 1.
DR Pfam; PF00955; HCO3_cotransp; 1.
DR PRINTS; PR00165; ANIONEXCHNGR.
DR PRINTS; PR01188; ANIONEXHNGR2.
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 Alternative splicing; Anion exchange; Antiport; Glycoprotein;
KW Ion transport; Lipoprotein; Membrane; Methylation; Palmitate;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..1237
FT /note="Anion exchange protein 2"
FT /id="PRO_0000079216"
FT TOPO_DOM 1..703
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 704..727
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 733..770
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 790..812
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 822..843
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 844..896
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 897..914
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 915..929
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 930..950
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 984..1006
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1032..1053
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1087..1132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1159..1195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..1237
FT /note="Membrane (anion exchange)"
FT COMPBIAS 32..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..316
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04920"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04920"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04920"
FT MOD_RES 253
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 270
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04920"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04920"
FT LIPID 1169
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 855
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 866
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 878
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..198
FT /note="Missing (in isoform C1)"
FT /evidence="ECO:0000305"
FT /id="VSP_000460"
FT VAR_SEQ 1..166
FT /note="Missing (in isoform C2)"
FT /evidence="ECO:0000305"
FT /id="VSP_000459"
FT VAR_SEQ 1..17
FT /note="MSSAPRRPASGADSLHT -> MTQ (in isoform B1)"
FT /evidence="ECO:0000305"
FT /id="VSP_000458"
FT VAR_SEQ 1..17
FT /note="MSSAPRRPASGADSLHT -> MDFLLRPQ (in isoform B2)"
FT /evidence="ECO:0000305"
FT /id="VSP_000457"
FT VAR_SEQ 167..193
FT /note="ERTSPSPPTQTPHQEAAPRASKGAQTG -> MPAFQEWKSGGLREEAVFGAH
FT GCSVCR (in isoform C2)"
FT /evidence="ECO:0000305"
FT /id="VSP_000461"
FT CONFLICT 205
FT /note="A -> G (in Ref. 2; AAG23154/AAG23155/AAG23156/
FT AAG23158/AAG23157)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1237 AA; 136814 MW; 1A0782C0071782EE CRC64;
MSSAPRRPAS GADSLHTPEP ESLSPGTPGF PEQEEDELRT LGVERFEEIL QEAGSRGGEE
PGRSYGEEDF EYHRQSSHHI HHPLSTHLPP DARRRKTPQG PGRKPRRRPG ASPTGETPTI
EEGEEDEEEA SEAEGFRAPP QQPSPATTPS AVQFFLQEDE GAERKPERTS PSPPTQTPHQ
EAAPRASKGA QTGTLVEEMV AVASATAGGD DGGAAGRPLT KAQPGHRSYN LQERRRIGSM
TGVEQALLPR VPTDESEAQT LATADLDLMK SHRFEDVPGV RRHLVRKNAK GSTQAAREGR
EPGPTPRARP RAPHKPHEVF VELNELLLDK NQEPQWRETA RWIKFEEDVE EETERWGKPH
VASLSFRSLL ELRRTLAHGA VLLDLDQQTL PGVAHQVVEQ MVISDQIKAE DRANVLRALL
LKHSHPSDEK EFSFPRNISA GSLGSLLGHH HAQGTESDPH VTEPLIGGVP ETRLEVDRER
ELPPPAPPAG ITRSKSKHEL KLLEKIPENA EATVVLVGCV EFLSRPTMAF VRLREAVELD
AVLEVPVPVR FLFLLLGPSS ANMDYHEIGR SISTLMSDKQ FHEAAYLADE RDDLLTAINA
FLDCSVVLPP SEVQGEELLR SVAHFQRQML KKREEQGRLL PPGAGLEPKS AQDKALLQMV
EVAGAAEDDP LRRTGRPFGG LIRDVRRRYP HYLSDFRDAL DPQCLAAVIF IYFAALSPAI
TFGGLLGEKT KDLIGVSELI MSTALQGVVF CLLGAQPLLV IGFSGPLLVF EEAFFSFCSS
NELEYLVGRV WIGFWLVFLA LLMVALEGSF LVRFVSRFTQ EIFAFLISLI FIYETFYKLI
KIFQEHPLHG CSGSNDSEAG SSSSSNMTWA TTILVPDNSS ASGQSGQEKP RGQPNTALLS
LVLMAGTFFI AFFLRKFKNS RFFPGRIRRV IGDFGVPIAI LIMVLVDYSI EDTYTQKLSV
PSGFSVTAPD KRGWVINPLG EKTPFPVWMM VASLLPAVLV FILIFMETQI TTLIISKKER
MLQKGSGFHL DLLLIVAMGG ICALFGLPWL AAATVRSVTH ANALTVMSKA VAPGDKPKIQ
EVKEQRVTGL LVALLVGLSM VIGDLLRQIP LAVLFGIFLY MGVTSLNGIQ FYERLHLLLM
PPKHHPDVTY VKKVRTMRMH LFTALQLLCL ALLWAVMSTA ASLAFPFILI LTVPLRMVVL
TRIFTEREMK CLDANEAEPV FDECEGVDEY NEMPMPV
