ID   B3A3_MOUSE              Reviewed;        1227 AA.
AC   P16283; Q9ERP5;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   02-SEP-2026, entry version 193.
DE   RecName: Full=Anion exchange protein 3;
DE            Short=AE 3;
DE            Short=Anion exchanger 3;
DE   AltName: Full=Neuronal band 3-like protein;
DE   AltName: Full=Solute carrier family 4 member 3;
GN   Name=Slc4a3; Synonyms=Ae3;
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], FUNCTION, TRANSPORTER ACTIVITY, ACTIVITY
RP   REGULATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=2686841; DOI=10.1016/0092-8674(89)90615-6;
RA   Kopito R.R., Lee B.S., Simmons D.M., Lindsey A.E., Morgans C.W.,
RA   Schneider K.;
RT   "Regulation of intracellular pH by a neuronal homolog of the erythrocyte
RT   anion exchanger.";
RL   Cell 59:927-937(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RX   PubMed=8126106; DOI=10.1242/jcs.106.4.1275;
RA   Morgans C.W., Kopito R.R.;
RT   "Generation of truncated brain AE3 isoforms by alternate mRNA processing.";
RL   J. Cell Sci. 106:1275-1282(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Sv;
RX   PubMed=12592704; DOI=10.1080/1042517021000011654;
RA   Iwaasa M., Tatewaki H., Ohno T., Okubo K., Hamasaki N., Kang D.;
RT   "Genomic cloning and promoter analysis of a mouse anion exchanger 3 (AE3)
RT   gene.";
RL   DNA Seq. 13:251-255(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA   Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in naive
RT   and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167; SER-170 AND SER-198, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Heart;
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).
RN   [7]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-294, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
CC   -!- FUNCTION: Sodium-independent anion exchanger which mediates the
CC       electroneutral exchange of chloride for bicarbonate ions across the
CC       cell membrane. May be involved in the regulation of intracellular pH,
CC       and the modulation of cardiac action potential (By similarity).
CC       {ECO:0000250|UniProtKB:P48751, ECO:0000269|PubMed:2686841}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hydrogencarbonate(in) + chloride(out) = hydrogencarbonate(out)
CC         + chloride(in); Xref=Rhea:RHEA:72363, ChEBI:CHEBI:17544,
CC         ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:2686841};
CC   -!- ACTIVITY REGULATION: Inhibited by 4,4'-diisothiocyanatostilbene-2,2'-
CC       disulfonic acid (DIDS). {ECO:0000269|PubMed:2686841}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2686841};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=FL-AE3;
CC         IsoId=P16283-1; Sequence=Displayed;
CC       Name=311-AE3;
CC         IsoId=P16283-2; Sequence=VSP_000464, VSP_000465;
CC       Name=14-AE3;
CC         IsoId=P16283-3; Sequence=VSP_000466, VSP_000467;
CC   -!- TISSUE SPECIFICITY: Expressed in the brain.
CC       {ECO:0000269|PubMed:2686841}.
CC   -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
CC       {ECO:0000305}.
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DR   EMBL; M28383; AAA37184.1; -; mRNA.
DR   EMBL; S69314; AAB30140.1; -; mRNA.
DR   EMBL; AF294651; AAG25582.1; -; Genomic_DNA.
DR   EMBL; CH466548; EDL00426.1; -; Genomic_DNA.
DR   CCDS; CCDS15080.1; -. [P16283-1]
DR   PIR; A33638; A33638.
DR   RefSeq; NP_001344078.1; NM_001357149.1. [P16283-1]
DR   RefSeq; NP_001344079.1; NM_001357150.1. [P16283-1]
DR   RefSeq; NP_033234.2; NM_009208.3. [P16283-1]
DR   RefSeq; XP_006496513.1; XM_006496450.4. [P16283-1]
DR   RefSeq; XP_006496514.1; XM_006496451.4. [P16283-1]
DR   RefSeq; XP_006496516.1; XM_006496453.3. [P16283-1]
DR   AlphaFoldDB; P16283; -.
DR   SMR; P16283; -.
DR   BioGRID; 203315; 1.
DR   FunCoup; P16283; 261.
DR   STRING; 10090.ENSMUSP00000116747; -.
DR   GlyCosmos; P16283; 1 site, No reported glycans.
DR   GlyGen; P16283; 2 sites, 1 N-linked glycan (1 site).
DR   iPTMnet; P16283; -.
DR   PhosphoSitePlus; P16283; -.
DR   PaxDb; 10090-ENSMUSP00000116747; -.
DR   PeptideAtlas; P16283; -.
DR   ProteomicsDB; 273521; -. [P16283-1]
DR   ProteomicsDB; 273522; -. [P16283-2]
DR   ProteomicsDB; 273523; -. [P16283-3]
DR   Antibodypedia; 52538; 35 antibodies from 15 providers.
DR   DNASU; 20536; -.
DR   Ensembl; ENSMUST00000124341.8; ENSMUSP00000116747.2; ENSMUSG00000006576.17. [P16283-1]
DR   GeneID; 20536; -.
DR   KEGG; mmu:20536; -.
DR   UCSC; uc007bpv.2; mouse. [P16283-1]
DR   AGR; MGI:109350; -.
DR   CTD; 6508; -.
DR   MGI; MGI:109350; Slc4a3.
DR   VEuPathDB; HostDB:ENSMUSG00000006576; -.
DR   eggNOG; KOG1172; Eukaryota.
DR   GeneTree; ENSGT00940000159765; -.
DR   HOGENOM; CLU_002289_1_0_1; -.
DR   InParanoid; P16283; -.
DR   OMA; CLMNVGC; -.
DR   OrthoDB; 1735926at2759; -.
DR   PhylomeDB; P16283; -.
DR   Reactome; R-MMU-425381; Bicarbonate transporters.
DR   BioGRID-ORCS; 20536; 3 hits in 76 CRISPR screens.
DR   PRO; PR:P16283; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; P16283; protein.
DR   Bgee; ENSMUSG00000006576; Expressed in perirhinal cortex and 227 other cell types or tissues.
DR   ExpressionAtlas; P16283; baseline and differential.
DR   GO; GO:0009897; C:external side of plasma membrane; ISO:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0015106; F:bicarbonate transmembrane transporter activity; ISO:GO_Central.
DR   GO; GO:0140900; F:chloride:bicarbonate antiporter activity; IDA:UniProtKB.
DR   GO; GO:0019899; F:enzyme binding; ISO:GO_Central.
DR   GO; GO:0015701; P:bicarbonate transport; ISO:GO_Central.
DR   GO; GO:0061337; P:cardiac conduction; ISO:GO_Central.
DR   GO; GO:0045851; P:pH reduction; ISS:UniProtKB.
DR   GO; GO:0098901; P:regulation of cardiac muscle cell action potential; ISS:UniProtKB.
DR   GO; GO:0051453; P:regulation of intracellular pH; IDA:MGI.
DR   FunFam; 1.10.287.570:FF:000001; Anion exchange protein; 1.
DR   FunFam; 3.40.930.10:FF:000004; Anion exchange protein; 1.
DR   Gene3D; 1.10.287.570; Helical hairpin bin; 1.
DR   Gene3D; 3.40.930.10; Mannitol-specific EII, Chain A; 1.
DR   InterPro; IPR001717; Anion_exchange.
DR   InterPro; IPR002979; Anion_exchange_3.
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   NCBIfam; TIGR00834; ae; 1.
DR   PANTHER; PTHR11453; ANION EXCHANGE PROTEIN; 1.
DR   PANTHER; PTHR11453:SF15; ANION EXCHANGE PROTEIN 3; 1.
DR   Pfam; PF07565; Band_3_cyto; 1.
DR   Pfam; PF00955; HCO3_cotransp; 1.
DR   PRINTS; PR00165; ANIONEXCHNGR.
DR   PRINTS; PR01189; ANIONEXHNGR3.
DR   PRINTS; PR01231; HCO3TRNSPORT.
DR   SUPFAM; SSF55804; Phoshotransferase/anion transport protein; 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; Cell membrane;
KW   Glycoprotein; Ion transport; Lipoprotein; Membrane; Methylation; Palmitate;
KW   Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..1227
FT                   /note="Anion exchange protein 3"
FT                   /id="PRO_0000079220"
FT   TOPO_DOM        1..707
FT                   /note="Cytoplasmic"
FT   TRANSMEM        708..730
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        736..773
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        793..815
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        825..846
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        888..905
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        906..920
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        921..941
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        975..997
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1023..1044
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1078..1123
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1150..1186
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          286..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          428..497
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          708..1227
FT                   /note="Membrane (anion exchange)"
FT   COMPBIAS        1..11
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..75
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        76..97
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..113
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        134..152
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..215
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        435..448
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        480..497
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         167
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         170
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         175
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P23348"
FT   MOD_RES         198
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         294
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   LIPID           1160
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        868
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         381..391
FT                   /note="AALLDLEQTTL -> RAFWAGNESLL (in isoform 311-AE3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_000464"
FT   VAR_SEQ         392..1227
FT                   /note="Missing (in isoform 311-AE3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_000465"
FT   VAR_SEQ         487..503
FT                   /note="KPLHMPGGDGHRGKSLK -> FCVLRSPSPCLGETVTEGKA (in
FT                   isoform 14-AE3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_000466"
FT   VAR_SEQ         504..1227
FT                   /note="Missing (in isoform 14-AE3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_000467"
FT   CONFLICT        530
FT                   /note="A -> G (in Ref. 1; AAA37184)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        812
FT                   /note="S -> T (in Ref. 1; AAA37184)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1150..1151
FT                   /note="MH -> ID (in Ref. 1; AAA37184)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1187..1188
FT                   /note="RR -> SG (in Ref. 1; AAA37184)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1227 AA;  135373 MW;  68BC64B72E5FDC55 CRC64;
     MANGVIPPPG GASPLPQVRV PLEEPPLGPD VEEEDDDLGK TLAVSRFGDL ISKTPAWDPE
     KPSRSYSERD FEFHRHTSHH THHPLSARLP PPHKLRRPPP TSARHTRRKR KKEKTSAPPS
     EGTPPIQEEG GAGAEEEEEE EEEEEGESEA EPVEPLPPGP PQKAKFSIGS DEDDSPGLPV
     KAPCAKALPS VGLQSDQSPQ RSGSSPSPRA RASRISTEKS RPWSPSASYD LRERLCPGSA
     LGNPGPEQRV PTDEAEAQML GSADLDDMKS HRLEDNPGVR RHLVKKPSRI QGGRGSPSGL
     APILRRKKKK KKLDRRPHEV FVELNELMLD RSQEPHWRET ARWIKFEEDV EEETERWGKP
     HVASLSFRSL LELRRTIAQG AALLDLEQTT LPGIAHLVVE TMIVSDQIRP EDRASVLRTL
     LLKHSHPNDD KDSGFFPRNP SSSSVNSVLG NHHPTPSHGP DGAVPTMADD QGEPAPLWPH
     DPDAKEKPLH MPGGDGHRGK SLKLLEKIPE DAEATVVLVG CVPFLEQPAA AFVRLSEAVL
     LESVLEVPVP VRFLFVMLGP SHTSTDYHEL GRSIATLMSD KLFHEAAYQA DDRQDLLGAI
     SEFLDGSIVI PPSEVEGRDL LRSVAAFQRE LLRKRREREQ TKVEMTTRGG YAAPGKELSL
     EMGGSEATSE DDPLQRTGSV FGGLVRDVKR RYPHYPSDLR DALHSQCVAA VLFIYFAALS
     PAITFGGLLG EKTEGLMGVS ELIVSTAVLG VLFSLLGAQP LLVVGFSGPL LVFEEAFFKF
     CRAQDLEYLT GRVWVGLWLV VFVLALVAAE GSFLVRYISP FTQEIFAFLI SLIFIYETFH
     KLYKVFTEHP LLPFYPPDEA LETGLELNSS ALPPTEGPPG PRNQPNTALL SLILMLGTFL
     IAFFLRKFRN SRFLGGKARR IIGDFGIPIS ILVMVLVDYS ITDTYTQKLT VPTGLSVTSP
     HKRTWFIPPL GSARPFPPWM MVAAAVPALL VLILIFMETQ ITALIVSQKA RRLLKGSGFH
     LDLLLIGSLG GLCGLFGLPW LTAATVRSVT HVNALTVMRT AIAPGDKPQI QEVREQRVTG
     VLIASLVGLS IVMGAVLRRI PLAVLFGIFL YMGVTSLSGI QLSQRLLLIF MPAKHHPEQP
     YVTKVKTWRM HLFTCIQLGC IALLWVVKST AASLAFPFLL LLTVPLRRCL LPRLFQDREL
     QALDSEDAEP NFDEDGQDEY NELHMPV
//