B3A3_MOUSE
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 03-AUG-2022, entry version 175.
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].
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: Plasma membrane anion exchange protein.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
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: Neuronal.
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_033234.2; NM_009208.3. [P16283-1]
DR RefSeq; XP_006496512.1; XM_006496449.3.
DR RefSeq; XP_006496513.1; XM_006496450.3. [P16283-1]
DR RefSeq; XP_006496514.1; XM_006496451.3. [P16283-1]
DR RefSeq; XP_006496515.1; XM_006496452.3.
DR RefSeq; XP_006496516.1; XM_006496453.2. [P16283-1]
DR AlphaFoldDB; P16283; -.
DR SMR; P16283; -.
DR STRING; 10090.ENSMUSP00000116747; -.
DR GlyGen; P16283; 1 site.
DR iPTMnet; P16283; -.
DR PhosphoSitePlus; P16283; -.
DR MaxQB; P16283; -.
DR PaxDb; P16283; -.
DR PeptideAtlas; P16283; -.
DR PRIDE; P16283; -.
DR ProteomicsDB; 273521; -. [P16283-1]
DR ProteomicsDB; 273522; -. [P16283-2]
DR ProteomicsDB; 273523; -. [P16283-3]
DR Antibodypedia; 52538; 33 antibodies from 14 providers.
DR DNASU; 20536; -.
DR Ensembl; ENSMUST00000124341; ENSMUSP00000116747; ENSMUSG00000006576. [P16283-1]
DR GeneID; 20536; -.
DR KEGG; mmu:20536; -.
DR UCSC; uc007bpv.2; mouse. [P16283-1]
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; IMSDQIR; -.
DR PhylomeDB; P16283; -.
DR TreeFam; TF313630; -.
DR Reactome; R-MMU-425381; Bicarbonate transporters.
DR BioGRID-ORCS; 20536; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Slc4a3; mouse.
DR PRO; PR:P16283; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P16283; protein.
DR Bgee; ENSMUSG00000006576; Expressed in perirhinal cortex and 226 other tissues.
DR ExpressionAtlas; P16283; baseline and differential.
DR Genevisible; P16283; MM.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0015301; F:anion:anion antiporter activity; IDA:MGI.
DR GO; GO:0015106; F:bicarbonate transmembrane transporter activity; ISO:MGI.
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:0015701; P:bicarbonate transport; ISO:MGI.
DR GO; GO:0061337; P:cardiac conduction; ISO:MGI.
DR GO; GO:0050801; P:ion homeostasis; IBA:GO_Central.
DR GO; GO:0051453; P:regulation of intracellular pH; IDA: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; 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 PANTHER; PTHR11453; PTHR11453; 1.
DR PANTHER; PTHR11453:SF15; PTHR11453:SF15; 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; 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..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 9..23
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..113
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..151
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..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
