GBRA3_MOUSE
ID GBRA3_MOUSE Reviewed; 492 AA.
AC P26049;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Gamma-aminobutyric acid receptor subunit alpha-3;
DE AltName: Full=GABA(A) receptor subunit alpha-3;
DE Flags: Precursor;
GN Name=Gabra3; Synonyms=Gabra-3;
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].
RC STRAIN=C57BL/6J, and DBA/2J; TISSUE=Brain;
RX PubMed=1356407;
RA Wang J.B., Kofuji P., Fernando J.C., Moss S.J., Huganir R.L., Burt D.R.;
RT "The alpha 1, alpha 2, and alpha 3 subunits of GABAA receptors: comparison
RT in seizure-prone and -resistant mice and during development.";
RL J. Mol. Neurosci. 3:177-184(1992).
RN [2]
RP INTERACTION WITH UBQLN1.
RX PubMed=11528422; DOI=10.1038/nn0901-908;
RA Bedford F.K., Kittler J.T., Muller E., Thomas P., Uren J.M., Merlo D.,
RA Wisden W., Triller A., Smart T.G., Moss S.J.;
RT "GABA(A) receptor cell surface number and subunit stability are regulated
RT by the ubiquitin-like protein Plic-1.";
RL Nat. Neurosci. 4:908-916(2001).
RN [3]
RP RNA EDITING OF POSITION 342.
RX PubMed=17369310; DOI=10.1261/rna.349107;
RA Ohlson J., Pedersen J.S., Haussler D., Ohman M.;
RT "Editing modifies the GABA(A) receptor subunit alpha3.";
RL RNA 13:698-703(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-426; THR-427; SER-433 AND
RP SER-442, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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: GABA, the major inhibitory neurotransmitter in the vertebrate
CC brain, mediates neuronal inhibition by binding to the
CC GABA/benzodiazepine receptor and opening an integral chloride channel.
CC -!- SUBUNIT: Generally pentameric. There are five types of GABA(A) receptor
CC chains: alpha, beta, gamma, delta, and rho. Binds UBQLN1
CC (PubMed:11528422). Interacts with GPHN (By similarity).
CC {ECO:0000250|UniProtKB:P34903, ECO:0000269|PubMed:11528422}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC protein. Cell membrane; Multi-pass membrane protein.
CC -!- RNA EDITING: Modified_positions=342 {ECO:0000269|PubMed:17369310};
CC Note=The extent of editing is low at birth but increases with age,
CC reaching close to 100% in the adult brain.;
CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily. GABRA3 sub-
CC subfamily. {ECO:0000305}.
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DR EMBL; M86568; AAA37651.1; -; mRNA.
DR CCDS; CCDS30187.1; -.
DR RefSeq; NP_032093.3; NM_008067.4.
DR RefSeq; XP_006527886.1; XM_006527823.3.
DR RefSeq; XP_011245824.1; XM_011247522.2.
DR AlphaFoldDB; P26049; -.
DR SMR; P26049; -.
DR BioGRID; 199799; 1.
DR ComplexPortal; CPX-2982; GABA-A receptor, alpha-3/beta-3/gamma-2.
DR STRING; 10090.ENSMUSP00000062638; -.
DR ChEMBL; CHEMBL2094133; -.
DR DrugCentral; P26049; -.
DR GlyConnect; 2322; 8 N-Linked glycans (3 sites).
DR GlyGen; P26049; 4 sites, 8 N-linked glycans (3 sites).
DR iPTMnet; P26049; -.
DR PhosphoSitePlus; P26049; -.
DR MaxQB; P26049; -.
DR PaxDb; P26049; -.
DR PRIDE; P26049; -.
DR ProteomicsDB; 267773; -.
DR Antibodypedia; 335; 222 antibodies from 30 providers.
DR DNASU; 14396; -.
DR Ensembl; ENSMUST00000055966; ENSMUSP00000062638; ENSMUSG00000031343.
DR GeneID; 14396; -.
DR KEGG; mmu:14396; -.
DR UCSC; uc009tkp.2; mouse.
DR CTD; 2556; -.
DR MGI; MGI:95615; Gabra3.
DR VEuPathDB; HostDB:ENSMUSG00000031343; -.
DR eggNOG; KOG3642; Eukaryota.
DR GeneTree; ENSGT00940000159444; -.
DR HOGENOM; CLU_010920_2_2_1; -.
DR InParanoid; P26049; -.
DR OMA; LTKKANN; -.
DR OrthoDB; 1057372at2759; -.
DR PhylomeDB; P26049; -.
DR TreeFam; TF315453; -.
DR Reactome; R-MMU-977443; GABA receptor activation.
DR BioGRID-ORCS; 14396; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Gabra3; mouse.
DR PRO; PR:P26049; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; P26049; protein.
DR Bgee; ENSMUSG00000031343; Expressed in anterior amygdaloid area and 131 other tissues.
DR ExpressionAtlas; P26049; baseline and differential.
DR Genevisible; P26049; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0032590; C:dendrite membrane; IBA:GO_Central.
DR GO; GO:1902711; C:GABA-A receptor complex; IBA:GO_Central.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099060; C:integral component of postsynaptic specialization membrane; IDA:SynGO.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0098794; C:postsynapse; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0004890; F:GABA-A receptor activity; ISO:MGI.
DR GO; GO:0022851; F:GABA-gated chloride ion channel activity; IBA:GO_Central.
DR GO; GO:0005237; F:inhibitory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IDA:SynGO.
DR GO; GO:0007268; P:chemical synaptic transmission; ISO:MGI.
DR GO; GO:1902476; P:chloride transmembrane transport; IBA:GO_Central.
DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IBA:GO_Central.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:0060078; P:regulation of postsynaptic membrane potential; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0051932; P:synaptic transmission, GABAergic; IBA:GO_Central.
DR Gene3D; 1.20.58.390; -; 1.
DR Gene3D; 2.70.170.10; -; 1.
DR InterPro; IPR006028; GABAA/Glycine_rcpt.
DR InterPro; IPR001390; GABAAa_rcpt.
DR InterPro; IPR005433; GABBAa3_rcpt.
DR InterPro; IPR006202; Neur_chan_lig-bd.
DR InterPro; IPR036734; Neur_chan_lig-bd_sf.
DR InterPro; IPR006201; Neur_channel.
DR InterPro; IPR036719; Neuro-gated_channel_TM_sf.
DR InterPro; IPR038050; Neuro_actylchol_rec.
DR InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR PANTHER; PTHR18945; PTHR18945; 1.
DR Pfam; PF02931; Neur_chan_LBD; 1.
DR Pfam; PF02932; Neur_chan_memb; 1.
DR PRINTS; PR01079; GABAARALPHA.
DR PRINTS; PR01616; GABAARALPHA3.
DR PRINTS; PR00253; GABAARECEPTR.
DR PRINTS; PR00252; NRIONCHANNEL.
DR SUPFAM; SSF63712; SSF63712; 1.
DR SUPFAM; SSF90112; SSF90112; 1.
DR TIGRFAMs; TIGR00860; LIC; 1.
DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Chloride; Chloride channel; Disulfide bond; Glycoprotein;
KW Ion channel; Ion transport; Ligand-gated ion channel; Membrane;
KW Phosphoprotein; Postsynaptic cell membrane; Receptor; Reference proteome;
KW RNA editing; Signal; Synapse; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..492
FT /note="Gamma-aminobutyric acid receptor subunit alpha-3"
FT /id="PRO_0000000438"
FT TOPO_DOM 29..276
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 277..298
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TRANSMEM 304..325
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TRANSMEM 338..359
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 360..457
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 458..479
FT /note="Helical"
FT /evidence="ECO:0000305"
FT REGION 27..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 427
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 191..205
FT /evidence="ECO:0000250"
FT VARIANT 342
FT /note="I -> M (in RNA edited version)"
SQ SEQUENCE 492 AA; 55398 MW; 3CA193B97833CAE2 CRC64;
MIITQMWHFY VTRVVLLLLI SILPGTTSQG ESRRQEPGDF VKQDIGGLSP KHAPDIPDDS
TDNITIFTRI LDRLLDGYDN RLRPGLGDAV TEVKTDIYVT SFGPVSDTDM EYTIDVFFRQ
TWHDERLKFD GPMKILPLNN LLASKIWTPD TFFHNGKKSV AHNMTTPNKL LRLVDNGTLL
YTMRLTIHAE CPMHLEDFPM DVHACPLKFG SYAYTKAEVI YSWTLGKNKS VEVAQDGSRL
NQYDLLGHVV GTEIIRSSTG EYVVMTTHFH LKRKIGYFVI QTYLPCIMTV ILSQVSFWLN
RESVPARTVF GVTTVLTMTT LSISARNSLP KVAYATAMDW FIAVCYAFVF SALIEFATVN
YFTKRSWAWE GKKVPEALEM KKKTPAAPTK KNTTFNIVGT TYPINLAKDT EFSTISKSAA
APSASSTPTA IASPKATYVQ DSPAETKTYN SVSKVDKISR IIFPVLFAIF NLVYWATYVN
RESAIKGMIR KQ
