ID B1AVY2_MOUSE Unreviewed; 533 AA. AC B1AVY2; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 27-MAR-2024, entry version 118. DE SubName: Full=Gamma-aminobutyric acid (GABA) A receptor, subunit alpha 3 {ECO:0000313|Ensembl:ENSMUSP00000110201.3}; GN Name=Gabra3 {ECO:0000313|Ensembl:ENSMUSP00000110201.3, GN ECO:0000313|MGI:MGI:95615}; 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 {ECO:0000313|Ensembl:ENSMUSP00000110201.3, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0000313|Ensembl:ENSMUSP00000110201.3, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000110201.3, RC ECO:0000313|Proteomes:UP000000589}; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] {ECO:0007829|PubMed:21183079} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [3] {ECO:0000313|Ensembl:ENSMUSP00000110201.3} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000110201.3}; RG Ensembl; RL Submitted (NOV-2023) to UniProtKB. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. Postsynaptic cell membrane CC {ECO:0000256|ARBA:ARBA00034104}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00034104}. Synaptic cell membrane CC {ECO:0000256|ARBA:ARBA00034099}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00034099}. CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family. CC {ECO:0000256|RuleBase:RU000687}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR AlphaFoldDB; B1AVY2; -. DR SMR; B1AVY2; -. DR MaxQB; B1AVY2; -. DR PeptideAtlas; B1AVY2; -. DR ProteomicsDB; 359163; -. DR Antibodypedia; 335; 259 antibodies from 30 providers. DR Ensembl; ENSMUST00000114554.3; ENSMUSP00000110201.3; ENSMUSG00000031343.14. DR AGR; MGI:95615; -. DR MGI; MGI:95615; Gabra3. DR VEuPathDB; HostDB:ENSMUSG00000031343; -. DR GeneTree; ENSGT00940000159444; -. DR HOGENOM; CLU_010920_2_1_1; -. DR PhylomeDB; B1AVY2; -. DR ChiTaRS; Gabra3; mouse. DR Proteomes; UP000000589; Chromosome X. DR Bgee; ENSMUSG00000031343; Expressed in anterior amygdaloid area and 134 other cell types or tissues. DR ExpressionAtlas; B1AVY2; baseline and differential. DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW. DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004890; F:GABA-A receptor activity; IEA:InterPro. DR GO; GO:0022851; F:GABA-gated chloride ion channel activity; IEA:Ensembl. DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IEA:InterPro. DR CDD; cd19036; LGIC_ECD_GABAAR_A3; 1. DR CDD; cd19052; LGIC_TM_GABAAR_alpha; 1. DR Gene3D; 2.70.170.10; Neurotransmitter-gated ion-channel ligand-binding domain; 1. DR Gene3D; 1.20.58.390; Neurotransmitter-gated ion-channel transmembrane domain; 1. DR InterPro; IPR006028; GABAA/Glycine_rcpt. DR InterPro; IPR001390; GABAAa_rcpt. DR InterPro; IPR005433; GABBAa3_rcpt. DR InterPro; IPR047024; Gabra-1-6_TM. 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 NCBIfam; TIGR00860; LIC; 1. DR PANTHER; PTHR18945:SF216; GAMMA-AMINOBUTYRIC ACID RECEPTOR SUBUNIT ALPHA-3; 1. DR PANTHER; PTHR18945; NEUROTRANSMITTER GATED ION CHANNEL; 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; SSF90112; Neurotransmitter-gated ion-channel transmembrane pore; 1. DR SUPFAM; SSF63712; Nicotinic receptor ligand binding domain-like; 1. DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1. PE 1: Evidence at protein level; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475}; KW Chloride {ECO:0000256|ARBA:ARBA00023214}; KW Chloride channel {ECO:0000256|ARBA:ARBA00023173}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000256|RuleBase:RU000687}; KW Ion transport {ECO:0000256|ARBA:ARBA00023065, KW ECO:0000256|RuleBase:RU000687}; KW Ligand-gated ion channel {ECO:0000256|ARBA:ARBA00023286}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU000687}; KW Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257}; KW Proteomics identification {ECO:0007829|MaxQB:B1AVY2, KW ECO:0007829|PeptideAtlas:B1AVY2}; Receptor {ECO:0000256|ARBA:ARBA00023170}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}; KW Signal {ECO:0000256|ARBA:ARBA00022729}; KW Synapse {ECO:0000256|ARBA:ARBA00023018}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU000687}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|RuleBase:RU000687}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000687}. FT TRANSMEM 48..66 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU000687" FT TRANSMEM 316..340 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU000687" FT TRANSMEM 346..366 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU000687" FT TRANSMEM 378..403 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU000687" FT TRANSMEM 502..521 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU000687" FT DOMAIN 109..316 FT /note="Neurotransmitter-gated ion-channel ligand-binding" FT /evidence="ECO:0000259|Pfam:PF02931" FT DOMAIN 323..516 FT /note="Neurotransmitter-gated ion-channel transmembrane" FT /evidence="ECO:0000259|Pfam:PF02932" FT REGION 68..95 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 533 AA; 59912 MW; 5B82129252D544CF CRC64; MEGREERKGG SSHFGPEERS KHLTAACTVD LTGLFKLLSK KMIITQMWHF YVTRVVLLLL ISILPGTTSQ GESRRQEPGD FVKQDIGGLS PKHAPDIPDD STDNITIFTR ILDRLLDGYD NRLRPGLGDA VTEVKTDIYV TSFGPVSDTD MEYTIDVFFR QTWHDERLKF DGPMKILPLN NLLASKIWTP DTFFHNGKKS VAHNMTTPNK LLRLVDNGTL LYTMRLTIHA ECPMHLEDFP MDVHACPLKF GSYAYTKAEV IYSWTLGKNK SVEVAQDGSR LNQYDLLGHV VGTEIIRSST GEYVVMTTHF HLKRKIGYFV IQTYLPCIMT VILSQVSFWL NRESVPARTV FGVTTVLTMT TLSISARNSL PKVAYATAMD WFIAVCYAFV FSALIEFATV NYFTKRSWAW EGKKVPEALE MKKKTPAAPT KKNTTFNIVG TTYPINLAKD TEFSTISKSA AAPSASSTPT AIASPKATYV QDSPAETKTY NSVSKVDKIS RIIFPVLFAI FNLVYWATYV NRESAIKGMI RKQ //