ID   GBRA3_RAT               Reviewed;         493 AA.
AC   P20236; F1LNZ5;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   18-JUL-2018, sequence version 2.
DT   24-JAN-2024, entry version 180.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=2153588; DOI=10.1016/0014-5793(90)80118-3;
RA   Malherbe P., Sigel E., Baur R., Persohn E., Richards J.G., Moehler H.;
RT   "Functional expression and sites of gene transcription of a novel alpha
RT   subunit of the GABAA receptor in rat brain.";
RL   FEBS Lett. 260:261-265(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1966765; DOI=10.1101/sqb.1990.055.01.006;
RA   Seeburg P.H., Wisden W., Verdoorn T., Pritchett D., Werner P., Herb A.,
RA   Lueddens H., Sprengel R., Sakmann B.;
RT   "The GABAA receptor family: molecular and functional diversity.";
RL   Cold Spring Harb. Symp. Quant. Biol. 55:29-40(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
RN   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-163, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=24090084; DOI=10.1021/pr400783j;
RA   Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA   Graham M.E., Packer N.H., Cordwell S.J.;
RT   "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT   heterogeneity.";
RL   J. Proteome Res. 12:5791-5800(2013).
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 (By
CC       similarity). Interacts with GPHN (By similarity).
CC       {ECO:0000250|UniProtKB:P26049, ECO:0000250|UniProtKB:P34903}.
CC   -!- INTERACTION:
CC       P20236; Q03555-6: Gphn; NbExp=5; IntAct=EBI-5273284, EBI-5273276;
CC   -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC       protein. Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed in most brain regions.
CC       {ECO:0000269|PubMed:2153588}.
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; X51991; CAA36247.1; -; mRNA.
DR   EMBL; L08492; AAC42031.1; -; Genomic_DNA.
DR   EMBL; AABR07042312; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07042313; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07042314; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07042315; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07042316; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07042317; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07042318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; A34130; A34130.
DR   RefSeq; NP_058765.3; NM_017069.3.
DR   RefSeq; XP_017457405.1; XM_017601916.1.
DR   PDB; 4TK1; X-ray; 2.70 A; C/D=396-406.
DR   PDB; 4TK2; X-ray; 4.10 A; C/D=396-406.
DR   PDB; 4TK3; X-ray; 2.70 A; C/D=396-406.
DR   PDB; 4TK4; X-ray; 3.60 A; C/D=396-406.
DR   PDB; 4U90; X-ray; 2.00 A; D/E=396-404.
DR   PDB; 6HSN; X-ray; 1.55 A; D/E=396-405.
DR   PDBsum; 4TK1; -.
DR   PDBsum; 4TK2; -.
DR   PDBsum; 4TK3; -.
DR   PDBsum; 4TK4; -.
DR   PDBsum; 4U90; -.
DR   PDBsum; 6HSN; -.
DR   AlphaFoldDB; P20236; -.
DR   SMR; P20236; -.
DR   ComplexPortal; CPX-409; GABA-A receptor, alpha-3/beta-3/gamma-2.
DR   CORUM; P20236; -.
DR   IntAct; P20236; 1.
DR   STRING; 10116.ENSRNOP00000075419; -.
DR   BindingDB; P20236; -.
DR   ChEMBL; CHEMBL328; -.
DR   DrugCentral; P20236; -.
DR   GlyCosmos; P20236; 4 sites, 9 glycans.
DR   GlyGen; P20236; 4 sites, 9 N-linked glycans (1 site).
DR   iPTMnet; P20236; -.
DR   PhosphoSitePlus; P20236; -.
DR   PaxDb; 10116-ENSRNOP00000050712; -.
DR   GeneID; 24947; -.
DR   KEGG; rno:24947; -.
DR   AGR; RGD:2648; -.
DR   CTD; 2556; -.
DR   RGD; 2648; Gabra3.
DR   VEuPathDB; HostDB:ENSRNOG00000056558; -.
DR   eggNOG; KOG3642; Eukaryota.
DR   HOGENOM; CLU_010920_2_1_1; -.
DR   InParanoid; P20236; -.
DR   OrthoDB; 4265336at2759; -.
DR   PhylomeDB; P20236; -.
DR   TreeFam; TF315453; -.
DR   Reactome; R-RNO-977443; GABA receptor activation.
DR   PRO; PR:P20236; -.
DR   Proteomes; UP000002494; Chromosome X.
DR   Bgee; ENSRNOG00000056558; Expressed in frontal cortex and 4 other cell types or tissues.
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:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0098794; C:postsynapse; IBA:GO_Central.
DR   GO; GO:0099634; C:postsynaptic specialization membrane; IDA:SynGO.
DR   GO; GO:0048787; C:presynaptic active zone membrane; IDA:SynGO.
DR   GO; GO:0045202; C:synapse; IDA:SynGO.
DR   GO; GO:0004890; F:GABA-A receptor activity; IDA:RGD.
DR   GO; GO:0022851; F:GABA-gated chloride ion channel activity; ISS:UniProtKB.
DR   GO; GO:0005237; F:inhibitory extracellular ligand-gated monoatomic ion channel activity; IBA:GO_Central.
DR   GO; GO:0099507; F:ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential; IDA:SynGO.
DR   GO; GO:1904315; F:transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential; IDA:SynGO.
DR   GO; GO:0007268; P:chemical synaptic transmission; IMP:RGD.
DR   GO; GO:0099565; P:chemical synaptic transmission, postsynaptic; ISO:RGD.
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:monoatomic ion transmembrane transport; ISO:RGD.
DR   GO; GO:0060078; P:regulation of postsynaptic membrane potential; ISO:RGD.
DR   GO; GO:0051932; P:synaptic transmission, GABAergic; IBA:GO_Central.
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   3D-structure; Cell membrane; Chloride; Chloride channel; Disulfide bond;
KW   Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel;
KW   Membrane; Phosphoprotein; Postsynaptic cell membrane; Receptor;
KW   Reference proteome; Signal; Synapse; Transmembrane; Transmembrane helix;
KW   Transport.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..493
FT                   /note="Gamma-aminobutyric acid receptor subunit alpha-3"
FT                   /id="PRO_0000000439"
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..458
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        459..480
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   REGION          27..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         427
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P26049"
FT   MOD_RES         428
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P26049"
FT   MOD_RES         434
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P26049"
FT   MOD_RES         443
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P26049"
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:0007744|PubMed:24090084"
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   CONFLICT        160
FT                   /note="V -> M (in Ref. 2; AAC42031)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        324
FT                   /note="S -> T (in Ref. 2; AAC42031)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        342
FT                   /note="I -> M (in Ref. 1; CAA36247 and 2; AAC42031)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        409
FT                   /note="K -> L (in Ref. 1; CAA36247)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   493 AA;  55430 MW;  4A685D5E05D76B41 CRC64;
     MITTQMWHFY VTRVGLLLLI SILPGTTGQG 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 KTSTTFNIVG TTYPINLAKD TEFSTISKAA
     AAPSASSTPT VIASPKTTYV QDSPAETKTY NSVSKVDKIS RIIFPVLFAI FNLVYWATYV
     NRESAIKGMI RKQ
//