ID   GBRT_MOUSE              Reviewed;         638 AA.
AC   Q9JLF1;
DT   04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   24-JAN-2024, entry version 167.
DE   RecName: Full=Gamma-aminobutyric acid receptor subunit theta;
DE   AltName: Full=GABA(A) receptor subunit theta;
DE   Flags: Precursor;
GN   Name=Gabrq;
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=10804200; DOI=10.1523/jneurosci.20-10-03588.2000;
RA   Sinkkonen S.T., Hanna M.C., Kirkness E.F., Korpi E.R.;
RT   "GABAA receptor epsilon and theta subunits display unusual structural
RT   variation between species and are enriched in the rat locus ceruleus.";
RL   J. Neurosci. 20:3588-3595(2000).
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. This subunit coassembles with alpha-2,
CC       beta-1 and gamma-1.
CC   -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC       protein. Cell membrane; Multi-pass membrane protein.
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. GABRQ sub-
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF189260; AAF70381.1; -; mRNA.
DR   CCDS; CCDS30188.1; -.
DR   RefSeq; NP_065234.1; NM_020488.2.
DR   RefSeq; XP_006528236.1; XM_006528173.1.
DR   AlphaFoldDB; Q9JLF1; -.
DR   SMR; Q9JLF1; -.
DR   STRING; 10090.ENSMUSP00000033711; -.
DR   ChEMBL; CHEMBL2094133; -.
DR   DrugCentral; Q9JLF1; -.
DR   GlyCosmos; Q9JLF1; 1 site, No reported glycans.
DR   GlyGen; Q9JLF1; 1 site.
DR   PhosphoSitePlus; Q9JLF1; -.
DR   PaxDb; 10090-ENSMUSP00000033711; -.
DR   ProteomicsDB; 272942; -.
DR   Antibodypedia; 73628; 130 antibodies from 21 providers.
DR   DNASU; 57249; -.
DR   Ensembl; ENSMUST00000033711.6; ENSMUSP00000033711.6; ENSMUSG00000031344.12.
DR   GeneID; 57249; -.
DR   KEGG; mmu:57249; -.
DR   UCSC; uc009tkq.2; mouse.
DR   AGR; MGI:1888498; -.
DR   CTD; 55879; -.
DR   MGI; MGI:1888498; Gabrq.
DR   VEuPathDB; HostDB:ENSMUSG00000031344; -.
DR   eggNOG; KOG3643; Eukaryota.
DR   GeneTree; ENSGT00940000162167; -.
DR   InParanoid; Q9JLF1; -.
DR   OMA; IVLYWEG; -.
DR   OrthoDB; 4265336at2759; -.
DR   PhylomeDB; Q9JLF1; -.
DR   TreeFam; TF315453; -.
DR   Reactome; R-MMU-977443; GABA receptor activation.
DR   BioGRID-ORCS; 57249; 4 hits in 80 CRISPR screens.
DR   PRO; PR:Q9JLF1; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; Q9JLF1; Protein.
DR   Bgee; ENSMUSG00000031344; Expressed in secondary oocyte and 24 other cell types or tissues.
DR   ExpressionAtlas; Q9JLF1; baseline and differential.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:1902711; C:GABA-A receptor complex; IBA:GO_Central.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISS:MGI.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043235; C:receptor complex; ISO:MGI.
DR   GO; GO:0045202; C:synapse; IBA:GO_Central.
DR   GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0005230; F:extracellular ligand-gated monoatomic ion channel activity; IEA:InterPro.
DR   GO; GO:0004890; F:GABA-A receptor activity; ISS:MGI.
DR   GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR   GO; GO:1902476; P:chloride transmembrane transport; IBA:GO_Central.
DR   GO; GO:0006821; P:chloride transport; ISS:MGI.
DR   GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; ISS:MGI.
DR   CDD; cd19003; LGIC_ECD_GABAAR_theta; 1.
DR   CDD; cd19056; LGIC_TM_GABAAR_theta; 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; IPR008101; GABAAt_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   NCBIfam; TIGR00860; LIC; 1.
DR   PANTHER; PTHR18945:SF579; GAMMA-AMINOBUTYRIC ACID RECEPTOR SUBUNIT THETA; 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; PR00253; GABAARECEPTR.
DR   PRINTS; PR01725; GABAARTHETA.
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.
DR   Genevisible; Q9JLF1; MM.
PE   2: Evidence at transcript level;
KW   Cell membrane; Chloride; Chloride channel; Disulfide bond; Glycoprotein;
KW   Ion channel; Ion transport; Membrane; Postsynaptic cell membrane;
KW   Reference proteome; Signal; Synapse; Transmembrane; Transmembrane helix;
KW   Transport.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..638
FT                   /note="Gamma-aminobutyric acid receptor subunit theta"
FT                   /id="PRO_0000000496"
FT   TOPO_DOM        22..267
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        268..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        326..346
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        618..638
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          491..515
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        127
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        183..197
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   638 AA;  72799 MW;  4E2C4FA02E9BF8A3 CRC64;
     MGIRGMLRAA ALLLLIRTWL AESNGPSPTP KFHFELSSST PEVILDLFNC KNCANEAVVQ
     KILDRVLSTY DVRLRPNFGG APVPVSVSIY VSSIEQISEI NMDYTITMFL HQTWKDTRLA
     YYETNLNLTL DYRMHEKLWV PDCYFVNSKD AFVHDVTVEN RVFQLHPDGT VRYGIRLTTT
     AACSLDLQKF PMDKQSCKLE VESYGYTVED IVLSWEDDNA IHITDGLHIP QYTYLGRTIT
     SKEVYFYTGS YMRLIVKFQV QREVRSYLVQ VYWPTVLTTI LSWISFWMNY DSSAARVTIG
     LTSILVLTTI DSHMRDKLPH ISCIKAIDIY ILVCLFFVFL SLLEYVYINY LFFSQVPRRN
     HRRCRKPRRV VARYRYQEVV VANVQDGLIN VEDRVEDRAG PLPDSPMQAH LASQESLGSL
     VFTSEQAQLA TSESLSLLSS ASSQTQLATG ESLSDLPSTS EQTVPECTIH FHGFLTNDSI
     IPIKIHSRSD ACDDEDSEES LSSEESHGHG SSHTGRLKLQ ISQRCVQEAS WDLDKIEILQ
     DDISITSSWL GLDEQCKGDA DSIWSLTDEE LMACDQEKDS SSESEENCSP SPGCSFNEGF
     SFQLFKPNRV PKVDRWSRFL FPLSFGLFNV VYWLYHVY
//