ID   GBRR1_MOUSE             Reviewed;         480 AA.
AC   P56475; A3KG51;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   27-MAR-2024, entry version 174.
DE   RecName: Full=Gamma-aminobutyric acid receptor subunit rho-1;
DE   AltName: Full=GABA(A) receptor subunit rho-1;
DE   AltName: Full=GABA(C) receptor;
DE   Flags: Precursor;
GN   Name=Gabrr1;
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   TISSUE=Retina;
RA   Greka A., Koolen J.A., Lipton S.A., Zhang D.;
RT   "Molecular cloning of GABA rho subunits in the mouse retina.";
RL   Abstr. - Soc. Neurosci. 23:1262-1262(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
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).
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       Rho-1 GABA receptor could play a role in retinal neurotransmission (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Generally pentameric. There are five types of GABA(A) receptor
CC       chains: alpha, beta, gamma, delta, and rho. Interacts with SQSTM1 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250}; Multi-
CC       pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
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. GABRR1 sub-
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB81964.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAM45896.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF024620; AAB81964.1; ALT_INIT; mRNA.
DR   EMBL; AL670464; CAM45896.1; ALT_INIT; Genomic_DNA.
DR   CCDS; CCDS18021.2; -.
DR   RefSeq; NP_032101.3; NM_008075.2.
DR   AlphaFoldDB; P56475; -.
DR   SMR; P56475; -.
DR   STRING; 10090.ENSMUSP00000029947; -.
DR   GlyCosmos; P56475; 3 sites, No reported glycans.
DR   GlyGen; P56475; 3 sites.
DR   iPTMnet; P56475; -.
DR   PhosphoSitePlus; P56475; -.
DR   PaxDb; 10090-ENSMUSP00000029947; -.
DR   ProteomicsDB; 268854; -.
DR   Antibodypedia; 31856; 262 antibodies from 24 providers.
DR   DNASU; 14408; -.
DR   Ensembl; ENSMUST00000029947.6; ENSMUSP00000029947.7; ENSMUSG00000028280.10.
DR   GeneID; 14408; -.
DR   KEGG; mmu:14408; -.
DR   UCSC; uc008sfr.2; mouse.
DR   AGR; MGI:95625; -.
DR   CTD; 2569; -.
DR   MGI; MGI:95625; Gabrr1.
DR   VEuPathDB; HostDB:ENSMUSG00000028280; -.
DR   eggNOG; KOG3643; Eukaryota.
DR   GeneTree; ENSGT00940000158591; -.
DR   HOGENOM; CLU_010920_0_1_1; -.
DR   InParanoid; P56475; -.
DR   OMA; WRKRDIQ; -.
DR   OrthoDB; 4265336at2759; -.
DR   PhylomeDB; P56475; -.
DR   TreeFam; TF315453; -.
DR   Reactome; R-MMU-977443; GABA receptor activation.
DR   BioGRID-ORCS; 14408; 2 hits in 75 CRISPR screens.
DR   PRO; PR:P56475; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; P56475; Protein.
DR   Bgee; ENSMUSG00000028280; Expressed in retinal neural layer and 5 other cell types or tissues.
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:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042734; C:presynaptic membrane; IDA:SynGO.
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:0016917; F:GABA receptor activity; ISO:MGI.
DR   GO; GO:0004890; F:GABA-A receptor activity; IEA:InterPro.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0099507; F:ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential; IDA:SynGO.
DR   GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR   GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR   GO; GO:1902476; P:chloride transmembrane transport; IBA:GO_Central.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; IDA:SynGO.
DR   CDD; cd19005; LGIC_ECD_GABAAR_rho; 1.
DR   CDD; cd19059; LGIC_TM_GABAAR_rho; 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; IPR008058; GABAAa_rho1_rcpt.
DR   InterPro; IPR008057; GABAAa_rho_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:SF30; GAMMA-AMINOBUTYRIC ACID RECEPTOR SUBUNIT RHO-1; 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; PR01670; GABAARRHO.
DR   PRINTS; PR01671; GABAARRHO1.
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; P56475; 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..480
FT                   /note="Gamma-aminobutyric acid receptor subunit rho-1"
FT                   /id="PRO_0000000486"
FT   TOPO_DOM        22..282
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        283..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        310..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        344..366
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        367..458
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        459..480
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   REGION          29..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..60
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        141
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        235
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        275
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        199..213
FT                   /evidence="ECO:0000250"
FT   CONFLICT        414
FT                   /note="M -> L (in Ref. 1; AAB81964)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   480 AA;  55488 MW;  BF071780C464FCCA CRC64;
     MLAVQNMKFG IFLLWWGWVL AAESTAHWPG REVHEPSRKG SRPQRQRRGA HDDAHKQGSP
     ILRRSSDITK SPLTKSEQLL RIDDHDFSMR PGFGGPAIPV GVDVQVESLD SISEVDMDFT
     MTLYLRHYWK DERLSFPSSN NLSMTFDGRL VKKIWVPDMF FVHSKRSFIH DTTTDNVMLR
     VQPDGKVLYS LRVTVTAMCN MDFSRFPLDT QTCSLEIESY AYTEDDLMLY WKKGNDSLKT
     DERISLSQFL IQEFHTTTKL AFYSSTGWYN RLYINFTLRR HIFFFLLQTY FPATLMVMLS
     WVSFWIDRRA VPARVPLGIT TVLTMSTIIT GVNASMPRVS YIKAVDIYLW VSFVFVFLSV
     LEYAAVNYLT TVQERKERKL REKISCTCGL PQPRGVMLDS SYSDGEVNDL GGYMPENGEK
     PDRMMVQLTL ASERGSPQRK GQRGSYVSMR INTHAIDKYS RIIFPAAYIL FNLIYWSIFS
//