GBRR1_RAT
ID GBRR1_RAT Reviewed; 480 AA.
AC P50572;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 147.
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 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].
RC STRAIN=Sprague-Dawley;
RX PubMed=8524843; DOI=10.1073/pnas.92.25.11756;
RA Zhang D., Pan Z., Zhang X., Brideau A.D., Lipton S.A.;
RT "Cloning of a gamma-aminobutyric acid type C receptor subunit in rat retina
RT with a methionine residue critical for picrotoxinin channel block.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:11756-11760(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Retina;
RX PubMed=8905713; DOI=10.1097/00001756-199608120-00030;
RA Wegelius K., Reeben M., Saarma M.;
RT "The rho 1 GABA receptor cloned from rat retina is down-modulated by
RT protons.";
RL NeuroReport 7:2005-2009(1996).
RN [3]
RP INTERACTION WITH SQSTM1.
RX PubMed=12431995; DOI=10.1074/jbc.m205162200;
RA Croci C., Brandstaetter J.H., Enz R.;
RT "ZIP3, a new splice variant of the PKC-zeta-interacting protein family,
RT binds to GABAC receptors, PKC-zeta, and Kv beta 2.";
RL J. Biol. Chem. 278:6128-6135(2003).
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.
CC -!- SUBUNIT: Generally pentameric. There are five types of GABA(A) receptor
CC chains: alpha, beta, gamma, delta, and rho. Interacts with SQSTM1.
CC {ECO:0000269|PubMed:12431995}.
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. GABRR1 sub-
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA87730.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA64832.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U21070; AAA87730.1; ALT_INIT; mRNA.
DR EMBL; X95579; CAA64832.1; ALT_INIT; mRNA.
DR AlphaFoldDB; P50572; -.
DR SMR; P50572; -.
DR STRING; 10116.ENSRNOP00000010172; -.
DR GuidetoPHARMACOLOGY; 420; -.
DR GlyGen; P50572; 3 sites.
DR iPTMnet; P50572; -.
DR PhosphoSitePlus; P50572; -.
DR PaxDb; P50572; -.
DR Ensembl; ENSRNOT00000010172; ENSRNOP00000010172; ENSRNOG00000007603.
DR UCSC; RGD:61900; rat.
DR RGD; 61900; Gabrr1.
DR eggNOG; KOG3643; Eukaryota.
DR GeneTree; ENSGT00940000158591; -.
DR InParanoid; P50572; -.
DR PhylomeDB; P50572; -.
DR Reactome; R-RNO-977443; GABA receptor activation.
DR PRO; PR:P50572; -.
DR Proteomes; UP000002494; Chromosome 5.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0016917; F:GABA receptor activity; IDA:RGD.
DR GO; GO:0004890; F:GABA-A receptor activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0099507; F:ligand-gated ion channel activity involved in regulation of presynaptic membrane potential; ISO:RGD.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; ISO:RGD.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:1902476; P:chloride transmembrane transport; 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:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0007601; P:visual perception; NAS:RGD.
DR Gene3D; 1.20.58.390; -; 1.
DR Gene3D; 2.70.170.10; -; 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 PANTHER; PTHR18945; PTHR18945; 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; 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; 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_0000000487"
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 31..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..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"
SQ SEQUENCE 480 AA; 55532 MW; 18998C6C86CDC93C CRC64;
MLAVRNMKFG IFLLWWGWVL AAESTVHWPG REVHEPSKKG SRPQRQRRGA HDDAHKQGSP
ILKRSSDITK SPLTKSEQLL RIDDHDFSMR PGFGGPAIPV GVDVQVESLD SISEVDMDFT
MTLYLRHYWK DERLSFPSTN 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 SQRGSYVSMR INTHAIDKYS RIIFPAAYIL FNLIYWSIFS
