GBRR3_RAT
ID GBRR3_RAT Reviewed; 464 AA.
AC P50573;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Gamma-aminobutyric acid receptor subunit rho-3;
DE AltName: Full=GABA(A) receptor subunit rho-3;
DE AltName: Full=GABA(C) receptor;
DE Flags: Precursor;
GN Name=Gabrr3;
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; TISSUE=Retina;
RX PubMed=8605242; DOI=10.1016/0167-4781(95)00205-7;
RA Ogurusu T., Shingai R.;
RT "Cloning of a putative gamma-aminobutyric acid (GABA) receptor subunit rho
RT 3 cDNA.";
RL Biochim. Biophys. Acta 1305:15-18(1996).
RN [2]
RP INTERACTION WITH SQSTM1 AND PRKCZ, AND DOMAIN.
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 -!- SUBUNIT: Generally pentameric. There are five types of GABA(A) receptor
CC chains: alpha, beta, gamma, delta, and rho. Forms a ternary complex
CC with SQSTM1 and PRKCZ.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC protein. Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Retina.
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. GABRR3 sub-
CC subfamily. {ECO:0000305}.
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 EMBL; D50671; BAA09322.1; -; mRNA.
DR PIR; S65756; S65756.
DR RefSeq; NP_620252.1; NM_138897.1.
DR AlphaFoldDB; P50573; -.
DR SMR; P50573; -.
DR BioGRID; 251384; 1.
DR CORUM; P50573; -.
DR STRING; 10116.ENSRNOP00000002281; -.
DR GlyGen; P50573; 2 sites.
DR PhosphoSitePlus; P50573; -.
DR PaxDb; P50573; -.
DR Ensembl; ENSRNOT00000002281; ENSRNOP00000002281; ENSRNOG00000001679.
DR GeneID; 192258; -.
DR KEGG; rno:192258; -.
DR UCSC; RGD:621564; rat.
DR CTD; 200959; -.
DR RGD; 621564; Gabrr3.
DR eggNOG; KOG3643; Eukaryota.
DR GeneTree; ENSGT00940000159906; -.
DR HOGENOM; CLU_010920_0_1_1; -.
DR InParanoid; P50573; -.
DR OMA; STKVWPL; -.
DR OrthoDB; 480926at2759; -.
DR PhylomeDB; P50573; -.
DR TreeFam; TF315453; -.
DR Reactome; R-RNO-977443; GABA receptor activation.
DR PRO; PR:P50573; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000001679; Expressed in ovary and 3 other tissues.
DR Genevisible; P50573; RN.
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: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:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
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 Gene3D; 1.20.58.390; -; 1.
DR Gene3D; 2.70.170.10; -; 1.
DR InterPro; IPR006028; GABAA/Glycine_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; 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..464
FT /note="Gamma-aminobutyric acid receptor subunit rho-3"
FT /id="PRO_0000000491"
FT TOPO_DOM 22..264
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 265..288
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TRANSMEM 292..314
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TRANSMEM 326..348
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 349..442
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 443..464
FT /note="Helical"
FT /evidence="ECO:0000305"
FT REGION 344..445
FT /note="Interaction with SQSTM1"
FT /evidence="ECO:0000269|PubMed:12431995"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 181..195
FT /evidence="ECO:0000250"
SQ SEQUENCE 464 AA; 54031 MW; FC86BE7E8DA5ACE2 CRC64;
MVLAFWLAFF TYTWITLMLD ASAVKEPHQQ CLSSPKQTRI RETRMRKDDL TKVWPLKREQ
LLHIEDHDFS TRPGFGGSPV PVGIDVQVES IDSISEVNMD FTMTFYLRHY WKDERLSFPS
TTNKSMTFDR RLIQKIWVPD IFFVHSKRSF IHDTTVENIM LRVHPDGNVL FSLRITVSAM
CFMDFSRFPL DTQNCSLELE SYAYNEEDLM LYWKHGNKSL NTEEHISLSQ FFIEEFSASS
GLAFYSSTGW YYRLFINFVL RRHIFFFVLQ TYFPAMLMVM LSWVSFWIDR RAVPARVSLG
ITTVLTMSTI VTGVSASMPQ VSYVKAVDVY MWVSSLFVFL SVIEYAAVNY LTTVEEWKQL
NRRGKISGMY NIDAVQAMAF DGCYHDGETD VDQTSFFLHS EEDSMRTKFT GSPCADSSQI
KRKSLGGNVG RIILENNHVI DTYSRIVFPV VYIIFNLFYW GIYV
