GPR83_CANLF
ID GPR83_CANLF Reviewed; 422 AA.
AC Q9TTQ9;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=G-protein coupled receptor 83;
DE AltName: Full=Glucocorticoid-induced receptor;
DE Flags: Precursor;
GN Name=GPR83; Synonyms=GIR;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Thyroid;
RA Perret J., Simons M., De Moerlooze L., Parmentier M.;
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: G-protein coupled receptor for PEN, a neuropeptide produced
CC from the precursor protein, proSAAS (encoded by PCSK1N). Acts through a
CC G(i)- and G(q)-alpha-alpha-mediated pathway in response to PEN. Plays a
CC role in food intake and body weight regulation. May contribute to the
CC regulation of anxiety-related behaviors.
CC {ECO:0000250|UniProtKB:P30731}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P30731};
CC Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with GPR171
CC in the paraventricular nucleus. Colocalizes with the ghrelin receptor
CC GHSR1A in the hypothalamus. {ECO:0000250|UniProtKB:P30731}.
CC -!- MISCELLANEOUS: NPY has been reported to be a ligand for GPR83 (By
CC similarity). However, a more recent study found that radiolabeled PEN
CC binding to GPR83 is not affected by NPY concentrations below 1 mM, only
CC very high, non-physiological concentrations causes a partial,
CC displacement of PEN binding (By similarity).
CC {ECO:0000250|UniProtKB:P30731, ECO:0000250|UniProtKB:Q8VHD7}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; Y19224; CAB57795.1; -; mRNA.
DR RefSeq; NP_001003108.1; NM_001003108.1.
DR AlphaFoldDB; Q9TTQ9; -.
DR SMR; Q9TTQ9; -.
DR STRING; 9612.ENSCAFP00000039807; -.
DR PaxDb; Q9TTQ9; -.
DR Ensembl; ENSCAFT00030031874; ENSCAFP00030027796; ENSCAFG00030017283.
DR GeneID; 403699; -.
DR KEGG; cfa:403699; -.
DR CTD; 10888; -.
DR eggNOG; KOG3656; Eukaryota.
DR HOGENOM; CLU_009579_6_1_1; -.
DR InParanoid; Q9TTQ9; -.
DR OMA; SQTIHTN; -.
DR OrthoDB; 1254727at2759; -.
DR TreeFam; TF315303; -.
DR Reactome; R-CFA-418555; G alpha (s) signalling events.
DR Proteomes; UP000002254; Unplaced.
DR Bgee; ENSCAFG00000031257; Expressed in prefrontal cortex and 36 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0097730; C:non-motile cilium; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISS:UniProtKB.
DR GO; GO:0008188; F:neuropeptide receptor activity; ISS:UniProtKB.
DR GO; GO:0004983; F:neuropeptide Y receptor activity; IEA:InterPro.
DR GO; GO:0007631; P:feeding behavior; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007218; P:neuropeptide signaling pathway; ISS:UniProtKB.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR000611; NPY_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01012; NRPEPTIDEYR.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; G-protein coupled receptor; Glycoprotein; Membrane;
KW Receptor; Reference proteome; Signal; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..422
FT /note="G-protein coupled receptor 83"
FT /id="PRO_0000012802"
FT TOPO_DOM 17..70
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..106
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..128
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..144
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..166
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..185
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..207
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..237
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..259
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..292
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..314
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..326
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 348..422
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 422 AA; 48043 MW; C9C21DE85B9DFB67 CRC64;
MGRRGALLCL LPLLRAAERP EGRADEPGLE AALAGPNASH FFWSNYSFSD WQNFVGRRRY
GAESQNPTVK ALLVVAYSFI IVFSLFGNVL VCHVIFKNQR MRSATSLFIV NLAVADILIT
LLNTPFTLVR FVNSTWVFGK GMCHVSRFAQ YCSLHVSALT LTAIAVDRHQ VIMHPLKPRI
SITKGVIYIT VIWTMATFFS LPHAICQKLF TFKYSEDIVR SLCLPDFPEP ADLFWKYLDL
ATFILLYILP LLIISVAYAR VAKKLWLCNT IGDVTTEQYL ALRRKKKKTI KMLMLVVVLF
ALCWFPLNCY VLLLSSKVIH TNNALYFAFH WFAMSSTCYN PFIYCWLNEN FRIELKALLS
MCQRLPKPQE ERPPSPVPSF RVAWTEKSNG RRVPPANNLL LSSHLHSGKT DLSSVEPIVA
MS
