GPR83_RAT
ID GPR83_RAT Reviewed; 422 AA.
AC Q8VHD7;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=G-protein coupled receptor 83;
DE AltName: Full=Glucocorticoid-induced receptor {ECO:0000303|PubMed:11698613};
DE Flags: Precursor;
GN Name=Gpr83 {ECO:0000312|RGD:619891};
GN Synonyms=Gir {ECO:0000303|PubMed:17240481};
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], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=Sprague-Dawley;
RX PubMed=11698613; DOI=10.1523/jneurosci.21-22-09027.2001;
RA Wang D., Herman J.P., Pritchard L.M., Spitzer R.H., Ahlbrand R.L.,
RA Kramer G.L., Petty F., Sallee F.R., Richtand N.M.;
RT "Cloning, expression, and regulation of a glucocorticoid-induced receptor
RT in rat brain: effect of repetitive amphetamine.";
RL J. Neurosci. 21:9027-9035(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP CAUTION.
RX PubMed=17240481; DOI=10.1016/j.peptides.2006.11.013;
RA Sah R., Parker S.L., Sheriff S., Eaton K., Balasubramaniam A., Sallee F.R.;
RT "Interaction of NPY compounds with the rat glucocorticoid-induced receptor
RT (GIR) reveals similarity to the NPY-Y2 receptor.";
RL Peptides 28:302-309(2007).
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 -!- TISSUE SPECIFICITY: Expressed preferentially in brain, and its neuronal
CC expression is relegated to limbic brain regions, particularly in
CC forebrain. {ECO:0000269|PubMed:11698613}.
CC -!- INDUCTION: Increased in the prefrontal cortex of rat chronically
CC treated with amphetamines. {ECO:0000269|PubMed:11698613}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|RuleBase:RU000688}.
CC -!- CAUTION: NPY has been reported to be a ligand for GPR83
CC (PubMed:17240481). However, a more recent study found that radiolabeled
CC PEN binding to GPR83 is not affected by NPY concentrations below 1 mM,
CC only very high, non-physiological concentrations causes a partial,
CC displacement of PEN binding (By similarity).
CC {ECO:0000250|UniProtKB:P30731, ECO:0000269|PubMed:17240481}.
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DR EMBL; AY029071; AAK29999.1; -; mRNA.
DR EMBL; AC097778; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473993; EDL78460.1; -; Genomic_DNA.
DR RefSeq; NP_536336.1; NM_080411.1.
DR AlphaFoldDB; Q8VHD7; -.
DR SMR; Q8VHD7; -.
DR STRING; 10116.ENSRNOP00000043707; -.
DR PaxDb; Q8VHD7; -.
DR Ensembl; ENSRNOT00000044945; ENSRNOP00000043707; ENSRNOG00000030318.
DR GeneID; 140595; -.
DR KEGG; rno:140595; -.
DR UCSC; RGD:619891; rat.
DR CTD; 10888; -.
DR RGD; 619891; Gpr83.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000154336; -.
DR HOGENOM; CLU_009579_6_1_1; -.
DR InParanoid; Q8VHD7; -.
DR OMA; SQTIHTN; -.
DR OrthoDB; 1254727at2759; -.
DR PhylomeDB; Q8VHD7; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Proteomes; UP000234681; Chromosome 8.
DR Bgee; ENSRNOG00000030318; Expressed in frontal cortex and 5 other tissues.
DR GO; GO:0005929; C:cilium; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0097730; C:non-motile cilium; ISO:RGD.
DR GO; GO:0008188; F:neuropeptide receptor activity; IBA:GO_Central.
DR GO; GO:0004983; F:neuropeptide Y receptor activity; IEA:InterPro.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR GO; GO:0051384; P:response to glucocorticoid; ISO:RGD.
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; Disulfide bond; G-protein coupled receptor; Membrane;
KW Receptor; Reference proteome; Signal; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..422
FT /note="G-protein coupled receptor 83"
FT /evidence="ECO:0000255"
FT /id="PRO_5014107612"
FT TOPO_DOM 18..70
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 71..91
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..106
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 107..127
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..143
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 144..166
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..184
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 185..205
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..236
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 237..257
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..292
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 293..313
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 314..326
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 327..347
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 348..422
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 401..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 143..223
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 422 AA; 47957 MW; 4917CA9C33A8BFE9 CRC64;
MNVPPVLLLF LLSSVRATEQ PQVVTEHPSM DAALTGANAS HFWANYTFSD WQNFVGRRRY
GAESQNPTVK ALLIVAYSFI IVFSLFGNVL VCHVIFKNQR MHSATSLFIV NLAVADIMIT
LLNTPFTLVR FVNSTWVFGK GMCHVSRFAQ YCSLHVSALT LTAIAVDRHQ VIMHPLKPRI
SITKGVIYIA VIWVMATFFS LPHAICQKLF TFKYSEDIVR SLCLPDFPEP ADLFWKYLDL
ATFILLYLLP LFIISVAYAR VAKKLWLCNT IGDVTTEQYL ALRRKKKTTV KMLVLVVVLF
ALCWFPLNCY VLLLSSKAIH TNNALYFAFH WFAMSSTCYN PFIYCWLNEN FRVELKALLS
MCQRPSKPQE DRLPSPVPSF RVAWTEKSHG RRALLANHHL PSSQIQSGKT DLSSVEPTVA
VS
