GPR83_MOUSE
ID GPR83_MOUSE Reviewed; 423 AA.
AC P30731; Q542Q9; Q544C4;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=G-protein coupled receptor 83;
DE AltName: Full=Glucocorticoid-induced receptor {ECO:0000303|PubMed:1663214};
DE Flags: Precursor;
GN Name=Gpr83 {ECO:0000312|MGI:MGI:95712};
GN Synonyms=Gir {ECO:0000303|PubMed:1663214}, Gpr72,
GN Jp05 {ECO:0000303|PubMed:9675427};
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] (ISOFORMS 1; 2; 3 AND 4), AND INDUCTION.
RX PubMed=1663214; DOI=10.1210/mend-5-9-1331;
RA Harrigan M.T., Campbell N.F., Bourgeois S.;
RT "Identification of a gene induced by glucocorticoids in murine T-cells: a
RT potential G protein-coupled receptor.";
RL Mol. Endocrinol. 5:1331-1338(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Corpus striatum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=9675427; DOI=10.1016/s0169-328x(98)00099-0;
RA Pesini P., Detheux M., Parmentier M., Hoekfelt T.;
RT "Distribution of a glucocorticoid-induced orphan receptor (JP05) mRNA in
RT the central nervous system of the mouse.";
RL Brain Res. Mol. Brain Res. 57:281-300(1998).
RN [4]
RP SUBCELLULAR LOCATION, FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
RX PubMed=23744028; DOI=10.1038/ncomms2968;
RA Mueller T.D., Mueller A., Yi C.X., Habegger K.M., Meyer C.W., Gaylinn B.D.,
RA Finan B., Heppner K., Trivedi C., Bielohuby M., Abplanalp W., Meyer F.,
RA Piechowski C.L., Pratzka J., Stemmer K., Holland J., Hembree J.,
RA Bhardwaj N., Raver C., Ottaway N., Krishna R., Sah R., Sallee F.R.,
RA Woods S.C., Perez-Tilve D., Bidlingmaier M., Thorner M.O., Krude H.,
RA Smiley D., DiMarchi R., Hofmann S., Pfluger P.T., Kleinau G.,
RA Biebermann H., Tschoep M.H.;
RT "The orphan receptor Gpr83 regulates systemic energy metabolism via
RT ghrelin-dependent and ghrelin-independent mechanisms.";
RL Nat. Commun. 4:1968-1968(2013).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, LIGAND-BINDING, AND CAUTION.
RX PubMed=27117253; DOI=10.1126/scisignal.aad0694;
RA Gomes I., Bobeck E.N., Margolis E.B., Gupta A., Sierra S., Fakira A.K.,
RA Fujita W., Mueller T.D., Mueller A., Tschoep M.H., Kleinau G.,
RA Fricker L.D., Devi L.A.;
RT "Identification of GPR83 as the receptor for the neuroendocrine peptide
RT PEN.";
RL Sci. Signal. 9:ra43-ra43(2016).
RN [6]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=34512237; DOI=10.3389/fnins.2021.675769;
RA Fakira A.K., Lueptow L.M., Trimbake N.A., Devi L.A.;
RT "PEN Receptor GPR83 in Anxiety-Like Behaviors: Differential Regulation in
RT Global vs Amygdalar Knockdown.";
RL Front. Neurosci. 15:675769-675769(2021).
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
CC (PubMed:27117253). Plays a role in food intake and body weight
CC regulation (PubMed:23744028). May contribute to the regulation of
CC anxiety-related behaviors (PubMed:34512237).
CC {ECO:0000269|PubMed:23744028, ECO:0000269|PubMed:27117253,
CC ECO:0000269|PubMed:34512237}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27117253};
CC Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with GPR171
CC in the paraventricular nucleus (PubMed:27117253). Colocalizes with the
CC ghrelin receptor GHSR1A in the hypothalamus (PubMed:23744028).
CC {ECO:0000269|PubMed:23744028, ECO:0000269|PubMed:27117253}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=1;
CC IsoId=P30731-1; Sequence=Displayed;
CC Name=2; Synonyms=RP39;
CC IsoId=P30731-2; Sequence=VSP_001988;
CC Name=3; Synonyms=RP82;
CC IsoId=P30731-3; Sequence=VSP_001989;
CC Name=4; Synonyms=RP105;
CC IsoId=P30731-4; Sequence=VSP_001990;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the brain, with moderate
CC expression in the hypothalamus (PubMed:23744028). Expressed in the
CC thymus (PubMed:16141072). {ECO:0000269|PubMed:16141072,
CC ECO:0000269|PubMed:23744028}.
CC -!- INDUCTION: By glucocorticoids and cAMP in T-cells.
CC {ECO:0000269|PubMed:1663214}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice have normal body weight and
CC glucose tolerance when fed a regular chow diet, but are protected from
CC obesity and glucose intolerance when challenged with a high-fat diet
CC (PubMed:23744028). Knockdown of GPR83 has minimal impact on anxiety-
CC like behaviors in female mice and a decrease in anxiety-related
CC behaviors in male mice. In contrast, a local GPR83 knockdown in the
CC basolateral amygdala leads to more anxiety-related behaviors in female
CC mice (PubMed:34512237). {ECO:0000269|PubMed:23744028,
CC ECO:0000269|PubMed:34512237}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- CAUTION: 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 (PubMed:27117253).
CC {ECO:0000250|UniProtKB:Q8VHD7, ECO:0000269|PubMed:27117253}.
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DR EMBL; M80481; AAA17882.1; -; mRNA.
DR EMBL; AK081276; BAC38181.1; -; mRNA.
DR EMBL; AK041527; BAC30974.1; -; mRNA.
DR CCDS; CCDS22829.1; -. [P30731-1]
DR CCDS; CCDS80959.1; -. [P30731-2]
DR PIR; A40470; A40470.
DR PIR; B40470; B40470.
DR PIR; C40470; C40470.
DR PIR; D40470; D40470.
DR RefSeq; NP_001297663.1; NM_001310734.1.
DR RefSeq; NP_034417.1; NM_010287.3. [P30731-1]
DR RefSeq; XP_006510080.1; XM_006510017.2. [P30731-4]
DR AlphaFoldDB; P30731; -.
DR SMR; P30731; -.
DR STRING; 10090.ENSMUSP00000034408; -.
DR GuidetoPHARMACOLOGY; 119; -.
DR GlyGen; P30731; 3 sites.
DR PhosphoSitePlus; P30731; -.
DR PaxDb; P30731; -.
DR PRIDE; P30731; -.
DR ProteomicsDB; 271043; -. [P30731-1]
DR ProteomicsDB; 271044; -. [P30731-2]
DR ProteomicsDB; 271045; -. [P30731-3]
DR ProteomicsDB; 271046; -. [P30731-4]
DR Antibodypedia; 17864; 408 antibodies from 34 providers.
DR DNASU; 14608; -.
DR Ensembl; ENSMUST00000034408; ENSMUSP00000034408; ENSMUSG00000031932. [P30731-1]
DR Ensembl; ENSMUST00000115624; ENSMUSP00000111287; ENSMUSG00000031932. [P30731-2]
DR GeneID; 14608; -.
DR KEGG; mmu:14608; -.
DR UCSC; uc009off.1; mouse. [P30731-1]
DR CTD; 10888; -.
DR MGI; MGI:95712; Gpr83.
DR VEuPathDB; HostDB:ENSMUSG00000031932; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000154336; -.
DR HOGENOM; CLU_009579_6_1_1; -.
DR InParanoid; P30731; -.
DR OMA; SQTIHTN; -.
DR OrthoDB; 1254727at2759; -.
DR PhylomeDB; P30731; -.
DR TreeFam; TF315303; -.
DR Reactome; R-MMU-418555; G alpha (s) signalling events.
DR BioGRID-ORCS; 14608; 0 hits in 71 CRISPR screens.
DR PRO; PR:P30731; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P30731; protein.
DR Bgee; ENSMUSG00000031932; Expressed in olfactory tubercle and 86 other tissues.
DR ExpressionAtlas; P30731; baseline and differential.
DR Genevisible; P30731; MM.
DR GO; GO:0005929; C:cilium; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0097730; C:non-motile cilium; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IDA:UniProtKB.
DR GO; GO:0008188; F:neuropeptide receptor activity; IDA:UniProtKB.
DR GO; GO:0004983; F:neuropeptide Y receptor activity; IEA:InterPro.
DR GO; GO:0007631; P:feeding behavior; IMP:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IDA:UniProtKB.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0051384; P:response to glucocorticoid; IDA:MGI.
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 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Signal; Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..423
FT /note="G-protein coupled receptor 83"
FT /id="PRO_0000012804"
FT TOPO_DOM 18..71
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..107
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..129
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..145
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..167
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..186
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..208
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..238
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..260
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..293
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..315
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 316..327
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 349..423
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 389..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 144..224
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VAR_SEQ 130..171
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1663214"
FT /id="VSP_001988"
FT VAR_SEQ 171
FT /note="Q -> QGLTAIAVDRHQGLELQKMVRPRGDGGELRSPSVTFVPSSLCPALFT
FT CKRPWDFQESQSLHDTLFPPLE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:1663214"
FT /id="VSP_001989"
FT VAR_SEQ 171
FT /note="Q -> QRPWDFQESQSLHDTLFPPLE (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:1663214"
FT /id="VSP_001990"
SQ SEQUENCE 423 AA; 48137 MW; 3ACE43452BF15391 CRC64;
MKVPPVLLLF LLSSVRATEQ PQVVTEHPSM EAALTGPNAS SHFWANYTFS DWQNFVGRRR
YGAESQNPTV KALLIVAYSF TIVFSLFGNV LVCHVIFKNQ RMHSATSLFI VNLAVADIMI
TLLNTPFTLV RFVNSTWVFG KGMCHVSRFA QYCSLHVSAL TLTAIAVDRH QVIMHPLKPR
ISITKGVIYI AVIWVMATFF SLPHAICQKL FTFKYSEDIV RSLCLPDFPE PADLFWKYLD
LATFILLYLL PLFIISVAYA RVAKKLWLCN TIGDVTTEQY LALRRKKKTT VKMLVLVVVL
FALCWFPLNC YVLLLSSKAI HTNNALYFAF HWFAMSSTCY NPFIYCWLNE NFRVELKALL
SMCQRPPKPQ EDRLPSPVPS FRVAWTEKSH GRRAPLPNHH LPSSQIQSGK TDLSSVEPVV
AMS
