GPR83_HUMAN
ID GPR83_HUMAN Reviewed; 423 AA.
AC Q9NYM4; B0M0K5; F5GZ43; Q6NWR4; Q9P1Y8;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=G-protein coupled receptor 83;
DE AltName: Full=G-protein coupled receptor 72;
DE Flags: Precursor;
GN Name=GPR83 {ECO:0000312|HGNC:HGNC:4523};
GN Synonyms=GPR72 {ECO:0000303|PubMed:10760605},
GN JP05 {ECO:0000303|PubMed:11720708}, KIAA1540 {ECO:0000303|PubMed:10819331};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLN-374.
RX PubMed=10760605; DOI=10.1016/s0167-4781(00)00023-3;
RA Parker R., Liu M., Eyre H.J., Copeland N.G., Gilbert D.J., Crawford J.,
RA Sutherland G.R., Jenkins N.A., Herzog H.;
RT "Y-receptor-like genes GPR72 and GPR73: molecular cloning, genomic
RT organisation and assignment to human chromosome 11q21.1 and 2p14 and mouse
RT chromosome 9 and 6.";
RL Biochim. Biophys. Acta 1491:369-375(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-374.
RC TISSUE=Brain;
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLN-374.
RC TISSUE=Brain;
RA Kaighin V.A., Martin A.L., Aronstam R.S.;
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=11720708; DOI=10.1016/s0006-8993(01)03068-2;
RA Brezillon S., Detheux M., Parmentier M., Hoekfelt T., Hurd Y.L.;
RT "Distribution of an orphan G-protein coupled receptor (JP05) mRNA in the
RT human brain.";
RL Brain Res. 921:21-30(2001).
RN [9]
RP FUNCTION, AND LIGAND-BINDING.
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).
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. May contribute to the regulation of anxiety-related
CC behaviors (By similarity). {ECO:0000250|UniProtKB:P30731,
CC ECO:0000269|PubMed:27117253}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NYM4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NYM4-2; Sequence=VSP_061501;
CC -!- TISSUE SPECIFICITY: Highly expressed in the brain and spinal cord, and
CC found in lower concentrations in the thymus and other tissues.
CC {ECO:0000269|PubMed:11720708}.
CC -!- MISCELLANEOUS: NPY has been reported to be a ligand for GPR83 (in
CC vitro) (By similarity). However, a more recent study found that
CC radiolabeled PEN binding to GPR83 is not affected by NPY concentrations
CC below 1 mM, only very high, non-physiological concentrations causes a
CC partial, 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA96064.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF236081; AAF43705.1; -; mRNA.
DR EMBL; AB040973; BAA96064.1; ALT_INIT; mRNA.
DR EMBL; AK315161; BAG37605.1; -; mRNA.
DR EMBL; EU432120; ABY87919.1; -; mRNA.
DR EMBL; AP000765; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC067473; AAH67473.1; -; mRNA.
DR EMBL; CH471065; EAW66929.1; -; Genomic_DNA.
DR CCDS; CCDS8297.1; -. [Q9NYM4-1]
DR RefSeq; NP_001317274.1; NM_001330345.1.
DR RefSeq; NP_057624.3; NM_016540.3.
DR AlphaFoldDB; Q9NYM4; -.
DR SMR; Q9NYM4; -.
DR BioGRID; 116095; 2.
DR STRING; 9606.ENSP00000243673; -.
DR ChEMBL; CHEMBL4523924; -.
DR GlyGen; Q9NYM4; 3 sites.
DR iPTMnet; Q9NYM4; -.
DR PhosphoSitePlus; Q9NYM4; -.
DR BioMuta; GPR83; -.
DR DMDM; 212276435; -.
DR PaxDb; Q9NYM4; -.
DR PeptideAtlas; Q9NYM4; -.
DR PRIDE; Q9NYM4; -.
DR Antibodypedia; 17864; 408 antibodies from 34 providers.
DR DNASU; 10888; -.
DR Ensembl; ENST00000243673.7; ENSP00000243673.2; ENSG00000123901.9. [Q9NYM4-1]
DR Ensembl; ENST00000539203.2; ENSP00000441550.1; ENSG00000123901.9. [Q9NYM4-2]
DR GeneID; 10888; -.
DR KEGG; hsa:10888; -.
DR MANE-Select; ENST00000243673.7; ENSP00000243673.2; NM_016540.4; NP_057624.3.
DR UCSC; uc001pet.2; human. [Q9NYM4-1]
DR CTD; 10888; -.
DR DisGeNET; 10888; -.
DR GeneCards; GPR83; -.
DR HGNC; HGNC:4523; GPR83.
DR HPA; ENSG00000123901; Group enriched (brain, thyroid gland).
DR MIM; 605569; gene.
DR neXtProt; NX_Q9NYM4; -.
DR OpenTargets; ENSG00000123901; -.
DR PharmGKB; PA28927; -.
DR VEuPathDB; HostDB:ENSG00000123901; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000154336; -.
DR HOGENOM; CLU_009579_6_1_1; -.
DR InParanoid; Q9NYM4; -.
DR OMA; SQTIHTN; -.
DR OrthoDB; 1254727at2759; -.
DR PhylomeDB; Q9NYM4; -.
DR TreeFam; TF315303; -.
DR PathwayCommons; Q9NYM4; -.
DR Reactome; R-HSA-418555; G alpha (s) signalling events.
DR Reactome; R-HSA-9660821; ADORA2B mediated anti-inflammatory cytokines production.
DR BioGRID-ORCS; 10888; 10 hits in 1065 CRISPR screens.
DR GeneWiki; GPR83; -.
DR GenomeRNAi; 10888; -.
DR Pharos; Q9NYM4; Tchem.
DR PRO; PR:Q9NYM4; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9NYM4; protein.
DR Bgee; ENSG00000123901; Expressed in cerebellar vermis and 84 other tissues.
DR ExpressionAtlas; Q9NYM4; baseline and differential.
DR Genevisible; Q9NYM4; HS.
DR GO; GO:0005929; C:cilium; IDA:MGI.
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 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..16
FT /evidence="ECO:0000255"
FT CHAIN 17..423
FT /note="G-protein coupled receptor 83"
FT /id="PRO_0000012803"
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 402..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 37
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 131..172
FT /note="Missing (in isoform 2)"
FT /id="VSP_061501"
FT VARIANT 374
FT /note="P -> Q (in dbSNP:rs3740868)"
FT /evidence="ECO:0000269|PubMed:10760605,
FT ECO:0000269|PubMed:10819331, ECO:0000269|Ref.6"
FT /id="VAR_047079"
FT CONFLICT 373
FT /note="R -> G (in Ref. 1; AAF43705)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 423 AA; 48339 MW; D9E2D96ADC1B44AA CRC64;
MVPHLLLLCL LPLVRATEPH EGRADEQSAE AALAVPNASH FFSWNNYTFS DWQNFVGRRR
YGAESQNPTV KALLIVAYSF IIVFSLFGNV LVCHVIFKNQ RMHSATSLFI VNLAVADIMI
TLLNTPFTLV RFVNSTWIFG KGMCHVSRFA QYCSLHVSAL TLTAIAVDRH QVIMHPLKPR
ISITKGVIYI AVIWTMATFF SLPHAICQKL FTFKYSEDIV RSLCLPDFPE PADLFWKYLD
LATFILLYIL PLLIISVAYA RVAKKLWLCN MIGDVTTEQY FALRRKKKKT IKMLMLVVVL
FALCWFPLNC YVLLLSSKVI RTNNALYFAF HWFAMSSTCY NPFIYCWLNE NFRIELKALL
SMCQRPPKPQ EDRPPSPVPS FRVAWTEKND GQRAPLANNL LPTSQLQSGK TDLSSVEPIV
TMS
