GPR39_MOUSE
ID GPR39_MOUSE Reviewed; 456 AA.
AC Q5U431; Q80UC7;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=G-protein coupled receptor 39;
GN Name=Gpr39;
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 [LARGE SCALE MRNA].
RC STRAIN=C3H/He; TISSUE=Mesenchymal stem cell;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 10-164.
RX PubMed=12679517; DOI=10.1073/pnas.0230374100;
RA Vassilatis D.K., Hohmann J.G., Zeng H., Li F., Ranchalis J.E.,
RA Mortrud M.T., Brown A., Rodriguez S.S., Weller J.R., Wright A.C.,
RA Bergmann J.E., Gaitanaris G.A.;
RT "The G protein-coupled receptor repertoires of human and mouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:4903-4908(2003).
RN [3]
RP TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=17030183; DOI=10.1053/j.gastro.2006.07.009;
RA Moechars D., Depoortere I., Moreaux B., de Smet B., Goris I., Hoskens L.,
RA Daneels G., Kass S., Ver Donck L., Peeters T., Coulie B.;
RT "Altered gastrointestinal and metabolic function in the GPR39-obestatin
RT receptor-knockout mouse.";
RL Gastroenterology 131:1131-1141(2006).
RN [4]
RP TISSUE SPECIFICITY, AND PRELIMINARY FUNCTION.
RX PubMed=16959833; DOI=10.1210/en.2006-0933;
RA Holst B., Egerod K.L., Schild E., Vickers S.P., Cheetham S., Gerlach L.O.,
RA Storjohann L., Stidsen C.E., Jones R., Beck-Sickinger A.G., Schwartz T.W.;
RT "GPR39 signaling is stimulated by zinc ions but not by obestatin.";
RL Endocrinology 148:13-20(2007).
RN [5]
RP FUNCTION.
RX PubMed=18180304; DOI=10.1074/jbc.m704323200;
RA Dittmer S., Sahin M., Pantlen A., Saxena A., Toutzaris D., Pina A.L.,
RA Geerts A., Golz S., Methner A.;
RT "The constitutively active orphan G-protein-coupled receptor GPR39 protects
RT from cell death by increasing secretion of pigment epithelium-derived
RT growth factor.";
RL J. Biol. Chem. 283:7074-7081(2008).
CC -!- FUNCTION: Zn(2+) acts as an agonist (By similarity). This receptor
CC mediates its action by association with G proteins that activate a
CC phosphatidylinositol-calcium second messenger system. Its effect is
CC mediated mainly through G(q)-alpha and G(12)/G(13) proteins. Involved
CC in regulation of body weight, gastrointestinal mobility, hormone
CC secretion and cell death. {ECO:0000250, ECO:0000269|PubMed:17030183,
CC ECO:0000269|PubMed:18180304}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expression is detected in septumamygdala, parietal
CC cells, enterocytes, neurons and pancreas, in peripheral organs such as
CC the duodenum and kidney but not in the pituitary and hypothalamus.
CC {ECO:0000269|PubMed:16959833, ECO:0000269|PubMed:17030183}.
CC -!- MISCELLANEOUS: Was originally reported to be the receptor of obestatin.
CC However, numerous reports concluded that GPR39 was not the receptor for
CC obestatin (PubMed:16959833). {ECO:0000305|PubMed:16959833}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; BC085285; AAH85285.1; -; mRNA.
DR EMBL; AY255549; AAO85061.1; -; mRNA.
DR CCDS; CCDS48344.1; -.
DR AlphaFoldDB; Q5U431; -.
DR SMR; Q5U431; -.
DR STRING; 10090.ENSMUSP00000027581; -.
DR BindingDB; Q5U431; -.
DR ChEMBL; CHEMBL3341584; -.
DR GlyGen; Q5U431; 2 sites.
DR iPTMnet; Q5U431; -.
DR PhosphoSitePlus; Q5U431; -.
DR MaxQB; Q5U431; -.
DR PaxDb; Q5U431; -.
DR PRIDE; Q5U431; -.
DR ProteomicsDB; 271273; -.
DR UCSC; uc007ckh.2; mouse.
DR MGI; MGI:1918361; Gpr39.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q5U431; -.
DR PhylomeDB; Q5U431; -.
DR Reactome; R-MMU-373076; Class A/1 (Rhodopsin-like receptors).
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR Reactome; R-MMU-418555; G alpha (s) signalling events.
DR ChiTaRS; Gpr39; mouse.
DR PRO; PR:Q5U431; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q5U431; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IMP:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008343; P:adult feeding behavior; IMP:MGI.
DR GO; GO:0071294; P:cellular response to zinc ion; IMP:MGI.
DR GO; GO:0042632; P:cholesterol homeostasis; IMP:MGI.
DR GO; GO:0002024; P:diet induced thermogenesis; IMP:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0001696; P:gastric acid secretion; IMP:MGI.
DR GO; GO:0035483; P:gastric emptying; IMP:MGI.
DR GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR GO; GO:0030073; P:insulin secretion; IMP:MGI.
DR GO; GO:0035773; P:insulin secretion involved in cellular response to glucose stimulus; IMP:MGI.
DR GO; GO:0060455; P:negative regulation of gastric acid secretion; IMP:MGI.
DR GO; GO:0070050; P:neuron cellular homeostasis; IMP:MGI.
DR GO; GO:0032024; P:positive regulation of insulin secretion; IMP:MGI.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:MGI.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IMP:MGI.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IMP:MGI.
DR GO; GO:0030641; P:regulation of cellular pH; IMP:MGI.
DR GO; GO:0019216; P:regulation of lipid metabolic process; IMP:MGI.
DR GO; GO:0042391; P:regulation of membrane potential; IMP:MGI.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IMP:MGI.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
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; Glycoprotein;
KW Membrane; Metal-binding; Phosphoprotein; Receptor; Reference proteome;
KW Transducer; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..456
FT /note="G-protein coupled receptor 39"
FT /id="PRO_0000069566"
FT TOPO_DOM 1..34
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TRANSMEM 35..55
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TOPO_DOM 56..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TRANSMEM 70..89
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TOPO_DOM 90..109
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TRANSMEM 110..131
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TOPO_DOM 132..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TRANSMEM 152..172
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TOPO_DOM 173..217
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TRANSMEM 218..242
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TOPO_DOM 243..283
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TRANSMEM 284..305
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TOPO_DOM 306..323
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TRANSMEM 324..344
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TOPO_DOM 345..456
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT REGION 415..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 17
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O43194"
FT BINDING 19
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O43194"
FT MOD_RES 397
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43194"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 11..191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 108..210
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 456 AA; 51589 MW; EDF5DFB455D0A5CA CRC64;
MASSSGSNHI CSRVIDHSHV PEFEVATWIK ITLILVYLII FVVGILGNSV TIRVTQVLQK
KGYLQKEVTD HMVSLACSDI LVFLIGMPME FYSIIWNPLT TPSYALSCKL HTFLFETCSY
ATLLHVLTLS FERYIAICHP FKYKAVSGPR QVKLLIGFVW VTSALVALPL LFAMGIEYPL
VNVPTHKGLN CNLSRTRHHD EPGNSNMSIC TNLSNRWEVF QSSIFGAFAV YLVVLASVAF
MCWNMMKVLM KSKQGTLAGT GPQLQLRKSE SEESRTARRQ TIIFLRLIVV TLAVCWMPNQ
IRRIMAAAKP KHDWTRTYFR AYMILLPFSD TFFYLSSVVN PLLYNVSSQQ FRKVFWQVLC
CRLTLQHANQ EKRQRARFIS TKDSTSSARS PLIFLASRRS NSSSRRTNKV FLSTFQTEAK
PGEAKPQPLS PESPQTGSET KPAGSTTENS LQEQEV
