GHSR_MOUSE
ID GHSR_MOUSE Reviewed; 364 AA.
AC Q99P50; Q8BWX8; Q91Z82;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 3.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Growth hormone secretagogue receptor type 1;
DE Short=GHS-R;
DE AltName: Full=GH-releasing peptide receptor;
DE Short=GHRP;
DE AltName: Full=Ghrelin receptor;
GN Name=Ghsr;
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=C57BL/6J; TISSUE=Spinal cord;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-183.
RC STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RA Kacsoh B.;
RT "Cloning of mouse ghrelin/growth hormone secretagogue receptor cDNA by
RT rapid amplification of cDNA ends (RACE).";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 73-257.
RC STRAIN=129S1/SvImJ;
RA Peng X., Frohman L.A., Kineman R.D.;
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor for ghrelin, coupled to G-alpha-11 proteins.
CC Stimulates growth hormone secretion. Binds also other growth hormone
CC releasing peptides (GHRP) (e.g. Met-enkephalin and GHRP-6) as well as
CC non-peptide, low molecular weight secretagogues (e.g. L-692,429, MK-
CC 0677, adenosine) (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AK049671; BAC33866.1; -; mRNA.
DR EMBL; AY056474; AAL13336.1; -; mRNA.
DR EMBL; AF332997; AAG61141.1; -; mRNA.
DR CCDS; CCDS17273.1; -.
DR RefSeq; NP_796304.1; NM_177330.4.
DR AlphaFoldDB; Q99P50; -.
DR SMR; Q99P50; -.
DR STRING; 10090.ENSMUSP00000061153; -.
DR ChEMBL; CHEMBL3428; -.
DR GuidetoPHARMACOLOGY; 246; -.
DR GlyGen; Q99P50; 3 sites.
DR PaxDb; Q99P50; -.
DR PRIDE; Q99P50; -.
DR Antibodypedia; 3248; 296 antibodies from 32 providers.
DR DNASU; 208188; -.
DR Ensembl; ENSMUST00000057186; ENSMUSP00000061153; ENSMUSG00000051136.
DR GeneID; 208188; -.
DR KEGG; mmu:208188; -.
DR UCSC; uc008oto.1; mouse.
DR CTD; 2693; -.
DR MGI; MGI:2441906; Ghsr.
DR VEuPathDB; HostDB:ENSMUSG00000051136; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244813; -.
DR HOGENOM; CLU_009579_6_5_1; -.
DR InParanoid; Q99P50; -.
DR OMA; MVWTSSI; -.
DR OrthoDB; 890529at2759; -.
DR PhylomeDB; Q99P50; -.
DR TreeFam; TF332184; -.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR BioGRID-ORCS; 208188; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q99P50; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q99P50; protein.
DR Bgee; ENSMUSG00000051136; Expressed in median eminence of neurohypophysis and 13 other tissues.
DR ExpressionAtlas; Q99P50; baseline and differential.
DR Genevisible; Q99P50; MM.
DR GO; GO:0009986; C:cell surface; ISS:HGNC-UCL.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0099699; C:integral component of synaptic membrane; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:MGI.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISS:UniProtKB.
DR GO; GO:0001616; F:growth hormone secretagogue receptor activity; ISS:HGNC-UCL.
DR GO; GO:0016520; F:growth hormone-releasing hormone receptor activity; ISS:HGNC-UCL.
DR GO; GO:0042562; F:hormone binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0017046; F:peptide hormone binding; ISO:MGI.
DR GO; GO:0008154; P:actin polymerization or depolymerization; ISS:UniProtKB.
DR GO; GO:0008343; P:adult feeding behavior; IMP:HGNC-UCL.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IDA:MGI.
DR GO; GO:1990314; P:cellular response to insulin-like growth factor stimulus; IEA:Ensembl.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0097067; P:cellular response to thyroid hormone stimulus; IEA:Ensembl.
DR GO; GO:0046697; P:decidualization; ISS:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:HGNC-UCL.
DR GO; GO:0036321; P:ghrelin secretion; ISO:MGI.
DR GO; GO:0030252; P:growth hormone secretion; IGI:MGI.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; ISS:HGNC-UCL.
DR GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; IMP:MGI.
DR GO; GO:0007611; P:learning or memory; ISO:MGI.
DR GO; GO:0032099; P:negative regulation of appetite; ISO:MGI.
DR GO; GO:0050728; P:negative regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:0046676; P:negative regulation of insulin secretion; ISO:MGI.
DR GO; GO:0032691; P:negative regulation of interleukin-1 beta production; ISS:UniProtKB.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; ISS:UniProtKB.
DR GO; GO:0090327; P:negative regulation of locomotion involved in locomotory behavior; ISO:MGI.
DR GO; GO:2000110; P:negative regulation of macrophage apoptotic process; ISO:MGI.
DR GO; GO:0010700; P:negative regulation of norepinephrine secretion; ISO:MGI.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISS:UniProtKB.
DR GO; GO:0032100; P:positive regulation of appetite; IMP:HGNC-UCL.
DR GO; GO:1904000; P:positive regulation of eating behavior; ISO:MGI.
DR GO; GO:0045923; P:positive regulation of fatty acid metabolic process; ISO:MGI.
DR GO; GO:0045927; P:positive regulation of growth; ISO:MGI.
DR GO; GO:0043568; P:positive regulation of insulin-like growth factor receptor signaling pathway; IMP:MGI.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; ISS:HGNC-UCL.
DR GO; GO:0120058; P:positive regulation of small intestinal transit; ISO:MGI.
DR GO; GO:1904349; P:positive regulation of small intestine smooth muscle contraction; ISO:MGI.
DR GO; GO:1903672; P:positive regulation of sprouting angiogenesis; ISO:MGI.
DR GO; GO:1905564; P:positive regulation of vascular endothelial cell proliferation; ISO:MGI.
DR GO; GO:0099170; P:postsynaptic modulation of chemical synaptic transmission; ISO:MGI.
DR GO; GO:0060259; P:regulation of feeding behavior; ISO:MGI.
DR GO; GO:1905333; P:regulation of gastric motility; ISO:MGI.
DR GO; GO:0060123; P:regulation of growth hormone secretion; ISO:MGI.
DR GO; GO:0043134; P:regulation of hindgut contraction; ISO:MGI.
DR GO; GO:0098696; P:regulation of neurotransmitter receptor localization to postsynaptic specialization membrane; ISO:MGI.
DR GO; GO:0099175; P:regulation of postsynapse organization; ISO:MGI.
DR GO; GO:0051963; P:regulation of synapse assembly; IMP:MGI.
DR GO; GO:0051969; P:regulation of transmission of nerve impulse; ISO:MGI.
DR GO; GO:0071548; P:response to dexamethasone; IEA:Ensembl.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:0032354; P:response to follicle-stimulating hormone; IEA:Ensembl.
DR GO; GO:0032094; P:response to food; IDA:MGI.
DR GO; GO:0060416; P:response to growth hormone; IEA:Ensembl.
DR GO; GO:0009725; P:response to hormone; ISS:UniProtKB.
DR GO; GO:1904008; P:response to monosodium glutamate; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR InterPro; IPR039129; 7tmA_GHSR.
DR InterPro; IPR003905; GHS-R/MTLR.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24243:SF7; PTHR24243:SF7; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR01417; GHSRECEPTOR.
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; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..364
FT /note="Growth hormone secretagogue receptor type 1"
FT /id="PRO_0000069480"
FT TOPO_DOM 1..40
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..66
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..72
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..96
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..117
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..139
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..162
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..211
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..235
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..263
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..285
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..302
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..326
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..364
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 13
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 115..197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 59
FT /note="G -> S (in Ref. 2; AAL13336)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 364 AA; 40969 MW; 8F1214E58EF3B2E8 CRC64;
MWNATPSEEP EPNVTLDLDW DASPGNDSLS DELLPLFPAP LLAGVTATCV ALFVVGISGN
LLTMLVVSRF RELRTTTNLY LSSMAFSDLL IFLCMPLDLV RLWQYRPWNF GDLLCKLFQF
VSESCTYATV LTITALSVER YFAICFPLRA KVVVTKGRVK LVILVIWAVA FCSAGPIFVL
VGVEHENGTD PRDTNECRAT EFAVRSGLLT VMVWVSSVFF FLPVFCLTVL YSLIGRKLWR
RRGDAAVGSS LRDQNHKQTV KMLAVVVFAF ILCWLPFHVG RYLFSKSFEP GSLEIAQISQ
YCNLVSFVLF YLSAAINPIL YNIMSKKYRV AVFKLLGFES FSQRKLSTLK DESSRAWTKS
SINT
