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   24-JAN-2024, entry version 169.
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   GlyCosmos; Q99P50; 3 sites, No reported glycans.
DR   GlyGen; Q99P50; 3 sites.
DR   PhosphoSitePlus; Q99P50; -.
DR   PaxDb; 10090-ENSMUSP00000061153; -.
DR   Antibodypedia; 3248; 321 antibodies from 32 providers.
DR   DNASU; 208188; -.
DR   Ensembl; ENSMUST00000057186.2; ENSMUSP00000061153.2; ENSMUSG00000051136.2.
DR   GeneID; 208188; -.
DR   KEGG; mmu:208188; -.
DR   UCSC; uc008oto.1; mouse.
DR   AGR; MGI:2441906; -.
DR   CTD; 2693; -.
DR   MGI; MGI:2441906; Ghsr.
DR   VEuPathDB; HostDB:ENSMUSG00000051136; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01100000263484; -.
DR   HOGENOM; CLU_009579_6_5_1; -.
DR   InParanoid; Q99P50; -.
DR   OMA; IGNLMTM; -.
DR   OrthoDB; 3471593at2759; -.
DR   PhylomeDB; Q99P50; -.
DR   TreeFam; TF332184; -.
DR   Reactome; R-MMU-416476; G alpha (q) signalling events.
DR   BioGRID-ORCS; 208188; 2 hits in 78 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 cell types or tissues.
DR   ExpressionAtlas; Q99P50; baseline and differential.
DR   GO; GO:0009986; C:cell surface; ISS:HGNC-UCL.
DR   GO; GO:0098978; C:glutamatergic synapse; 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; IBA:GO_Central.
DR   GO; GO:0098794; C:postsynapse; IEA:GOC.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:MGI.
DR   GO; GO:0097060; C:synaptic membrane; 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:1902065; P:response to L-glutamate; IEA:Ensembl.
DR   GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR   CDD; cd15131; 7tmA_GHSR; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR003905; GHS-R/MTLR.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   PANTHER; PTHR24243; G-PROTEIN COUPLED RECEPTOR; 1.
DR   PANTHER; PTHR24243:SF7; GROWTH HORMONE SECRETAGOGUE RECEPTOR TYPE 1; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR01417; GHSRECEPTOR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   Genevisible; Q99P50; MM.
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
//