ID   GHSR_HUMAN              Reviewed;         366 AA.
AC   Q92847; Q14D12; Q6ISR8; Q92848; Q96RJ7;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   10-JUN-2026, entry version 207.
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   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] (ISOFORMS 1A AND 1B).
RC   TISSUE=Pituitary;
RX   PubMed=8688086; DOI=10.1126/science.273.5277.974;
RA   Howard A.D., Feighner S.D., Cully D.F., Arena J.P., Liberator P.A.,
RA   Rosenblum C.I., Hamelin M., Hreniuk D.L., Palyha O.C., Anderson J.,
RA   Paress P.S., Diaz C., Chou M., Liu K.K., McKee K.K., Pong S.-S.,
RA   Chaung L.-Y., Elbrecht A., Dashkevicz M., Heavens R., Rigby M.,
RA   Sirinathsinghji D.J.S., Dean D.C., Melillo D.G., Patchett A.A., Nargund R.,
RA   Griffin P.R., Demartino J.A., Gupta S.K., Schaeffer J.M., Smith R.G.,
RA   van der Ploeg L.H.T.;
RT   "A receptor in pituitary and hypothalamus that functions in growth hormone
RT   release.";
RL   Science 273:974-977(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1A AND 1B).
RX   PubMed=11356716; DOI=10.1210/endo.142.6.8184;
RA   Petersenn S., Rasch A.C., Penshorn M., Beil F.U., Schulte H.M.;
RT   "Genomic structure and transcriptional regulation of the human growth
RT   hormone secretagogue receptor.";
RL   Endocrinology 142:2649-2659(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1A AND 1B).
RA   Kopatz S.A., Aronstam R.S., Sharma S.V.;
RT   "cDNA clones of human proteins involved in signal transduction sequenced by
RT   the Guthrie cDNA resource center (www.cdna.org).";
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1A AND 1B).
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   [6]
RP   FUNCTION.
RX   PubMed=11322507; DOI=10.1385/endo:14:1:009;
RA   Smith R.G., Leonard R., Bailey A.R.T., Palyha O.C., Feighner S.D.,
RA   Tan C.P., Mckee K.K., Pong S.-S., Griffin P.R., Howard A.D.;
RT   "Growth hormone secretagogue receptor family members and ligands.";
RL   Endocrine 14:9-14(2001).
RN   [7]
RP   FUNCTION.
RX   PubMed=10604470; DOI=10.1038/45230;
RA   Kojima M., Hosoda H., Date Y., Nakazato M., Matsuo H., Kangawa K.;
RT   "Ghrelin is a growth-hormone-releasing acylated peptide from stomach.";
RL   Nature 402:656-660(1999).
RN   [8] {ECO:0007744|PDB:7F83, ECO:0007744|PDB:7W2Z}
RP   STRUCTURE BY ELECTRON MICROSCOPY (2.80 ANGSTROMS) IN COMPLEX WITH
RP   OCTANOYLATED GHRELIN; GNB1 AND GNG2, FUNCTION, ACTIVITY REGULATION,
RP   SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLU-124; LEU-210;
RP   TRP-276; PHE-279; ARG-283; PHE-286; GLN-302; ASN-305 AND PHE-312.
RX   PubMed=35027551; DOI=10.1038/s41467-022-27975-9;
RA   Qin J., Cai Y., Xu Z., Ming Q., Ji S.Y., Wu C., Zhang H., Mao C.,
RA   Shen D.D., Hirata K., Ma Y., Yan W., Zhang Y., Shao Z.;
RT   "Molecular mechanism of agonism and inverse agonism in ghrelin receptor.";
RL   Nat. Commun. 13:300-300(2022).
RN   [9] {ECO:0007744|PDB:8JSR}
RP   STRUCTURE BY ELECTRON MICROSCOPY (2.90 ANGSTROMS) OF 2-366 IN COMPLEX WITH
RP   ANAMORELIN; GNB1 AND GNG2, FUNCTION, ACTIVITY REGULATION, SUBUNIT,
RP   SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-99; ARG-102; LEU-103; GLN-120;
RP   GLU-124; ILE-178; LEU-210; MET-213; SER-217; ARG-283; PHE-286; ASN-305;
RP   PHE-309 AND PHE-312.
RX   PubMed=39833471; DOI=10.1038/s41594-024-01481-6;
RA   Shiimura Y., Im D., Tany R., Asada H., Kise R., Kurumiya E.,
RA   Wakasugi-Masuho H., Yasuda S., Matsui K., Kishikawa J.I., Kato T.,
RA   Murata T., Kojima M., Iwata S., Masuho I.;
RT   "The structure and function of the ghrelin receptor coding for drug
RT   actions.";
RL   Nat. Struct. Mol. Biol. 32:531-542(2025).
RN   [10]
RP   INVOLVEMENT IN GHDP, VARIANT GHDP GLU-204, AND CHARACTERIZATION OF VARIANT
RP   GHDP GLU-204.
RX   PubMed=16511605; DOI=10.1172/jci25303;
RA   Pantel J., Legendre M., Cabrol S., Hilal L., Hajaji Y., Morisset S.,
RA   Nivot S., Vie-Luton M.-P., Grouselle D., de Kerdanet M., Kadiri A.,
RA   Epelbaum J., Le Bouc Y., Amselem S.;
RT   "Loss of constitutive activity of the growth hormone secretagogue receptor
RT   in familial short stature.";
RL   J. Clin. Invest. 116:760-768(2006).
RN   [11]
RP   INVOLVEMENT IN GHDP, VARIANT GHDP TRP-237, AND CHARACTERIZATION OF VARIANT
RP   GHDP TRP-237.
RX   PubMed=19789204; DOI=10.1210/jc.2009-1327;
RA   Pantel J., Legendre M., Nivot S., Morisset S., Vie-Luton M.P., le Bouc Y.,
RA   Epelbaum J., Amselem S.;
RT   "Recessive isolated growth hormone deficiency and mutations in the ghrelin
RT   receptor.";
RL   J. Clin. Endocrinol. Metab. 94:4334-4341(2009).
CC   -!- FUNCTION: G protein-coupled receptor specific to ghrelin, an appetite-
CC       regulating peptide hormone commonly found in stomach (PubMed:35027551,
CC       PubMed:39833471). Upon activation, stimulates appetite and promotes
CC       growth hormone secretion (PubMed:11322507, PubMed:10604470,
CC       PubMed:35027551, PubMed:39833471). Also binds 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) (PubMed:11322507, PubMed:10604470).
CC       {ECO:0000269|PubMed:10604470, ECO:0000269|PubMed:11322507,
CC       ECO:0000269|PubMed:35027551, ECO:0000269|PubMed:39833471}.
CC   -!- ACTIVITY REGULATION: Activated by octanoylated ghrelin; octanoylation
CC       is essential for full activation of the receptor (PubMed:35027551).
CC       Stimulated by anamorelin, which binds to the same binding sites as
CC       ghrelin (PubMed:39833471). {ECO:0000269|PubMed:35027551,
CC       ECO:0000269|PubMed:39833471}.
CC   -!- SUBUNIT: Interacts with the heterotrimeric G protein complex composed
CC       of 3 units, alpha, beta and gamma; this complex may consist of GNB1 and
CC       GNG2. {ECO:0000269|PubMed:35027551, ECO:0000269|PubMed:39833471}.
CC   -!- INTERACTION:
CC       Q92847-1; Q92847-1: GHSR; NbExp=12; IntAct=EBI-21459171, EBI-21459171;
CC       Q92847-1; Q92847-2: GHSR; NbExp=10; IntAct=EBI-21459171, EBI-21459245;
CC       Q92847-1; Q99720: SIGMAR1; NbExp=8; IntAct=EBI-21459171, EBI-3248663;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:35027551,
CC       ECO:0000269|PubMed:39833471}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:35027551, ECO:0000269|PubMed:39833471}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1A;
CC         IsoId=Q92847-1; Sequence=Displayed;
CC       Name=1B;
CC         IsoId=Q92847-2; Sequence=VSP_001916, VSP_001917;
CC   -!- TISSUE SPECIFICITY: Pituitary and hypothalamus.
CC   -!- DISEASE: Growth hormone deficiency, isolated partial (GHDP)
CC       [MIM:615925]: A disorder characterized by partial growth hormone
CC       deficiency resulting in growth delay and short stature, sometimes
CC       associated with recurrent episodes of abdominal pain, vomiting, ketosis
CC       and hypoglycemia. {ECO:0000269|PubMed:16511605,
CC       ECO:0000269|PubMed:19789204}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the G protein-coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; U60179; AAC50653.1; -; mRNA.
DR   EMBL; U60181; AAC50654.1; -; mRNA.
DR   EMBL; AF369786; AAK71539.1; -; Genomic_DNA.
DR   EMBL; AF369786; AAK71540.1; -; Genomic_DNA.
DR   EMBL; AY429112; AAR07907.1; -; mRNA.
DR   EMBL; AY322544; AAP84357.1; -; Genomic_DNA.
DR   EMBL; CH471052; EAW78468.1; -; Genomic_DNA.
DR   EMBL; BC069068; AAH69068.1; -; mRNA.
DR   EMBL; BC069374; AAH69374.1; -; mRNA.
DR   EMBL; BC113547; AAI13548.1; -; mRNA.
DR   CCDS; CCDS3218.1; -. [Q92847-1]
DR   CCDS; CCDS46959.1; -. [Q92847-2]
DR   RefSeq; NP_004113.1; NM_004122.2. [Q92847-2]
DR   RefSeq; NP_940799.1; NM_198407.2. [Q92847-1]
DR   PDB; 6KO5; X-ray; 3.30 A; A=29-346.
DR   PDB; 7F83; X-ray; 2.94 A; A/B=35-243, A/B=253-342.
DR   PDB; 7F9Y; EM; 2.90 A; R=1-366.
DR   PDB; 7F9Z; EM; 3.20 A; R=1-366.
DR   PDB; 7NA7; EM; 2.70 A; R=1-366.
DR   PDB; 7NA8; EM; 2.70 A; R=1-366.
DR   PDB; 7W2Z; EM; 2.80 A; R=1-366.
DR   PDB; 8JSR; EM; 2.90 A; R=2-366.
DR   PDB; 9UY3; EM; 2.52 A; R=1-366.
DR   PDB; 9V2N; EM; 2.63 A; R=1-366.
DR   PDBsum; 6KO5; -.
DR   PDBsum; 7F83; -.
DR   PDBsum; 7F9Y; -.
DR   PDBsum; 7F9Z; -.
DR   PDBsum; 7NA7; -.
DR   PDBsum; 7NA8; -.
DR   PDBsum; 7W2Z; -.
DR   PDBsum; 8JSR; -.
DR   PDBsum; 9UY3; -.
DR   PDBsum; 9V2N; -.
DR   AlphaFoldDB; Q92847; -.
DR   EMDB; EMD-24267; -.
DR   EMDB; EMD-24268; -.
DR   EMDB; EMD-31501; -.
DR   EMDB; EMD-32268; -.
DR   EMDB; EMD-36627; -.
DR   EMDB; EMD-64606; -.
DR   EMDB; EMD-64734; -.
DR   SMR; Q92847; -.
DR   BioGRID; 108960; 9.
DR   CORUM; Q92847; -.
DR   FunCoup; Q92847; 763.
DR   IntAct; Q92847; 7.
DR   NDEx; IQUERY-CP-GHSR; 5 NDEx IQuery Curated Pathways.
DR   STRING; 9606.ENSP00000241256; -.
DR   BindingDB; Q92847; -.
DR   ChEMBL; CHEMBL4616; -.
DR   DrugBank; DB06645; Anamorelin.
DR   DrugBank; DB15205; Capromorelin.
DR   DrugBank; DB15488; Echinacoside.
DR   DrugBank; DB18214; Ibutamoren.
DR   DrugBank; DB12370; Ipamorelin.
DR   DrugBank; DB13074; Macimorelin.
DR   DrugBank; DB14870; PF-5190457.
DR   DrugBank; DB18252; Pralmorelin.
DR   DrugBank; DB20892; Tabimorelin.
DR   DrugBank; DB12128; Ulimorelin.
DR   DrugCentral; Q92847; -.
DR   GuidetoPHARMACOLOGY; 246; -.
DR   TCDB; 9.A.14.1.6; the g-protein-coupled receptor (gpcr) family.
DR   GlyCosmos; Q92847; 2 sites, No reported glycans.
DR   GlyGen; Q92847; 2 sites.
DR   iPTMnet; Q92847; -.
DR   PhosphoSitePlus; Q92847; -.
DR   BioMuta; GHSR; -.
DR   DMDM; 2494998; -.
DR   PaxDb; 9606-ENSP00000241256; -.
DR   ProteomicsDB; 75541; -. [Q92847-1]
DR   ProteomicsDB; 75542; -. [Q92847-2]
DR   Antibodypedia; 3248; 285 antibodies from 32 providers.
DR   DNASU; 2693; -.
DR   Ensembl; ENST00000241256.3; ENSP00000241256.2; ENSG00000121853.4. [Q92847-1]
DR   Ensembl; ENST00000427970.1; ENSP00000395344.1; ENSG00000121853.4. [Q92847-2]
DR   GeneID; 2693; -.
DR   KEGG; hsa:2693; -.
DR   MANE-Select; ENST00000241256.3; ENSP00000241256.2; NM_198407.2; NP_940799.1.
DR   UCSC; uc003fib.3; human. [Q92847-1]
DR   AGR; HGNC:4267; -.
DR   ClinPGx; PA28677; -.
DR   CTD; 2693; -.
DR   DisGeNET; 2693; -.
DR   GeneCards; GHSR; -.
DR   HGNC; HGNC:4267; GHSR.
DR   HPA; ENSG00000121853; Tissue enriched (pituitary).
DR   MalaCards; GHSR; -.
DR   MIM; 601898; gene.
DR   MIM; 615925; phenotype.
DR   OpenTargets; ENSG00000121853; -.
DR   Orphanet; 314811; Short stature due to GHSR deficiency.
DR   VEuPathDB; HostDB:ENSG00000121853; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01120000271823; -.
DR   HOGENOM; CLU_009579_6_5_1; -.
DR   InParanoid; Q92847; -.
DR   OMA; IGNLMTM; -.
DR   OrthoDB; 10011262at2759; -.
DR   PAN-GO; Q92847; 4 GO annotations based on evolutionary models.
DR   PhylomeDB; Q92847; -.
DR   PathwayCommons; Q92847; -.
DR   Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR   Reactome; R-HSA-416476; G alpha (q) signalling events.
DR   SignaLink; Q92847; -.
DR   SIGNOR; Q92847; -.
DR   Agora; ENSG00000121853; -.
DR   BioGRID-ORCS; 2693; 23 hits in 1140 CRISPR screens.
DR   GeneWiki; Growth_hormone_secretagogue_receptor; -.
DR   GenomeRNAi; 2693; -.
DR   Pharos; Q92847; Tclin.
DR   PRO; PR:Q92847; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q92847; protein.
DR   Bgee; ENSG00000121853; Expressed in pituitary gland and 20 other cell types or tissues.
DR   GO; GO:0009986; C:cell surface; IDA:HGNC-UCL.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
DR   GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProt.
DR   GO; GO:0098794; C:postsynapse; IEA:GOC.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR   GO; GO:0097060; C:synaptic membrane; IEA:Ensembl.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IDA:HGNC-UCL.
DR   GO; GO:0001616; F:growth hormone secretagogue receptor activity; IDA:HGNC-UCL.
DR   GO; GO:0016520; F:growth hormone-releasing hormone receptor activity; IDA:HGNC-UCL.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0017046; F:peptide hormone binding; IEA:Ensembl.
DR   GO; GO:0008154; P:actin polymerization or depolymerization; IDA:UniProtKB.
DR   GO; GO:0008343; P:adult feeding behavior; ISS:HGNC-UCL.
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; IDA:UniProtKB.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:HGNC-UCL.
DR   GO; GO:0036321; P:ghrelin secretion; IEA:Ensembl.
DR   GO; GO:0030252; P:growth hormone secretion; TAS:HGNC-UCL.
DR   GO; GO:0009755; P:hormone-mediated signaling pathway; IDA:HGNC-UCL.
DR   GO; GO:0007611; P:learning or memory; IEA:Ensembl.
DR   GO; GO:0032099; P:negative regulation of appetite; IEA:Ensembl.
DR   GO; GO:0050728; P:negative regulation of inflammatory response; IDA:UniProtKB.
DR   GO; GO:0032691; P:negative regulation of interleukin-1 beta production; IDA:UniProtKB.
DR   GO; GO:0032715; P:negative regulation of interleukin-6 production; IDA:UniProtKB.
DR   GO; GO:0090327; P:negative regulation of locomotion involved in locomotory behavior; IEA:Ensembl.
DR   GO; GO:2000110; P:negative regulation of macrophage apoptotic process; IEA:Ensembl.
DR   GO; GO:0010700; P:negative regulation of norepinephrine secretion; IEA:Ensembl.
DR   GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IDA:UniProtKB.
DR   GO; GO:0032100; P:positive regulation of appetite; ISS:HGNC-UCL.
DR   GO; GO:1904000; P:positive regulation of eating behavior; IEA:Ensembl.
DR   GO; GO:0045923; P:positive regulation of fatty acid metabolic process; IEA:Ensembl.
DR   GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:HGNC-UCL.
DR   GO; GO:0120058; P:positive regulation of small intestinal transit; IEA:Ensembl.
DR   GO; GO:1904349; P:positive regulation of small intestine smooth muscle contraction; IEA:Ensembl.
DR   GO; GO:1903672; P:positive regulation of sprouting angiogenesis; IEA:Ensembl.
DR   GO; GO:1905564; P:positive regulation of vascular endothelial cell proliferation; IEA:Ensembl.
DR   GO; GO:0099170; P:postsynaptic modulation of chemical synaptic transmission; IEA:Ensembl.
DR   GO; GO:1905333; P:regulation of gastric motility; IEA:Ensembl.
DR   GO; GO:0060123; P:regulation of growth hormone secretion; IEA:Ensembl.
DR   GO; GO:0043134; P:regulation of hindgut contraction; IEA:Ensembl.
DR   GO; GO:0098696; P:regulation of neurotransmitter receptor localization to postsynaptic specialization membrane; IEA:Ensembl.
DR   GO; GO:0099175; P:regulation of postsynapse organization; IEA:Ensembl.
DR   GO; GO:0051969; P:regulation of transmission of nerve impulse; IEA:Ensembl.
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:0060416; P:response to growth hormone; IEA:Ensembl.
DR   GO; GO:0009725; P:response to hormone; IDA: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   DisProt; DP03691; -.
DR   FunFam; 1.20.1070.10:FF:000125; growth hormone secretagogue receptor type 1; 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.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell membrane; Disease variant;
KW   Disulfide bond; Dwarfism; G protein-coupled receptor; Glycoprotein;
KW   Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..366
FT                   /note="Growth hormone secretagogue receptor type 1"
FT                   /id="PRO_0000069479"
FT   TOPO_DOM        1..40
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000269|PubMed:35027551,
FT                   ECO:0000269|PubMed:39833471, ECO:0007744|PDB:7F83,
FT                   ECO:0007744|PDB:7W2Z, ECO:0007744|PDB:8JSR"
FT   TRANSMEM        41..66
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000269|PubMed:35027551,
FT                   ECO:0000269|PubMed:39833471, ECO:0007744|PDB:7F83,
FT                   ECO:0007744|PDB:7W2Z, ECO:0007744|PDB:8JSR"
FT   TOPO_DOM        67..72
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:35027551,
FT                   ECO:0000269|PubMed:39833471, ECO:0007744|PDB:7F83,
FT                   ECO:0007744|PDB:7W2Z, ECO:0007744|PDB:8JSR"
FT   TRANSMEM        73..96
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000269|PubMed:35027551,
FT                   ECO:0000269|PubMed:39833471, ECO:0007744|PDB:7F83,
FT                   ECO:0007744|PDB:7W2Z, ECO:0007744|PDB:8JSR"
FT   TOPO_DOM        97..117
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000269|PubMed:35027551,
FT                   ECO:0000269|PubMed:39833471, ECO:0007744|PDB:7F83,
FT                   ECO:0007744|PDB:7W2Z, ECO:0007744|PDB:8JSR"
FT   TRANSMEM        118..139
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000269|PubMed:35027551,
FT                   ECO:0000269|PubMed:39833471, ECO:0007744|PDB:7F83,
FT                   ECO:0007744|PDB:7W2Z, ECO:0007744|PDB:8JSR"
FT   TOPO_DOM        140..162
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:35027551,
FT                   ECO:0000269|PubMed:39833471, ECO:0007744|PDB:7F83,
FT                   ECO:0007744|PDB:7W2Z, ECO:0007744|PDB:8JSR"
FT   TRANSMEM        163..183
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000269|PubMed:35027551,
FT                   ECO:0000269|PubMed:39833471, ECO:0007744|PDB:7F83,
FT                   ECO:0007744|PDB:7W2Z, ECO:0007744|PDB:8JSR"
FT   TOPO_DOM        184..211
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000269|PubMed:35027551,
FT                   ECO:0000269|PubMed:39833471, ECO:0007744|PDB:7F83,
FT                   ECO:0007744|PDB:7W2Z, ECO:0007744|PDB:8JSR"
FT   TRANSMEM        212..235
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000269|PubMed:35027551,
FT                   ECO:0000269|PubMed:39833471, ECO:0007744|PDB:7F83,
FT                   ECO:0007744|PDB:7W2Z, ECO:0007744|PDB:8JSR"
FT   TOPO_DOM        236..263
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:35027551,
FT                   ECO:0000269|PubMed:39833471, ECO:0007744|PDB:7F83,
FT                   ECO:0007744|PDB:7W2Z, ECO:0007744|PDB:8JSR"
FT   TRANSMEM        264..285
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000269|PubMed:35027551,
FT                   ECO:0000269|PubMed:39833471, ECO:0007744|PDB:7F83,
FT                   ECO:0007744|PDB:7W2Z, ECO:0007744|PDB:8JSR"
FT   TOPO_DOM        286..302
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000269|PubMed:35027551,
FT                   ECO:0000269|PubMed:39833471, ECO:0007744|PDB:7F83,
FT                   ECO:0007744|PDB:7W2Z, ECO:0007744|PDB:8JSR"
FT   TRANSMEM        303..326
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000269|PubMed:35027551,
FT                   ECO:0000269|PubMed:39833471, ECO:0007744|PDB:7F83,
FT                   ECO:0007744|PDB:7W2Z, ECO:0007744|PDB:8JSR"
FT   TOPO_DOM        327..366
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:35027551,
FT                   ECO:0000269|PubMed:39833471, ECO:0007744|PDB:7F83,
FT                   ECO:0007744|PDB:7W2Z, ECO:0007744|PDB:8JSR"
FT   BINDING         178
FT                   /ligand="octanoate"
FT                   /ligand_id="ChEBI:CHEBI:25646"
FT                   /evidence="ECO:0000269|PubMed:35027551,
FT                   ECO:0007744|PDB:7W2Z"
FT   BINDING         181
FT                   /ligand="octanoate"
FT                   /ligand_id="ChEBI:CHEBI:25646"
FT                   /evidence="ECO:0000269|PubMed:35027551,
FT                   ECO:0007744|PDB:7W2Z"
FT   BINDING         213
FT                   /ligand="octanoate"
FT                   /ligand_id="ChEBI:CHEBI:25646"
FT                   /evidence="ECO:0000269|PubMed:35027551,
FT                   ECO:0007744|PDB:7W2Z"
FT   BINDING         214
FT                   /ligand="octanoate"
FT                   /ligand_id="ChEBI:CHEBI:25646"
FT                   /evidence="ECO:0000269|PubMed:35027551,
FT                   ECO:0007744|PDB:7W2Z"
FT   BINDING         286
FT                   /ligand="octanoate"
FT                   /ligand_id="ChEBI:CHEBI:25646"
FT                   /evidence="ECO:0000269|PubMed:35027551,
FT                   ECO:0007744|PDB:7W2Z"
FT   CARBOHYD        13
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        27
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        116..198
FT                   /evidence="ECO:0007744|PDB:6KO5, ECO:0007744|PDB:7F83,
FT                   ECO:0007744|PDB:7F9Y, ECO:0007744|PDB:7F9Z,
FT                   ECO:0007744|PDB:7NA7, ECO:0007744|PDB:7NA8,
FT                   ECO:0007744|PDB:7W2Z, ECO:0007744|PDB:8JSR"
FT   VAR_SEQ         266..289
FT                   /note="AVVVFAFILCWLPFHVGRYLFSKS -> GGSQRALRLSLAGPILSLCLLPSL
FT                   (in isoform 1B)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:8688086, ECO:0000303|Ref.3"
FT                   /id="VSP_001916"
FT   VAR_SEQ         290..366
FT                   /note="Missing (in isoform 1B)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:8688086, ECO:0000303|Ref.3"
FT                   /id="VSP_001917"
FT   VARIANT         5
FT                   /note="T -> I (in dbSNP:rs2232165)"
FT                   /id="VAR_049389"
FT   VARIANT         204
FT                   /note="A -> E (in GHDP; affects cell-surface expression;
FT                   impairs constitutive activity; does not affect the ability
FT                   to respond to ghrelin; dbSNP:rs121917883)"
FT                   /evidence="ECO:0000269|PubMed:16511605"
FT                   /id="VAR_032705"
FT   VARIANT         237
FT                   /note="R -> W (in GHDP; results in partial loss of
FT                   constitutive activity of the receptor; does not affect
FT                   response to ghrelin; does not affect receptor cell-surface
FT                   expression; dbSNP:rs199588904)"
FT                   /evidence="ECO:0000269|PubMed:19789204"
FT                   /id="VAR_073173"
FT   MUTAGEN         99
FT                   /note="D->A: Impairs receptor activity stimulated by
FT                   anamorelin."
FT                   /evidence="ECO:0000269|PubMed:39833471"
FT   MUTAGEN         102
FT                   /note="R->A: Impairs receptor activity stimulated by
FT                   anamorelin."
FT                   /evidence="ECO:0000269|PubMed:39833471"
FT   MUTAGEN         103
FT                   /note="L->A: Impairs receptor activity stimulated by
FT                   anamorelin."
FT                   /evidence="ECO:0000269|PubMed:39833471"
FT   MUTAGEN         120
FT                   /note="Q->A: Impairs receptor activity stimulated by
FT                   anamorelin."
FT                   /evidence="ECO:0000269|PubMed:39833471"
FT   MUTAGEN         124
FT                   /note="E->A: Abolishes receptor activity stimulated by
FT                   anamorelin. Abolishes receptor activity stimulated by
FT                   ghrelin."
FT                   /evidence="ECO:0000269|PubMed:35027551,
FT                   ECO:0000269|PubMed:39833471"
FT   MUTAGEN         178
FT                   /note="I->A: Impairs receptor activity stimulated by
FT                   anamorelin."
FT                   /evidence="ECO:0000269|PubMed:39833471"
FT   MUTAGEN         210
FT                   /note="L->A: Impairs receptor activity stimulated by
FT                   anamorelin. Impairs receptor activity stimulated by
FT                   ghrelin."
FT                   /evidence="ECO:0000269|PubMed:35027551,
FT                   ECO:0000269|PubMed:39833471"
FT   MUTAGEN         213
FT                   /note="M->A: Impairs receptor activity stimulated by
FT                   anamorelin."
FT                   /evidence="ECO:0000269|PubMed:39833471"
FT   MUTAGEN         217
FT                   /note="S->A: Impairs receptor activity stimulated by
FT                   anamorelin."
FT                   /evidence="ECO:0000269|PubMed:39833471"
FT   MUTAGEN         276
FT                   /note="W->A: Impairs receptor activity stimulated by
FT                   ghrelin."
FT                   /evidence="ECO:0000269|PubMed:35027551"
FT   MUTAGEN         279
FT                   /note="F->A: Impairs receptor activity stimulated by
FT                   ghrelin."
FT                   /evidence="ECO:0000269|PubMed:35027551"
FT   MUTAGEN         283
FT                   /note="R->A: Abolishes receptor activity stimulated by
FT                   anamorelin. Impairs receptor activity stimulated by
FT                   ghrelin."
FT                   /evidence="ECO:0000269|PubMed:35027551,
FT                   ECO:0000269|PubMed:39833471"
FT   MUTAGEN         286
FT                   /note="F->A: Impairs receptor activity stimulated by
FT                   anamorelin. Abolishes receptor activity stimulated by
FT                   ghrelin."
FT                   /evidence="ECO:0000269|PubMed:35027551,
FT                   ECO:0000269|PubMed:39833471"
FT   MUTAGEN         302
FT                   /note="Q->A: Abolishes receptor activity stimulated by
FT                   ghrelin."
FT                   /evidence="ECO:0000269|PubMed:35027551"
FT   MUTAGEN         305
FT                   /note="N->A: Impairs receptor activity stimulated by
FT                   ghrelin."
FT                   /evidence="ECO:0000269|PubMed:35027551"
FT   MUTAGEN         305
FT                   /note="Missing: Impairs receptor activity stimulated by
FT                   anamorelin."
FT                   /evidence="ECO:0000269|PubMed:39833471"
FT   MUTAGEN         309
FT                   /note="F->A: Impairs receptor activity stimulated by
FT                   anamorelin."
FT                   /evidence="ECO:0000269|PubMed:39833471"
FT   MUTAGEN         312
FT                   /note="F->A: Impairs receptor activity stimulated by
FT                   anamorelin. Impairs receptor activity stimulated by
FT                   ghrelin."
FT                   /evidence="ECO:0000269|PubMed:35027551,
FT                   ECO:0000269|PubMed:39833471"
FT   HELIX           40..70
FT                   /evidence="ECO:0007829|PDB:9UY3"
FT   HELIX           72..74
FT                   /evidence="ECO:0007829|PDB:9UY3"
FT   HELIX           77..100
FT                   /evidence="ECO:0007829|PDB:9UY3"
FT   HELIX           101..105
FT                   /evidence="ECO:0007829|PDB:9UY3"
FT   HELIX           113..142
FT                   /evidence="ECO:0007829|PDB:9UY3"
FT   TURN            143..145
FT                   /evidence="ECO:0007829|PDB:9UY3"
FT   HELIX           148..154
FT                   /evidence="ECO:0007829|PDB:9UY3"
FT   HELIX           157..175
FT                   /evidence="ECO:0007829|PDB:9UY3"
FT   HELIX           178..181
FT                   /evidence="ECO:0007829|PDB:9UY3"
FT   STRAND          182..185
FT                   /evidence="ECO:0007829|PDB:9UY3"
FT   TURN            192..194
FT                   /evidence="ECO:0007829|PDB:9UY3"
FT   STRAND          197..200
FT                   /evidence="ECO:0007829|PDB:9UY3"
FT   HELIX           202..207
FT                   /evidence="ECO:0007829|PDB:9UY3"
FT   HELIX           209..240
FT                   /evidence="ECO:0007829|PDB:9UY3"
FT   HELIX           244..251
FT                   /evidence="ECO:0007829|PDB:7F83"
FT   TURN            252..254
FT                   /evidence="ECO:0007829|PDB:6KO5"
FT   HELIX           258..288
FT                   /evidence="ECO:0007829|PDB:9UY3"
FT   HELIX           295..320
FT                   /evidence="ECO:0007829|PDB:9UY3"
FT   HELIX           321..325
FT                   /evidence="ECO:0007829|PDB:9UY3"
FT   HELIX           328..333
FT                   /evidence="ECO:0007829|PDB:9UY3"
SQ   SEQUENCE   366 AA;  41329 MW;  D1B62710DA9DC0C6 CRC64;
     MWNATPSEEP GFNLTLADLD WDASPGNDSL GDELLQLFPA PLLAGVTATC VALFVVGIAG
     NLLTMLVVSR FRELRTTTNL YLSSMAFSDL LIFLCMPLDL VRLWQYRPWN FGDLLCKLFQ
     FVSESCTYAT VLTITALSVE RYFAICFPLR AKVVVTKGRV KLVIFVIWAV AFCSAGPIFV
     LVGVEHENGT DPWDTNECRP TEFAVRSGLL TVMVWVSSIF FFLPVFCLTV LYSLIGRKLW
     RRRRGDAVVG ASLRDQNHKQ TVKMLAVVVF AFILCWLPFH VGRYLFSKSF EPGSLEIAQI
     SQYCNLVSFV LFYLSAAINP ILYNIMSKKY RVAVFRLLGF EPFSQRKLST LKDESSRAWT
     ESSINT
//