GHSR
entrez
2693
canonical
uniprot
Q92847
canonical
ensembl
ENSG00000121853
resolver
ensp
ENSP00000241256
resolver
ensp
ENSP00000395344
resolver
genesymbol
GHSR
resolver
hgnc
HGNC:4267
resolver
uniprot
Q14D12
resolver
uniprot
Q6ISR8
resolver
uniprot
Q92848
resolver
uniprot
Q96RJ7
resolver
uniprot_entry
GHSR_HUMAN
resolver
uniprot_sec
Q14D12
resolver
uniprot_sec
Q6ISR8
resolver
uniprot_sec
Q92848
resolver
uniprot_sec
Q96RJ7
resolver
activity_regulation
ACTIVITY REGULATION: Activated by octanoylated ghrelin; octanoylation is essential for full activation of the receptor (PubMed:35027551). Stimulated by anamorelin, which binds to the same binding sites as ghrelin (PubMed:39833471). {ECO:0000269|PubMed:35027551, ECO:0000269|PubMed:39833471}.
uniprot
proteins
amino_acid_sequence
MWNATPSEEPGFNLTLADLDWDASPGNDSLGDELLQLFPAPLLAGVTATCVALFVVGIAGNLLTMLVVSRFRELRTTTNLYLSSMAFSDLLIFLCMPLDLVRLWQYRPWNFGDLLCKLFQFVSESCTYATVLTITALSVERYFAICFPLRAKVVVTKGRVKLVIFVIWAVAFCSAGPIFVLVGVEHENGTDPWDTNECRPTEFAVRSGLLTVMVWVSSIFFFLPVFCLTVLYSLIGRKLWRRRRGDAVVGASLRDQNHKQTVKMLAVVVFAFILCWLPFHVGRYLFSKSFEPGSLEIAQISQYCNLVSFVLFYLSAAINPILYNIMSKKYRVAVFRLLGFEPFSQRKLSTLKDESSRAWTESSINT
uniprot
proteins
disease_involvement
DISEASE: Growth hormone deficiency, isolated partial (GHDP) [MIM:615925]: A disorder characterized by partial growth hormone deficiency resulting in growth delay and short stature, sometimes associated with recurrent episodes of abdominal pain, vomiting, ketosis and hypoglycemia. {ECO:0000269|PubMed:16511605, ECO:0000269|PubMed:19789204}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: G protein-coupled receptor specific to ghrelin, an appetite-regulating peptide hormone commonly found in stomach (PubMed:35027551, PubMed:39833471). Upon activation, stimulates appetite and promotes growth hormone secretion (PubMed:10604470, PubMed:11322507, PubMed:35027551, PubMed:39833471). Ghrelin binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors, such as phospholipase C (By similarity). GHSR is coupled to G(q) G proteins and mediates production of diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) (By similarity). Also binds other growth hormone releasing peptides (GHRP) (e.g. Met-enkephalin and GHRP-6) as well as non-peptide, low molecular weight secretagogues (e.g. L-692, 429, MK-0677, adenosine) (PubMed:10604470, PubMed:11322507). Also plays a role in synaptic plasticity independently of ghrelin by forming a heteromer with the dopamine receptors DRD1 and DRD2 in neurons (By similarity). Following DRD1 activation by dopamine in hippocampal neurons, GHSR acts as a coreceptor, resulting in DRD1 coupling to G(q) at the expense of G(s), initiating hippocampal synaptic plasticity involved in memory and learning (By similarity). Following DRD2 activation by dopamine in lumbosacral defecation centers, GHSR acts as a coreceptor, resulting in DRD1 coupling to G(q) at the expense of G(i)/G(o), regulating defecation (By similarity). {ECO:0000250|UniProtKB:O08725, ECO:0000250|UniProtKB:Q99P50, ECO:0000269|PubMed:10604470, ECO:0000269|PubMed:11322507, ECO:0000269|PubMed:35027551, ECO:0000269|PubMed:39833471}.
uniprot
proteins
mass_dalton
41329
uniprot
proteins
mutagenesis
MUTAGEN 99; /note="D->A: Impairs receptor activity stimulated by anamorelin."; /evidence="ECO:0000269|PubMed:39833471"; MUTAGEN 102; /note="R->A: Impairs receptor activity stimulated by anamorelin."; /evidence="ECO:0000269|PubMed:39833471"; MUTAGEN 103; /note="L->A: Impairs receptor activity stimulated by anamorelin."; /evidence="ECO:0000269|PubMed:39833471"; MUTAGEN 120; /note="Q->A: Impairs receptor activity stimulated by anamorelin."; /evidence="ECO:0000269|PubMed:39833471"; MUTAGEN 124; /note="E->A: Abolishes receptor activity stimulated by anamorelin. Abolishes receptor activity stimulated by ghrelin."; /evidence="ECO:0000269|PubMed:35027551, ECO:0000269|PubMed:39833471"; MUTAGEN 178; /note="I->A: Impairs receptor activity stimulated by anamorelin."; /evidence="ECO:0000269|PubMed:39833471"; MUTAGEN 210; /note="L->A: Impairs receptor activity stimulated by anamorelin. Impairs receptor activity stimulated by ghrelin."; /evidence="ECO:0000269|PubMed:35027551, ECO:0000269|PubMed:39833471"; MUTAGEN 213; /note="M->A: Impairs receptor activity stimulated by anamorelin."; /evidence="ECO:0000269|PubMed:39833471"; MUTAGEN 217; /note="S->A: Impairs receptor activity stimulated by anamorelin."; /evidence="ECO:0000269|PubMed:39833471"; MUTAGEN 276; /note="W->A: Impairs receptor activity stimulated by ghrelin."; /evidence="ECO:0000269|PubMed:35027551"; MUTAGEN 279; /note="F->A: Impairs receptor activity stimulated by ghrelin."; /evidence="ECO:0000269|PubMed:35027551"; MUTAGEN 283; /note="R->A: Abolishes receptor activity stimulated by anamorelin. Impairs receptor activity stimulated by ghrelin."; /evidence="ECO:0000269|PubMed:35027551, ECO:0000269|PubMed:39833471"; MUTAGEN 286; /note="F->A: Impairs receptor activity stimulated by anamorelin. Abolishes receptor activity stimulated by ghrelin."; /evidence="ECO:0000269|PubMed:35027551, ECO:0000269|PubMed:39833471"; MUTAGEN 302; /note="Q->A: Abolishes receptor activity stimulated by ghrelin."; /evidence="ECO:0000269|PubMed:35027551"; MUTAGEN 305; /note="N->A: Impairs receptor activity stimulated by ghrelin."; /evidence="ECO:0000269|PubMed:35027551"; MUTAGEN 305; /note="Missing: Impairs receptor activity stimulated by anamorelin."; /evidence="ECO:0000269|PubMed:39833471"; MUTAGEN 309; /note="F->A: Impairs receptor activity stimulated by anamorelin."; /evidence="ECO:0000269|PubMed:39833471"; MUTAGEN 312; /note="F->A: Impairs receptor activity stimulated by anamorelin. Impairs receptor activity stimulated by ghrelin."; /evidence="ECO:0000269|PubMed:35027551, ECO:0000269|PubMed:39833471
uniprot
proteins
protein_family
G protein-coupled receptor 1 family
uniprot
proteins
pubmed
10604470
uniprot
proteins
pubmed
11322507
uniprot
proteins
pubmed
11356716
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16511605
uniprot
proteins
pubmed
19789204
uniprot
proteins
pubmed
35027551
uniprot
proteins
pubmed
39833471
uniprot
proteins
pubmed
8688086
uniprot
proteins
sequence_length
366
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:35027551, ECO:0000269|PubMed:39833471}; Multi-pass membrane protein {ECO:0000269|PubMed:35027551, ECO:0000269|PubMed:39833471}.
uniprot
proteins
transmembrane_region
TRANSMEM 41..66; /note="Helical; Name=1"; /evidence="ECO:0000269|PubMed:35027551, ECO:0000269|PubMed:39833471, ECO:0007744|PDB:7F83, ECO:0007744|PDB:7W2Z, ECO:0007744|PDB:8JSR"; TRANSMEM 73..96; /note="Helical; Name=2"; /evidence="ECO:0000269|PubMed:35027551, ECO:0000269|PubMed:39833471, ECO:0007744|PDB:7F83, ECO:0007744|PDB:7W2Z, ECO:0007744|PDB:8JSR"; TRANSMEM 118..139; /note="Helical; Name=3"; /evidence="ECO:0000269|PubMed:35027551, ECO:0000269|PubMed:39833471, ECO:0007744|PDB:7F83, ECO:0007744|PDB:7W2Z, ECO:0007744|PDB:8JSR"; TRANSMEM 163..183; /note="Helical; Name=4"; /evidence="ECO:0000269|PubMed:35027551, ECO:0000269|PubMed:39833471, ECO:0007744|PDB:7F83, ECO:0007744|PDB:7W2Z, ECO:0007744|PDB:8JSR"; TRANSMEM 212..235; /note="Helical; Name=5"; /evidence="ECO:0000269|PubMed:35027551, ECO:0000269|PubMed:39833471, ECO:0007744|PDB:7F83, ECO:0007744|PDB:7W2Z, ECO:0007744|PDB:8JSR"; TRANSMEM 264..285; /note="Helical; Name=6"; /evidence="ECO:0000269|PubMed:35027551, ECO:0000269|PubMed:39833471, ECO:0007744|PDB:7F83, ECO:0007744|PDB:7W2Z, ECO:0007744|PDB:8JSR"; TRANSMEM 303..326; /note="Helical; Name=7"; /evidence="ECO:0000269|PubMed:35027551, ECO:0000269|PubMed:39833471, ECO:0007744|PDB:7F83, ECO:0007744|PDB:7W2Z, ECO:0007744|PDB:8JSR
uniprot
proteins