Q8JFY4 · GHRL_ANGJA
- ProteinGhrelin
- Geneghrl
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids111 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Ligand for growth hormone secretagogue receptor type 1 (GHSR). Induces the release of growth hormone from the pituitary. Has an appetite-stimulating effect, induces adiposity and stimulates gastric acid secretion. Involved in growth regulation.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | extracellular space | |
Molecular Function | G protein-coupled receptor binding | |
Molecular Function | ghrelin receptor binding | |
Molecular Function | growth hormone-releasing hormone activity | |
Biological Process | G protein-coupled receptor signaling pathway | |
Biological Process | gastric acid secretion | |
Biological Process | negative regulation of inflammatory response | |
Biological Process | positive regulation of growth hormone secretion | |
Biological Process | regulation of response to food |
Keywords
- Molecular function
Names & Taxonomy
Protein names
- Recommended nameGhrelin
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Anguilliformes > Anguillidae > Anguilla
Accessions
- Primary accessionQ8JFY4
Subcellular Location
PTM/Processing
Features
Showing features for signal, peptide, lipidation, modified residue, propeptide.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-26 | |||||
Sequence: MRQMKRTAYIILLVCVLALWMDSVQA | ||||||
Peptide | PRO_0000019211 | 27-47 | Ghrelin | |||
Sequence: GSSFLSPSQRPQGKDKKPPRV | ||||||
Lipidation | 29 | O-decanoyl serine; alternate | ||||
Sequence: S | ||||||
Lipidation | 29 | O-hexanoyl serine; alternate | ||||
Sequence: S | ||||||
Lipidation | 29 | O-octanoyl serine; alternate | ||||
Sequence: S | ||||||
Modified residue | 47 | Valine amide | ||||
Sequence: V | ||||||
Propeptide | PRO_0000019212 | 51-111 | Removed in mature form | |||
Sequence: DSDGILDLFMRPPLQDEDIRHITFNTPFEIGITMTEELFQQYGEVMQKIMQDLLMDTPAKE |
Post-translational modification
O-octanoylated by GOAT/MBOAT4 (By similarity).
O-octanoylation or O-decanoylation is essential for activity. The O-decanoylated form ghrelin-21-C10 differs in the length of the carbon backbone of the carboxylic acid forming an ester bond with Ser-29. 44% of eel ghrelin is O-decanoylated (PubMed:12630926).
O-octanoylation or O-decanoylation is essential for activity. The O-decanoylated form ghrelin-21-C10 differs in the length of the carbon backbone of the carboxylic acid forming an ester bond with Ser-29. 44% of eel ghrelin is O-decanoylated (PubMed:12630926).
Keywords
- PTM
Expression
Tissue specificity
Highest levels in stomach and anterior intestine. Lower levels in posterior intestine, kidney and brain. Low levels in heart, head kidney and middle intestine.
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 28-53 | Disordered | ||||
Sequence: SSFLSPSQRPQGKDKKPPRVGRRDSD | ||||||
Compositional bias | 39-53 | Basic and acidic residues | ||||
Sequence: GKDKKPPRVGRRDSD |
Sequence similarities
Belongs to the motilin family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length111
- Mass (Da)12,831
- Last updated2002-10-01 v1
- Checksum7AF95E04DD22DE7B
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 39-53 | Basic and acidic residues | ||||
Sequence: GKDKKPPRVGRRDSD |
Mass Spectrometry
Keywords
- Technical term