Q76IQ4 · GHRL_ONCMY
- ProteinGhrelin
- Geneghrl
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids111 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Ligand for growth hormone secretagogue receptor type 1 (GHSR). Has an appetite-stimulating effect, induces adiposity and stimulates gastric acid secretion. Involved in growth regulation (By similarity).
Induces the release of growth hormone from the pituitary
Induces the release of growth hormone from the pituitary
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 | growth hormone secretion | |
Biological Process | negative regulation of appetite | |
Biological Process | negative regulation of inflammatory response | |
Biological Process | positive regulation of gene expression | |
Biological Process | positive regulation of growth hormone secretion | |
Biological Process | positive regulation of superoxide dismutase activity | |
Biological Process | regulation of cytosolic calcium ion concentration | |
Biological Process | response to starvation |
Keywords
- Molecular function
Names & Taxonomy
Protein names
- Recommended nameGhrelin
- Cleaved into 2 chains
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Protacanthopterygii > Salmoniformes > Salmonidae > Salmoninae > Oncorhynchus
Accessions
- Primary accessionQ76IQ4
- Secondary accessions
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for signal, peptide, lipidation, modified residue, propeptide.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-26 | |||||
Sequence: MPLKRNTGLMILMLCTLALWAKSVSA | ||||||
Peptide | PRO_0000019217 | 27-49 | Ghrelin-23 | |||
Sequence: GSSFLSPSQKPQVRQGKGKPPRV | ||||||
Peptide | PRO_0000019216 | 27-50 | Ghrelin-24 | |||
Sequence: GSSFLSPSQKPQVRQGKGKPPRVG | ||||||
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 | 49 | Valine amide | ||||
Sequence: V | ||||||
Propeptide | PRO_0000019218 | 53-111 | Removed in mature form | |||
Sequence: DIESFAELFEGPLHQEDKHNTIKAPFEMGITMSEEEFQEYGAVLQKILQDVLGDTATAE |
Post-translational modification
O-octanoylated by GOAT/MBOAT4 (By similarity).
O-octanoylation or O-decanoylation is essential for activity. The O-decanoylated forms differ in the length of the carbon backbone of the carboxylic acid forming an ester bond with Ser-29 (By similarity).
The majority of trout ghrelin is Ghrelin-20 modified with unsaturated decanoic acid (PubMed:12970156).
O-octanoylation or O-decanoylation is essential for activity. The O-decanoylated forms differ in the length of the carbon backbone of the carboxylic acid forming an ester bond with Ser-29 (By similarity).
The majority of trout ghrelin is Ghrelin-20 modified with unsaturated decanoic acid (PubMed:12970156).
Ghrelin-20 and Ghrelin-23 are amidated. In some cases, Gly-50 is retained after dibasic amino acid cleavage, to produce non-amidated Ghrelin-21 and Ghrelin-24.
Keywords
- PTM
Expression
Tissue specificity
Highest levels in the stomach. Moderate levels in the brain, hypothalamus and intestinal tracts.
Structure
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
Q76IQ4-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length111
- Mass (Da)12,304
- Last updated2004-07-05 v1
- Checksum28CE572EA3BD3F96
Q76IQ4-2
- Name2
- Synonymsdes-VRQ-ghrelin
- Differences from canonical
- 39-41: Missing
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_051754 | 39-41 | in isoform 2 | |||
Sequence: Missing |
Mass Spectrometry
Isoform 2
Molecular mass is 2,204.8 Da. Determined by MALDI. With amidation and (C8:1) O-octanoylation. The measured range is 27-49.Isoform 2
Molecular mass is 2,206.6 Da. Determined by MALDI. With amidation and (C8:0) O-octanoylation. The measured range is 27-49.Isoform 2
Molecular mass is 2,230.7 Da. Determined by MALDI. With amidation and (C10:2) O-decanoylation. Major form. The measured range is 27-49.Isoform 2
Molecular mass is 2,232.5 Da. Determined by MALDI. With amidation and (C10:1) O-decanoylation. The measured range is 27-49.Isoform 2
Molecular mass is 2,235 Da. Determined by MALDI. With amidation and (C10:0) O-decanoylation. The measured range is 27-49.Isoform 2
Molecular mass is 2,264.1 Da. Determined by MALDI. With glycine retention and (C8:0) O-octanoylation. The measured range is 27-50.Isoform 2
Molecular mass is 2,288.4 Da. Determined by MALDI. With glycine retention and (C10:2) O-decanoylation. The measured range is 27-50.Isoform 2
Molecular mass is 2,291.1 Da. Determined by MALDI. With glycine retention and (C10:1) O-decanoylation. The measured range is 27-50.Isoform 1
Molecular mass is 2,590 Da. Determined by MALDI. With amidation and (C8:0) O-octanoylation. The measured range is 27-49.Isoform 1
Molecular mass is 2,613.9 Da. Determined by MALDI. With amidation and (C10:1) O-decanoylation. The measured range is 27-49.Isoform 1
Molecular mass is 2,648.2 Da. Determined by MALDI. With glycine retention and (C8:0) O-octanoylation. The measured range is 27-50.Isoform 1
Molecular mass is 2,672.3 Da. Determined by MALDI. With glycine retention and (C10:2) O-decanoylation. The measured range is 27-50.Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB096919 EMBL· GenBank· DDBJ | BAD02979.1 EMBL· GenBank· DDBJ | mRNA | ||
AB100839 EMBL· GenBank· DDBJ | BAD02980.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AB100839 EMBL· GenBank· DDBJ | BAD02981.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AB101443 EMBL· GenBank· DDBJ | BAD02982.1 EMBL· GenBank· DDBJ | mRNA |