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UniProtKB - Q90W22 (GHRL_LITCT)
Protein
Ghrelin
Gene
GHRL
Organism
Lithobates catesbeianus (American bullfrog) (Rana catesbeiana)
Status
Functioni
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.
1 PublicationGO - Molecular functioni
- hormone activity Source: UniProtKB-KW
Keywordsi
Molecular function | Hormone |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:GHRL |
Organismi | Lithobates catesbeianus (American bullfrog) (Rana catesbeiana) |
Taxonomic identifieri | 8400 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Neobatrachia › Ranoidea › Ranidae › Lithobates |
Subcellular locationi
Extracellular region or secreted
- Secreted Curated
Extracellular region or secreted
- extracellular region Source: UniProtKB-SubCell
Keywords - Cellular componenti
SecretedPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 24 | 1 PublicationAdd BLAST | 24 | |
PeptideiPRO_0000019219 | 25 – 52 | Ghrelin-281 PublicationAdd BLAST | 28 | |
PeptideiPRO_0000019220 | 25 – 51 | Ghrelin-271 PublicationAdd BLAST | 27 | |
PropeptideiPRO_0000019221 | 55 – 114 | Removed in mature formAdd BLAST | 60 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Lipidationi | 27 | O-decanoyl threonine; alternate1 Publication | 1 | |
Lipidationi | 27 | O-octanoyl threonine; alternate1 Publication | 1 |
Post-translational modificationi
O-octanoylated by GOAT/MBOAT4 (By similarity). O-octanoylation or O-decanoylation is essential for activity. The O-decanoylated form ghrelin-27-C10 differs in the length of the carbon backbone of the carboxylic acid bound to Thr-27. 33% of frog ghrelin is O-decanoylated (PubMed:11546772).By similarity1 Publication
80% of frog ghrelin has Asn-52 cleaved from its C-terminus giving rise to ghrelin-27.1 Publication
Keywords - PTMi
Cleavage on pair of basic residues, LipoproteinExpressioni
Tissue specificityi
High levels in stomach. Moderate levels in small intestine, pancreas and testis. Low levels in heart, lung and gall bladder.1 Publication
Family & Domainsi
Sequence similaritiesi
Belongs to the motilin family.Sequence analysis
Keywords - Domaini
Signali Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
Q90W22-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MNFGKAAIFG VVLFCLLWTE GAQAGLTFLS PADMQKIAER QSQNKLRHGN
60 70 80 90 100
MNRRGVEDDL AGEEIGVTFP LDMKMTQEQF QKQRAAVQDF LYSSLLSLGS
110
VQDTEDKNEN PQSQ
Mass spectrometryi
Molecular mass is 3308.5±0.9 Da. Determined by ESI. Ghrelin-28-C8, O-octanoylated form.1 Publication
Molecular mass is 3225.3±1.7 Da. Determined by ESI. Ghrelin-27-C10, O-decanoylated form.1 Publication
Molecular mass is 3196.1±0.9 Da. Determined by ESI. Ghrelin-28-C8, O-octanoylated form.1 Publication
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AB058510 mRNA Translation: BAB71718.1 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AB058510 mRNA Translation: BAB71718.1 |
3D structure databases
AlphaFoldDBi | Q90W22 |
SMRi | Q90W22 |
ModBasei | Search... |
Family and domain databases
MobiDBi | Search... |
Entry informationi
Entry namei | GHRL_LITCT | |
Accessioni | Q90W22Primary (citable) accession number: Q90W22 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | June 21, 2005 |
Last sequence update: | December 1, 2001 | |
Last modified: | May 25, 2022 | |
This is version 45 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencingDocuments
- SIMILARITY comments
Index of protein domains and families