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A0MLS4 (GHRL_PAPHA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 24. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Appetite-regulating hormone
Alternative name(s):
Growth hormone secretagogue
Growth hormone-releasing peptide
Motilin-related peptide

Cleaved into the following 2 chains:

  1. Ghrelin
  2. Obestatin
Gene names
Name:GHRL
OrganismPapio hamadryas (Hamadryas baboon)
Taxonomic identifier9557 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaePapio

Protein attributes

Sequence length117 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Ghrelin is the 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 By similarity.

Obestatin may be the ligand for GPR39. May have an appetite-reducing effect resulting in decreased food intake. May reduce gastric emptying activity and jejunal motility By similarity.

Subcellular location

Secreted By similarity.

Post-translational modification

O-octanoylation is essential for ghrelin activity By similarity.

Amidation of Leu-98 is essential for obestatin activity By similarity.

Sequence similarities

Belongs to the motilin family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionHormone
   PTMAmidation
Lipoprotein
Gene Ontology (GO)
   Biological_processactin polymerization or depolymerization

Inferred from sequence or structural similarity. Source: UniProtKB

activation of MAPK activity

Inferred from sequence or structural similarity. Source: UniProtKB

decidualization

Inferred from sequence or structural similarity. Source: UniProtKB

dendrite development

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of endothelial cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of inflammatory response

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of insulin secretion

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of interleukin-1 beta production

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of interleukin-6 biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of tumor necrosis factor biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cytosolic calcium ion concentration

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of insulin secretion

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein tyrosine kinase activity

Inferred from sequence or structural similarity. Source: GOC

positive regulation of response to food

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of synapse assembly

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of response to food

Inferred from sequence or structural similarity. Source: UniProtKB

response to estrogen

Inferred from sequence or structural similarity. Source: UniProtKB

response to hormone

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentaxon

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular region

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular space

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionghrelin receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

growth hormone-releasing hormone activity

Inferred from sequence or structural similarity. Source: UniProtKB

hormone activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein tyrosine kinase activator activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 By similarity
Peptide24 – 5128Ghrelin
PRO_0000278843
Propeptide52 – 7524Removed in mature form By similarity
PRO_0000278844
Peptide76 – 9823Obestatin By similarity
PRO_0000278845
Propeptide99 – 11719Removed in mature form By similarity
PRO_0000278846

Amino acid modifications

Modified residue981Leucine amide By similarity
Lipidation261O-octanoyl serine By similarity

Sequences

Sequence LengthMass (Da)Tools
A0MLS4 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 1B634ACE1E1F19FF

FASTA11712,913
        10         20         30         40         50         60 
MPSPGTVCSL LLLGMLWLDL AMAGSSFLSP EHQRAQQRKE SKKPPAKLQP RALGGWLRPE 

        70         80         90        100        110 
DGDQAEGAED ELEIQFNAPF DVGIKLSGVQ YQQHSQALGK FLQDILWEEA KEAPADK 

« Hide

References

[1]"Quantitative genetic analysis and characterization of ghrelin in baboons."
Voruganti V.S., Tejero M.E., Proffitt J.M., Cole S.A., Freeland-Graves J.H., Comuzzie A.G.
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Web resources

Protein Spotlight

Gut feelings - Issue 66 of January 2006

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ987858 mRNA. Translation: ABJ91203.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG018522.

Family and domain databases

InterProIPR006737. Motilin_assoc.
IPR006738. Motilin_ghrelin.
IPR005441. Preproghrelin.
[Graphical view]
PANTHERPTHR14122. PTHR14122. 1 hit.
PfamPF04643. Motilin_assoc. 1 hit.
PF04644. Motilin_ghrelin. 1 hit.
[Graphical view]
PRINTSPR01624. GHRELIN.
ProtoNetSearch...

Entry information

Entry nameGHRL_PAPHA
AccessionPrimary (citable) accession number: A0MLS4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: December 12, 2006
Last modified: April 16, 2014
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries