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Q9BDJ6 (GHRL_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 73. 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
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length116 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-97 is essential for obestatin activity By similarity.

Sequence similarities

Belongs to the motilin family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionHormone
   PTMAmidation
Lipoprotein
   Technical termComplete proteome
Reference proteome
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 – 5027Ghrelin By similarity
PRO_0000019194
Propeptide51 – 7424Removed in mature form By similarity
PRO_0000019195
Peptide75 – 9723Obestatin By similarity
PRO_0000045132
Propeptide98 – 11619Removed in mature form By similarity
PRO_0000045133

Amino acid modifications

Modified residue971Leucine amide By similarity
Lipidation261O-octanoyl serine By similarity

Experimental info

Sequence conflict341K → E in BAB19047. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9BDJ6 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: F55536DAC5FA59B6

FASTA11612,793
        10         20         30         40         50         60 
MPAPWTICSL LLLSVLCMDL AMAGSSFLSP EHQKLQRKEA KKPSGRLKPR TLEGQFDPEV 

        70         80         90        100        110 
GSQAEGAEDE LEIRFNAPFN IGIKLAGAQS LQHGQTLGKF LQDILWEEAE ETLANE 

« Hide

References

[1]Kita K., Harada K., Yokota H.
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"A full length genomic sequence of the bovine ghrelin gene."
Li C., Lobo S., Wang Z., Fu A., Meng Y., Murdoch B., Hansen C., Moore S.
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]Kojima M.
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 24-99.

Web resources

Protein Spotlight

Gut feelings - Issue 66 of January 2006

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF350329 mRNA. Translation: AAK18612.1.
AY903701 Genomic DNA. Translation: AAX89508.1.
AB035702 mRNA. Translation: BAB19047.1.
RefSeqNP_776492.1. NM_174067.2.
UniGeneBt.8142.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000016350; ENSBTAP00000016350; ENSBTAG00000012328.
GeneID281192.
KEGGbta:281192.

Organism-specific databases

CTD51738.

Phylogenomic databases

eggNOGNOG45924.
GeneTreeENSGT00390000004064.
HOGENOMHOG000236303.
HOVERGENHBG018522.
KOK05254.

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...

Other

NextBio20805249.

Entry information

Entry nameGHRL_BOVIN
AccessionPrimary (citable) accession number: Q9BDJ6
Secondary accession number(s): Q0VH85, Q9GKY6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 13, 2001
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 73 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