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Q9EQX0 (GHRL_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·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
Protein M46

Cleaved into the following 2 chains:

  1. Ghrelin
  2. Obestatin
Gene names
Name:Ghrl
Synonyms:Mtlrp
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length117 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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.

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 Ref.1.

Tissue specificity

Mainly expressed in the gastrointestinal tract with higher levels in the stomach, medium levels in the duodenum, jejunum, ileum and colon. Low expression in the testis and brain. Not detected in the salivary gland, pancreas, liver and lung. Ref.1

Developmental stage

Levels of n-octanoylated and n-decanoylated ghrelin drop by one third and 3-fold, respectively, between postnatal weeks 3 and 4 due to change of diet during weaning. Ref.5

Post-translational modification

O-octanoylation or O-decanoylation is essential for ghrelin activity By similarity. The O-decanoylated form ghrelin-C10 differs in the length of the carbon backbone of the carboxylic acid bound to Ser-26 (Ref.5).

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

Sequence similarities

Belongs to the motilin family.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
   DomainSignal
   Molecular functionHormone
   PTMAmidation
Lipoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

actin polymerization or depolymerization

Inferred from sequence or structural similarity. Source: UniProtKB

activation of MAPK activity

Inferred from sequence or structural similarity. Source: UniProtKB

adult feeding behavior

Inferred from direct assay PubMed 16322794. Source: HGNC

decidualization

Inferred from sequence or structural similarity. Source: UniProtKB

dendrite development

Inferred from sequence or structural similarity. Source: UniProtKB

gastric acid secretion

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of circadian sleep/wake cycle, REM sleep

Inferred from electronic annotation. Source: Ensembl

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 locomotion

Inferred from mutant phenotype PubMed 16322795. Source: MGI

negative regulation of tumor necrosis factor biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of appetite

Inferred from direct assay PubMed 16322794. Source: HGNC

positive regulation of circadian sleep/wake cycle, non-REM sleep

Inferred from electronic annotation. Source: Ensembl

positive regulation of corticotropin secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of cortisol secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of cytosolic calcium ion concentration

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of growth hormone secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of insulin secretion

Inferred from sequence or structural similarity. Source: UniProtKB

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 excitatory postsynaptic membrane potential

Inferred from mutant phenotype PubMed 16491079. Source: MGI

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

cytoplasm

Inferred from direct assay Ref.1. Source: MGI

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...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9EQX0-1)

Also known as: Ghrelin;

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.
Isoform 2 (identifier: Q9EQX0-2)

Also known as: des-Gln14-ghrelin;

The sequence of this isoform differs from the canonical sequence as follows:
     37-37: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Ref.1
Peptide24 – 5128Ghrelin
PRO_0000019205
Propeptide52 – 7524Removed in mature form By similarity
PRO_0000019206
Peptide76 – 9823Obestatin
PRO_0000045142
Propeptide99 – 11719Removed in mature form By similarity
PRO_0000045143

Amino acid modifications

Modified residue981Leucine amide Ref.7
Lipidation261O-decanoyl serine; alternate
Lipidation261O-octanoyl serine; alternate

Natural variations

Alternative sequence371Missing in isoform 2.
VSP_003246

Secondary structure

...... 117
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Ghrelin) [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: EACB49D2E3CA7203

FASTA11713,207
        10         20         30         40         50         60 
MLSSGTICSL LLLSMLWMDM AMAGSSFLSP EHQKAQQRKE SKKPPAKLQP RALEGWLHPE 

        70         80         90        100        110 
DRGQAEETEE ELEIRFNAPF DVGIKLSGAQ YQQHGRALGK FLQDILWEEV KEAPADK 

« Hide

Isoform 2 (des-Gln14-ghrelin) [UniParc].

Checksum: E00DA3D67998B6B8
Show »

FASTA11613,079

References

« Hide 'large scale' references
[1]"Identification and characterization of a novel gastric peptide hormone: the motilin-related peptide."
Tomasetto C., Karam S.M., Ribieras S., Masson R., Lefebvre O., Staub A., Alexander G., Chenard M.-P., Rio M.-C.
Gastroenterology 119:395-405(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 24-30, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Stomach.
[2]"Mouse mRNA for preproghrelin."
Kojima M.
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]Tanaka M., Hayashida Y., Iguchi T., Nakao N., Nakai N., Nakashima K.
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Stomach.
[5]"Developmental changes in the pattern of ghrelin's acyl modification and the levels of acyl-modified ghrelins in murine stomach."
Nishi Y., Hiejima H., Mifune H., Sato T., Kangawa K., Kojima M.
Endocrinology 146:2709-2715(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE, ACYLATION AT SER-26.
[6]"Ghrelin: discovery of the natural endogenous ligand for the growth hormone secretagogue receptor."
Kojima M., Hosoda H., Matsuo H., Kangawa K.
Trends Endocrinol. Metab. 12:118-122(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[7]"Obestatin conformational features: a strategy to unveil obestatin's biological role ?"
Scrima M., Campiglia P., Esposito C., Gomez-Monterrey I., Novellino E., D'Ursi A.M.
Biochem. Biophys. Res. Commun. 363:500-505(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 76-98, AMIDATION AT LEU-98.
+Additional computationally mapped references.

Web resources

Protein Spotlight

Gut feelings - Issue 66 of January 2006

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ243503 mRNA. Translation: CAB46500.1.
AB035701 mRNA. Translation: BAB19046.1.
AB060078 Genomic DNA. Translation: BAB69857.1.
AK008658 mRNA. Translation: BAB25814.1.
AK008860 mRNA. Translation: BAB25934.1.
CCDSCCDS20432.1. [Q9EQX0-1]
RefSeqNP_001273333.1. NM_001286404.1. [Q9EQX0-2]
NP_001273334.1. NM_001286405.1.
NP_001273335.1. NM_001286406.1.
NP_067463.2. NM_021488.5. [Q9EQX0-1]
XP_006506509.1. XM_006506446.1. [Q9EQX0-1]
UniGeneMm.379095.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2JSHNMR-A76-98[»]
2JSINMR-A86-98[»]
2JSJNMR-A76-98[»]
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ9EQX0.

Proteomic databases

MaxQBQ9EQX0.
PaxDbQ9EQX0.
PRIDEQ9EQX0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000064993; ENSMUSP00000069567; ENSMUSG00000064177. [Q9EQX0-1]
GeneID58991.
KEGGmmu:58991.
UCSCuc009dhj.1. mouse. [Q9EQX0-2]
uc009dhl.1. mouse. [Q9EQX0-1]

Organism-specific databases

CTD51738.
MGIMGI:1930008. Ghrl.

Phylogenomic databases

eggNOGNOG45924.
GeneTreeENSGT00390000004064.
HOGENOMHOG000236303.
HOVERGENHBG018522.
InParanoidQ9EQX0.
KOK05254.
OMASLGTICS.
OrthoDBEOG741Z4K.
PhylomeDBQ9EQX0.
TreeFamTF336219.

Gene expression databases

BgeeQ9EQX0.
CleanExMM_GHRL.
GenevestigatorQ9EQX0.

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

ChiTaRSGHRL. mouse.
EvolutionaryTraceQ9EQX0.
NextBio314490.
PROQ9EQX0.
SOURCESearch...

Entry information

Entry nameGHRL_MOUSE
AccessionPrimary (citable) accession number: Q9EQX0
Secondary accession number(s): Q9WUZ1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 13, 2001
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 112 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot