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Protein

Appetite-regulating hormone

Gene

Ghrl

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hormone

Enzyme and pathway databases

ReactomeiREACT_319210. Peptide ligand-binding receptors.
REACT_330516. Synthesis, secretion, and deacylation of Ghrelin.
REACT_347934. G alpha (q) signalling events.

Names & Taxonomyi

Protein namesi
Recommended 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:
Gene namesi
Name:Ghrl
Synonyms:Mtlrp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1930008. Ghrl.

Subcellular locationi

GO - Cellular componenti

  • axon Source: UniProtKB
  • cytoplasm Source: MGI
  • cytosol Source: GOC
  • extracellular region Source: UniProtKB
  • extracellular space Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 23231 PublicationAdd
BLAST
Peptidei24 – 5128GhrelinPRO_0000019205Add
BLAST
Propeptidei52 – 7524Removed in mature formBy similarityPRO_0000019206Add
BLAST
Peptidei76 – 9823ObestatinPRO_0000045142Add
BLAST
Propeptidei99 – 11719Removed in mature formBy similarityPRO_0000045143Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi26 – 261O-decanoyl serine; alternate1 Publication
Lipidationi26 – 261O-octanoyl serine; alternate1 Publication
Modified residuei98 – 981Leucine amide1 Publication

Post-translational modificationi

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 (PubMed:15746259).By similarity1 Publication
Amidation of Leu-98 is essential for obestatin activity.By similarity

Keywords - PTMi

Amidation, Lipoprotein

Proteomic databases

MaxQBiQ9EQX0.
PaxDbiQ9EQX0.
PRIDEiQ9EQX0.

PTM databases

PhosphoSiteiQ9EQX0.

Expressioni

Tissue specificityi

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.1 Publication

Developmental stagei

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.1 Publication

Gene expression databases

BgeeiQ9EQX0.
CleanExiMM_GHRL.
ExpressionAtlasiQ9EQX0. baseline and differential.
GenevisibleiQ9EQX0. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000069567.

Structurei

Secondary structure

1
117
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi84 – 863Combined sources
Helixi87 – 904Combined sources
Beta strandi94 – 963Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JSHNMR-A76-98[»]
2JSINMR-A86-98[»]
2JSJNMR-A76-98[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9EQX0.

Family & Domainsi

Sequence similaritiesi

Belongs to the motilin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG45924.
GeneTreeiENSGT00390000004064.
HOGENOMiHOG000236303.
HOVERGENiHBG018522.
InParanoidiQ9EQX0.
KOiK05254.
OMAiEIQFNAP.
OrthoDBiEOG741Z4K.
PhylomeDBiQ9EQX0.
TreeFamiTF336219.

Family and domain databases

InterProiIPR006737. Motilin_assoc.
IPR006738. Motilin_ghrelin.
IPR005441. Preproghrelin.
[Graphical view]
PANTHERiPTHR14122. PTHR14122. 1 hit.
PfamiPF04643. Motilin_assoc. 1 hit.
PF04644. Motilin_ghrelin. 1 hit.
[Graphical view]
PRINTSiPR01624. GHRELIN.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9EQX0-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MLSSGTICSL LLLSMLWMDM AMAGSSFLSP EHQKAQQRKE SKKPPAKLQP
60 70 80 90 100
RALEGWLHPE DRGQAEETEE ELEIRFNAPF DVGIKLSGAQ YQQHGRALGK
110
FLQDILWEEV KEAPADK
Length:117
Mass (Da):13,207
Last modified:March 1, 2001 - v1
Checksum:iEACB49D2E3CA7203
GO
Isoform 2 (identifier: Q9EQX0-2) [UniParc]FASTAAdd to basket

Also known as: des-Gln14-ghrelin

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

Show »
Length:116
Mass (Da):13,079
Checksum:iE00DA3D67998B6B8
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei37 – 371Missing in isoform 2. 1 PublicationVSP_003246

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS20432.1. [Q9EQX0-1]
RefSeqiNP_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_006506446.2. [Q9EQX0-1]
UniGeneiMm.379095.

Genome annotation databases

EnsembliENSMUST00000064993; ENSMUSP00000069567; ENSMUSG00000064177. [Q9EQX0-1]
GeneIDi58991.
KEGGimmu:58991.
UCSCiuc009dhj.1. mouse. [Q9EQX0-2]
uc009dhl.2. mouse. [Q9EQX0-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Protein Spotlight

Gut feelings - Issue 66 of January 2006

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS20432.1. [Q9EQX0-1]
RefSeqiNP_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_006506446.2. [Q9EQX0-1]
UniGeneiMm.379095.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JSHNMR-A76-98[»]
2JSINMR-A86-98[»]
2JSJNMR-A76-98[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000069567.

PTM databases

PhosphoSiteiQ9EQX0.

Proteomic databases

MaxQBiQ9EQX0.
PaxDbiQ9EQX0.
PRIDEiQ9EQX0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000064993; ENSMUSP00000069567; ENSMUSG00000064177. [Q9EQX0-1]
GeneIDi58991.
KEGGimmu:58991.
UCSCiuc009dhj.1. mouse. [Q9EQX0-2]
uc009dhl.2. mouse. [Q9EQX0-1]

Organism-specific databases

CTDi51738.
MGIiMGI:1930008. Ghrl.

Phylogenomic databases

eggNOGiNOG45924.
GeneTreeiENSGT00390000004064.
HOGENOMiHOG000236303.
HOVERGENiHBG018522.
InParanoidiQ9EQX0.
KOiK05254.
OMAiEIQFNAP.
OrthoDBiEOG741Z4K.
PhylomeDBiQ9EQX0.
TreeFamiTF336219.

Enzyme and pathway databases

ReactomeiREACT_319210. Peptide ligand-binding receptors.
REACT_330516. Synthesis, secretion, and deacylation of Ghrelin.
REACT_347934. G alpha (q) signalling events.

Miscellaneous databases

ChiTaRSiGhrl. mouse.
EvolutionaryTraceiQ9EQX0.
NextBioi314490.
PROiQ9EQX0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9EQX0.
CleanExiMM_GHRL.
ExpressionAtlasiQ9EQX0. baseline and differential.
GenevisibleiQ9EQX0. MM.

Family and domain databases

InterProiIPR006737. Motilin_assoc.
IPR006738. Motilin_ghrelin.
IPR005441. Preproghrelin.
[Graphical view]
PANTHERiPTHR14122. PTHR14122. 1 hit.
PfamiPF04643. Motilin_assoc. 1 hit.
PF04644. Motilin_ghrelin. 1 hit.
[Graphical view]
PRINTSiPR01624. GHRELIN.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiGHRL_MOUSE
AccessioniPrimary (citable) accession number: Q9EQX0
Secondary accession number(s): Q9WUZ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 13, 2001
Last sequence update: March 1, 2001
Last modified: July 22, 2015
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.