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Q9EQX0

- GHRL_MOUSE

UniProt

Q9EQX0 - GHRL_MOUSE

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Protein
Appetite-regulating hormone
Gene
Ghrl, Mtlrp
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.

GO - Molecular functioni

  1. ghrelin receptor binding Source: UniProtKB
  2. growth hormone-releasing hormone activity Source: UniProtKB
  3. hormone activity Source: UniProtKB
  4. protein tyrosine kinase activator activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. G-protein coupled receptor signaling pathway Source: Ensembl
  2. actin polymerization or depolymerization Source: UniProtKB
  3. activation of MAPK activity Source: UniProtKB
  4. adult feeding behavior Source: HGNC
  5. decidualization Source: UniProtKB
  6. dendrite development Source: UniProtKB
  7. gastric acid secretion Source: Ensembl
  8. negative regulation of apoptotic process Source: UniProtKB
  9. negative regulation of circadian sleep/wake cycle, REM sleep Source: Ensembl
  10. negative regulation of endothelial cell proliferation Source: UniProtKB
  11. negative regulation of inflammatory response Source: UniProtKB
  12. negative regulation of insulin secretion Source: UniProtKB
  13. negative regulation of interleukin-1 beta production Source: UniProtKB
  14. negative regulation of interleukin-6 biosynthetic process Source: UniProtKB
  15. negative regulation of locomotion Source: MGI
  16. negative regulation of tumor necrosis factor biosynthetic process Source: UniProtKB
  17. positive regulation of appetite Source: HGNC
  18. positive regulation of circadian sleep/wake cycle, non-REM sleep Source: Ensembl
  19. positive regulation of corticotropin secretion Source: Ensembl
  20. positive regulation of cortisol secretion Source: Ensembl
  21. positive regulation of cytosolic calcium ion concentration Source: UniProtKB
  22. positive regulation of growth hormone secretion Source: Ensembl
  23. positive regulation of insulin secretion Source: UniProtKB
  24. positive regulation of response to food Source: UniProtKB
  25. positive regulation of synapse assembly Source: UniProtKB
  26. regulation of cell proliferation Source: UniProtKB
  27. regulation of excitatory postsynaptic membrane potential Source: MGI
  28. regulation of response to food Source: UniProtKB
  29. response to estrogen Source: UniProtKB
  30. response to hormone Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hormone

Enzyme and pathway databases

ReactomeiREACT_207651. 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: Chromosome 6

Organism-specific databases

MGIiMGI:1930008. Ghrl.

Subcellular locationi

Secreted 1 Publication

GO - Cellular componenti

  1. axon Source: UniProtKB
  2. cytoplasm Source: MGI
  3. extracellular region Source: UniProtKB
  4. extracellular space Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 23231 Publication
Add
BLAST
Peptidei24 – 5128Ghrelin
PRO_0000019205Add
BLAST
Propeptidei52 – 7524Removed in mature form By similarity
PRO_0000019206Add
BLAST
Peptidei76 – 9823Obestatin
PRO_0000045142Add
BLAST
Propeptidei99 – 11719Removed in mature form By similarity
PRO_0000045143Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi26 – 261O-decanoyl serine; alternate
Lipidationi26 – 261O-octanoyl serine; alternate
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 (1 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.
GenevestigatoriQ9EQX0.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JSHNMR-A76-98[»]
2JSINMR-A86-98[»]
2JSJNMR-A76-98[»]

Miscellaneous databases

EvolutionaryTraceiQ9EQX0.

Family & Domainsi

Sequence similaritiesi

Belongs to the motilin family.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG45924.
GeneTreeiENSGT00390000004064.
HOGENOMiHOG000236303.
HOVERGENiHBG018522.
InParanoidiQ9EQX0.
KOiK05254.
OMAiSLGTICS.
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. Align

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

MLSSGTICSL LLLSMLWMDM AMAGSSFLSP EHQKAQQRKE SKKPPAKLQP    50
RALEGWLHPE DRGQAEETEE ELEIRFNAPF DVGIKLSGAQ YQQHGRALGK 100
FLQDILWEEV KEAPADK 117
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.
VSP_003246

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_006506446.1. [Q9EQX0-1]
UniGeneiMm.379095.

Genome annotation databases

EnsembliENSMUST00000064993; ENSMUSP00000069567; ENSMUSG00000064177. [Q9EQX0-1]
GeneIDi58991.
KEGGimmu:58991.
UCSCiuc009dhj.1. mouse. [Q9EQX0-2]
uc009dhl.1. 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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS20432.1. [Q9EQX0-1 ]
RefSeqi NP_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 ]
UniGenei Mm.379095.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2JSH NMR - A 76-98 [» ]
2JSI NMR - A 86-98 [» ]
2JSJ NMR - A 76-98 [» ]
ModBasei Search...

PTM databases

PhosphoSitei Q9EQX0.

Proteomic databases

MaxQBi Q9EQX0.
PaxDbi Q9EQX0.
PRIDEi Q9EQX0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000064993 ; ENSMUSP00000069567 ; ENSMUSG00000064177 . [Q9EQX0-1 ]
GeneIDi 58991.
KEGGi mmu:58991.
UCSCi uc009dhj.1. mouse. [Q9EQX0-2 ]
uc009dhl.1. mouse. [Q9EQX0-1 ]

Organism-specific databases

CTDi 51738.
MGIi MGI:1930008. Ghrl.

Phylogenomic databases

eggNOGi NOG45924.
GeneTreei ENSGT00390000004064.
HOGENOMi HOG000236303.
HOVERGENi HBG018522.
InParanoidi Q9EQX0.
KOi K05254.
OMAi SLGTICS.
OrthoDBi EOG741Z4K.
PhylomeDBi Q9EQX0.
TreeFami TF336219.

Enzyme and pathway databases

Reactomei REACT_207651. G alpha (q) signalling events.

Miscellaneous databases

ChiTaRSi GHRL. mouse.
EvolutionaryTracei Q9EQX0.
NextBioi 314490.
PROi Q9EQX0.
SOURCEi Search...

Gene expression databases

Bgeei Q9EQX0.
CleanExi MM_GHRL.
Genevestigatori Q9EQX0.

Family and domain databases

InterProi IPR006737. Motilin_assoc.
IPR006738. Motilin_ghrelin.
IPR005441. Preproghrelin.
[Graphical view ]
PANTHERi PTHR14122. PTHR14122. 1 hit.
Pfami PF04643. Motilin_assoc. 1 hit.
PF04644. Motilin_ghrelin. 1 hit.
[Graphical view ]
PRINTSi PR01624. GHRELIN.
ProtoNeti Search...

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: September 3, 2014
This is version 113 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

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