Ghrelin/MTLRP

Identity

Other names	Motilin-related peptide (MTLRP)
HGNC	GHRL
Location	3p26-p25

DNA/RNA

Transcription

600 bp, two mRNAs are encoded by the same genes, they are identical except for the lack of one codon (CAG) located at an exon intron boundary.

Protein

Description	two precursor s of 117 and 116 amino acids encoding preproGhrelin/MTLRP and prepro-des-Gln14-Ghrelin/ delta Gln14 MTLRP, respectively. The 28 amino-acids Ghrelin/MTLRP and the 27 amino-acids des-Gln14-Ghrelin/delta Gln14 MTLRP are modified post-translationally by the addition of a n-octanoic acid on Serine 3. The 28 amino acids Ghrelin/MTLRP is produced from a protein precursor of 117 residues that contains a signal peptide from residues 1to 23, the ghrelin/MTLRP moity from residues 24 to 51, the MTLRP-associated peptide moity from residues 52 to 117. The 27 amino acids des-Gln14-Ghrelin/delta Gln 14 MTLRP is produced from a protein precursor of 116 residues identical to the 117 aa precursor excep that the des-Gln14-Ghrelin/delta Gln14 MTLRP moity corresponds to residues 24 to 50 and accordingly the MTLRP-associated peptide moity from resisues 51 to 116.
Expression	Ghrelin/MTLRP is mainly expressed by the enteroendocrine cells of the stomach; its expression decreased gradually along the gastro-intestinal tract and a faint expression was also detected in testis. By Immnunochemistry Ghrelin-immuno reactive neurons were found in the hypothalamic arcuate nucleus.
Localisation	As a peptide hormone Ghrelin/MTLRP is secreted in the blood.
Function	As the endogenous ligand of the growth hormone secretagogues (GHS) receptor, Ghrelin/MTLRP is involved in the pulsatile secretion of Growth hormone. In addition to this role Ghrelin/MTLRP is in the regulation of feeding. In rodent In contrast to leptin, Ghrelin/MTLRP promotes food intake and obesity. In addition Ghrelin/MTLRP stimulates motricity of the gastrointestinal tract and acid secretion.
Homology	ppGhrelin/MTLRP share 47% of similarity with the precursor of Motilin. In addition Ghrelin receptor (GHS-R) and Motilin receptor (GPR38) share 52% identity.

External links

	Nomenclature
HGNC	GHRL   18129
Entrez_Gene	GHRL  51738  ghrelin/obestatin prepropeptide
	Cards
Atlas	GhrelinID327
GeneCards	GHRL
Ensembl	GHRL [Search_View]   ENSG00000157017 [Gene_View]
Genatlas	GHRL
GeneLynx	GHRL
eGenome	GHRL
euGene	51738
	Genomic and cartography
GoldenPath	GHRL  -     chr3:10302434-10307409 -  3p26-p25   [Description]    (hg18-Mar_2006)
Ensembl	GHRL - 3p26-p25 [CytoView]
NCBI	Mapview
OMIM	Disease map [OMIM]
HomoloGene	GHRL
	Gene and transcription
Genbank	AB029434 [ ENTREZ ]
Genbank	AB035700 [ ENTREZ ]
Genbank	AJ252278 [ ENTREZ ]
Genbank	AY184207 [ ENTREZ ]
Genbank	AY359053 [ ENTREZ ]
RefSeq	NM_016362 [ SRS ]    NM_016362 [ ENTREZ ]
RefSeq	AC_000046 [ SRS ]    AC_000046 [ ENTREZ ]
RefSeq	AC_000135 [ SRS ]    AC_000135 [ ENTREZ ]
RefSeq	NC_000003 [ SRS ]    NC_000003 [ ENTREZ ]
RefSeq	NT_022517 [ SRS ]    NT_022517 [ ENTREZ ]
RefSeq	NW_001838876 [ SRS ]    NW_001838876 [ ENTREZ ]
RefSeq	NW_921651 [ SRS ]    NW_921651 [ ENTREZ ]
AceView	GHRL AceView - NCBI
Unigene	Hs.590080 [ SRS ]    Hs.590080 [ NCBI ]     HS590080 [ spliceNest ]
Fast-db	1898 (alternative variants)
	Protein : pattern, domain, 3D structure
SwissProt	Q5Y392 [ SRS]    Q5Y392 [ EXPASY ]     Q5Y392 [ INTERPRO ]     Q5Y392 [ UNIPROT ]
Interpro	IPR005441 Preproghrelin [ SRS ]    IPR005441 Preproghrelin [ EBI ]
CluSTr	Q5Y392
Prodom	PD332162 Preproghrelin[INRA-Toulouse]
Prodom	Q5Y392 Q5Y392_HUMAN [ Domain structure ]   Q5Y392 Q5Y392_HUMAN  [ sequences sharing at least 1 domain ]
Blocks	Q5Y392
HPRD	05638
	Protein Interaction databases
DIP	Q5Y392
IntAct	Q5Y392
	Polymorphism : SNP, mutations, diseases
OMIM	601665;605353    [ map ]
GENECLINICS	601665;605353
SNP	GHRL [dbSNP-NCBI]
SNP	NM_016362 [SNP-NCI]
SNP	GHRL [GeneSNPs - Utah]  GHRL] [HGBASE - SRS]
HAPMAP	GHRL [HAPMAP]
HGMD	GHRL
	General knowledge
Family Browser	GHRL [UCSC Family Browser]
SOURCE	NM_016362
SMD	Hs.590080
SAGE	Hs.590080
GO	activation of MAPK activity [Amigo]  activation of MAPK activity
GO	negative regulation of endothelial cell proliferation [Amigo]  negative regulation of endothelial cell proliferation
GO	extracellular region [Amigo]  extracellular region
GO	extracellular region [Amigo]  extracellular region
GO	extracellular space [Amigo]  extracellular space
GO	cytoplasm [Amigo]  cytoplasm
GO	glucose metabolic process [Amigo]  glucose metabolic process
GO	G-protein coupled receptor protein signaling pathway [Amigo]  G-protein coupled receptor protein signaling pathway
GO	elevation of cytosolic calcium ion concentration [Amigo]  elevation of cytosolic calcium ion concentration
GO	actin polymerization and/or depolymerization [Amigo]  actin polymerization and/or depolymerization
GO	adult feeding behavior [Amigo]  adult feeding behavior
GO	hormone-mediated signaling [Amigo]  hormone-mediated signaling
GO	dendrite development [Amigo]  dendrite development
GO	negative regulation of angiogenesis [Amigo]  negative regulation of angiogenesis
GO	growth hormone-releasing hormone activity [Amigo]  growth hormone-releasing hormone activity
GO	growth hormone-releasing hormone activity [Amigo]  growth hormone-releasing hormone activity
GO	growth hormone secretion [Amigo]  growth hormone secretion
GO	protein tyrosine kinase activator activity [Amigo]  protein tyrosine kinase activator activity
GO	axon [Amigo]  axon
GO	ghrelin receptor binding [Amigo]  ghrelin receptor binding
GO	positive regulation of insulin secretion [Amigo]  positive regulation of insulin secretion
GO	positive regulation of appetite [Amigo]  positive regulation of appetite
GO	negative regulation of interleukin-1 beta production [Amigo]  negative regulation of interleukin-1 beta production
GO	negative regulation of locomotion [Amigo]  negative regulation of locomotion
GO	positive regulation of multicellular organism growth [Amigo]  positive regulation of multicellular organism growth
GO	regulation of cell proliferation [Amigo]  regulation of cell proliferation
GO	negative regulation of tumor necrosis factor biosynthetic process [Amigo]  negative regulation of tumor necrosis factor biosynthetic process
GO	negative regulation of apoptosis [Amigo]  negative regulation of apoptosis
GO	cortisol secretion [Amigo]  cortisol secretion
GO	response to estrogen stimulus [Amigo]  response to estrogen stimulus
GO	negative regulation of interleukin-6 biosynthetic process [Amigo]  negative regulation of interleukin-6 biosynthetic process
GO	negative regulation of insulin secretion [Amigo]  negative regulation of insulin secretion
GO	decidualization [Amigo]  decidualization
GO	negative regulation of inflammatory response [Amigo]  negative regulation of inflammatory response
GO	cartilage development [Amigo]  cartilage development
GO	positive regulation of synaptogenesis [Amigo]  positive regulation of synaptogenesis
GO	regulation of excitatory postsynaptic membrane potential [Amigo]  regulation of excitatory postsynaptic membrane potential
BIOCARTA	Ghrelin: Regulation of Food Intake and Energy Homeostasis    [Genes]
KEGG	Neuroactive ligand-receptor interaction
PubGene	GHRL
TreeFam	GHRL
CTD	51738 [Comparative ToxicoGenomics Database]
	Other databases
	Probes
Probe	Cancer Cytogenetics (Bari)
Probe	GHRL Related clones (RZPD - Berlin)
	PubMed
PubMed	297 Pubmed reference(s) in LocusLink

Bibliography

Ghrelin is a growth-hormone-releasing acylated peptide from stomach.

Kojima M, Hosoda H, Date Y, Nakazato M, Matsuo H, Kangawa K

Nature. 1999 ; 402 (6762) : 656-660.

PMID 10604470

Purification and characterization of rat des-Gln14-Ghrelin, a second endogenous ligand for the growth hormone secretagogue receptor.

Hosoda H, Kojima M, Matsuo H, Kangawa K

The Journal of biological chemistry. 2000 ; 275 (29) : 21995-22000.

PMID 10801861

Ghrelin stimulates gastric acid secretion and motility in rats.

Masuda Y, Tanaka T, Inomata N, Ohnuma N, Tanaka S, Itoh Z, Hosoda H, Kojima M, Kangawa K

Biochemical and biophysical research communications. 2000 ; 276 (3) : 905-908.

PMID 11027567

Identification and characterization of a novel gastric peptide hormone: the motilin-related peptide.

Tomasetto C, Karam SM, Ribieras S, Masson R, LefˆŽbvre O, Staub A, Alexander G, Chenard MP, Rio MC

Gastroenterology. 2000 ; 119 (2) : 395-405.

PMID 10930375

Ghrelin induces adiposity in rodents.

Tschˆp M, Smiley DL, Heiman ML

Nature. 2000 ; 407 (6806) : 908-913.

PMID 11057670

The novel hypothalamic peptide ghrelin stimulates food intake and growth hormone secretion.

Wren AM, Small CJ, Ward HL, Murphy KG, Dakin CL, Taheri S, Kennedy AR, Roberts GH, Morgan DG, Ghatei MA, Bloom SR

Endocrinology. 2000 ; 141 (11) : 4325-4328.

PMID 11089570

A role for ghrelin in the central regulation of feeding.

Nakazato M, Murakami N, Date Y, Kojima M, Matsuo H, Kangawa K, Matsukura S

Nature. 2001 ; 409 (6817) : 194-198.

PMID 11196643

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Contributor(s)

Written	03-2001	Catherine Tomasetto

Citation

This paper should be referenced as such :

Tomasetto C . Ghrelin/MTLRP. Atlas Genet Cytogenet Oncol Haematol. March 2001 . URL : http://AtlasGeneticsOncology.org/Genes/GhrelinID327.html

© Atlas of Genetics and Cytogenetics in Oncology and Haematology

indexed on : Mon Aug 11 21:14:15 2008