Appetite-regulating hormone precursor

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Alternative products

Sequence annotation (Features)

Sequences

References

Web resources

Cross-references

Entry information

Relevant documents

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Alternative products

Sequence annotation (Features)

Sequences

References

Web resources

Cross-references

Entry information

Relevant documents

Cleaved into the following 2 chains:

Molecule processing

Amino acid modifications

Natural variations

Secondary structure

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Preferred order of sections

Cleaved into the following 2 chains:

Molecule processing

Amino acid modifications

Natural variations

Secondary structure

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

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Q9EQX0 (GHRL_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 101. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents Customize order

Protein names

Recommended name:
Appetite-regulating hormone

Alternative name(s):
Growth hormone secretagogue
Growth hormone-releasing peptide
Motilin-related peptide
Protein M46

Ghrelin
Obestatin

Gene names

Name:	Ghrl
Synonyms:	Mtlrp

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Sequence length	117 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

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. Amidation of Leu-98 is essential for obestatin activity By similarity.
Sequence similarities	Belongs to the motilin family.

Keywords
Cellular component	Secreted
Coding sequence diversity	Alternative splicing
Domain	Signal
Molecular function	Hormone
PTM	Amidation Lipoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	G-protein coupled receptor signaling pathway Inferred from electronic annotation. Source: Compara 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 elevation of cytosolic calcium ion concentration Inferred from sequence or structural similarity. Source: UniProtKB gastric acid secretion Inferred from electronic annotation. Source: Compara 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: Compara 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: Compara positive regulation of corticotropin secretion Inferred from electronic annotation. Source: Compara positive regulation of cortisol secretion Inferred from electronic annotation. Source: Compara positive regulation of growth hormone secretion Inferred from electronic annotation. Source: Compara positive regulation of insulin secretion Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of synapse assembly Inferred from sequence or structural similarity. Source: UniProtKB regulation of excitatory postsynaptic membrane potential Inferred from mutant phenotype PubMed 16491079. Source: MGI response to estrogen stimulus Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	axon Inferred from sequence or structural similarity. Source: UniProtKB cytoplasm Inferred from direct assay Ref.1. Source: MGI extracellular space Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ghrelin receptor binding Inferred from sequence or structural similarity. Source: UniProtKB growth hormone-releasing 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...

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Signal peptide

1 – 23

Ref.1

Peptide

24 – 51

Ghrelin

PRO_0000019205

Propeptide

52 – 75

Removed in mature form By similarity

PRO_0000019206

Peptide

76 – 98

Obestatin

PRO_0000045142

Propeptide

99 – 117

Removed in mature form By similarity

PRO_0000045143

Modified residue

Leucine amide Ref.7

Lipidation

O-decanoyl serine; alternate

Lipidation

O-octanoyl serine; alternate

Alternative sequence

Missing in isoform 2.

VSP_003246

117

Helix Strand Turn

Details...

Sequence		Length	Mass (Da)
Isoform 1 (Ghrelin) [UniParc]. Last modified March 1, 2001. Version 1. Checksum: EACB49D2E3CA7203 Show »	FASTA	117	13,207
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 »	FASTA	116	13,079
10 20 30 40 50 60 MLSSGTICSL LLLSMLWMDM AMAGSSFLSP EHQKAQRKES KKPPAKLQPR ALEGWLHPED 70 80 90 100 110 RGQAEETEEE LEIRFNAPFD VGIKLSGAQY QQHGRALGKF LQDILWEEVK EAPADK « Hide

	« Hide 'large scale' referencesShow '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. 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.

Protein Spotlight

Gut feelings - Issue 66 of January 2006

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.

IPI

IPI00111663.
IPI00230764.

RefSeq

NP_067463.2. NM_021488.4.

UniGene

Mm.379095.

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2JSH	NMR	-	A	76-98	[»]
2JSI	NMR	-	A	86-98	[»]
2JSJ	NMR	-	A	76-98	[»]

ModBase

Search...

PhosphoSite

Q9EQX0.

PaxDb

Q9EQX0.

PRIDE

Q9EQX0.

StructuralBiologyKnowledgebase

Search...

Ensembl

ENSMUST00000064993; ENSMUSP00000069567; ENSMUSG00000064177.

GeneID

58991.

KEGG

mmu:58991.

UCSC

uc009dhj.1. mouse.

CTD

51738.

MGI

MGI:1930008. Ghrl.

eggNOG

NOG45924.

GeneTree

ENSGT00390000004064.

HOGENOM

HOG000236303.

HOVERGEN

HBG018522.

InParanoid

Q9EQX0.

K05254.

OMA

AQYQQHG.

ArrayExpress

Q9EQX0.

Bgee

Q9EQX0.

CleanEx

MM_GHRL.

Genevestigator

Q9EQX0.

GermOnline

ENSMUSG00000064177. Mus musculus.

InterPro

IPR006737. Motilin_assoc.
IPR006738. Motilin_ghrelin.
IPR005441. Preproghrelin.
[Graphical view]

PANTHER

PTHR14122. PTHR14122. 1 hit.

Pfam

PF04643. Motilin_assoc. 1 hit.
PF04644. Motilin_ghrelin. 1 hit.
[Graphical view]

PRINTS

PR01624. GHRELIN.

ProtoNet

Search...

ChiTaRS

GHRL. mouse.

EvolutionaryTrace

Q9EQX0.

NextBio

314490.

SOURCE

Search...

Entry name

GHRL_MOUSE

Accession

Primary (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:	April 3, 2013
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

MGD cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents

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.