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UniProtKB/Swiss-Prot entry Q9EQX0


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name GHRL_MOUSE
Primary accession number Q9EQX0
Secondary accession number Q9WUZ1
Integrated into Swiss-Prot on December 13, 2001
Sequence was last modified on March 1, 2001 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 72)
Name and origin of the protein
Protein name Appetite-regulating hormone [Precursor]
Synonyms Growth hormone secretagogue
Growth hormone-releasing peptide
Motilin-related peptide
Protein M46
Contains Ghrelin
Obestatin
Gene name
Name: Ghrl
Synonyms: Mtlrp
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 24-30, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Stomach;
PubMed=10930375 [NCBI, ExPASy, EBI, Israel, Japan]
Tomasetto C., Karam S.M., Ribieras S., Masson R., Lefebvre O., Staub A., Alexander G., Chenard M.-P., Rio M.-C.;
"Identification and characterization of a novel gastric peptide hormone: the motilin-related peptide.";
Gastroenterology 119:395-405(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Kojima M.;
"Mouse mRNA for preproghrelin.";
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
Tanaka M., Hayashida Y., Iguchi T., Nakao N., Nakai N., Nakashima K.;
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J;
TISSUE=Stomach;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
DEVELOPMENTAL STAGE, AND ACYLATION AT SER-26.
DOI=10.1210/en.2004-0645; PubMed=15746259 [NCBI, ExPASy, EBI, Israel, Japan]
Nishi Y., Hiejima H., Mifune H., Sato T., Kangawa K., Kojima M.;
"Developmental changes in the pattern of ghrelin's acyl modification and the levels of acyl-modified ghrelins in murine stomach.";
Endocrinology 146:2709-2715(2005).
[6]
REVIEW.
DOI=10.1016/S1043-2760(00)00362-3; PubMed=11306336 [NCBI, ExPASy, EBI, Israel, Japan]
Kojima M., Hosoda H., Matsuo H., Kangawa K.;
"Ghrelin: discovery of the natural endogenous ligand for the growth hormone secretagogue receptor.";
Trends Endocrinol. Metab. 12:118-122(2001).
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.
  • FUNCTION: 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.
  • ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.
    Name1
    SynonymsGhrelin
    Isoform IDQ9EQX0-1
    This is the isoform sequence displayed in this entry.
    Name2
    Synonymsdes-Gln14-ghrelin
    Isoform IDQ9EQX0-2
    Features which should be applied to build the isoform sequence: VSP_003246.
  • 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.
  • 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.
  • PTM: 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.
  • PTM: Amidation of Leu-98 is essential for obestatin activity (By similarity).
  • SIMILARITY: Belongs to the motilin family.
  • WEB RESOURCE: Name=Protein Spotlight; Note=Gut feelings - Issue 66 of January 2006; URL="http://www.expasy.org/spotlight/back_issues/sptlt066.shtml";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AJ243503; CAB46500.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB035701; BAB19046.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB060078; BAB69857.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK008658; BAB25814.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK008860; BAB25934.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00111663; -.
IPI00230764; -.
RefSeq NP_067463.2; -.
UniGene Mm.379095
3D structure databases
PDB
2JSH; NMR; -; A=76-98.[ExPASy / RCSB / EBI]
2JSI; NMR; -; A=86-98.[ExPASy / RCSB / EBI]
2JSJ; NMR; -; A=76-98.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2JSH; -.
2JSI; -.
2JSJ; -.
ModBase Q9EQX0.
PTM databases
PhosphoSite Q9EQX0; -.
Organism-specific databases
MGI MGI:1930008; Ghrl.
Gene expression databases
ArrayExpress Q9EQX0; -.
CleanEx MM_GHRL; -.
GermOnline ENSMUSG00000064177; Mus musculus.
Ontologies
GO
GO:0030424; Cellular component: axon (inferred from sequence or structural similarity from UniProtKB).
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from MGI).
GO:0005615; Cellular component: extracellular space (inferred from sequence or structural similarity from UniProtKB).
GO:0031768; Molecular function: ghrelin receptor binding (inferred from sequence or structural similarity from UniProtKB).
GO:0016608; Molecular function: growth hormone-releasing hormone activity (inferred from sequence or structural similarity from UniProtKB).
GO:0030296; Molecular function: protein tyrosine kinase activator activity (inferred from sequence or structural similarity from UniProtKB).
GO:0008154; Biological process: actin polymerization or depolymerization (inferred from sequence or structural similarity from UniProtKB).
GO:0000187; Biological process: activation of MAPK activity (inferred from sequence or structural similarity from UniProtKB).
GO:0046697; Biological process: decidualization (inferred from sequence or structural similarity from UniProtKB).
GO:0016358; Biological process: dendrite development (inferred from sequence or structural similarity from UniProtKB).
GO:0007204; Biological process: elevation of cytosolic calcium ion concentration (inferred from sequence or structural similarity from UniProtKB).
GO:0043066; Biological process: negative regulation of apoptosis (inferred from sequence or structural similarity from UniProtKB).
GO:0001937; Biological process: negative regulation of endothelial cell proliferation (inferred from sequence or structural similarity from UniProtKB).
GO:0050728; Biological process: negative regulation of inflammatory response (inferred from sequence or structural similarity from UniProtKB).
GO:0046676; Biological process: negative regulation of insulin secretion (inferred from sequence or structural similarity from UniProtKB).
GO:0032691; Biological process: negative regulation of interleukin-1 beta production (inferred from sequence or structural similarity from UniProtKB).
GO:0045409; Biological process: negative regulation of interleukin-6 biosynthetic process (inferred from sequence or structural similarity from UniProtKB).
GO:0040013; Biological process: negative regulation of locomotion (inferred from mutant phenotype from MGI).
GO:0042536; Biological process: negative regulation of tumor necrosis factor biosynthetic process (inferred from sequence or structural similarity from UniProtKB).
GO:0032100; Biological process: positive regulation of appetite (inferred from direct assay from MGI).
GO:0032024; Biological process: positive regulation of insulin secretion (inferred from sequence or structural similarity from UniProtKB).
GO:0051965; Biological process: positive regulation of synaptogenesis (inferred from sequence or structural similarity from UniProtKB).
GO:0060079; Biological process: regulation of excitatory postsynaptic membrane potential (inferred from mutant phenotype from MGI).
GO:0043627; Biological process: response to estrogen stimulus (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR006737; Motilin_assoc.
IPR006738; Motilin_ghrelin.
IPR005441; Preproghrelin.
Graphical view of domain structure.
PANTHER PTHR14122; Preproghrelin; 1.
Pfam PF04643; Motilin_assoc; 1.
PF04644; Motilin_ghrelin; 1.
Pfam graphical view of domain structure.
PRINTS PR01624; GHRELIN.
ProDom PD332162; Preproghrelin; 2.
[Domain structure / List of seq. sharing at least 1 domain]
Genome annotation databases
Ensembl ENSMUSG00000064177; Mus musculus. [Contig view]
GeneID 58991; -.
KEGG mmu:58991; -.
Phylogenomic databases
HOGENOM Q9EQX0; -.
HOVERGEN Q9EQX0; -.
OMA Q9EQX0; KLSGVQY.
Other
NextBio 314490; -.
SOURCE Ghrl; Mus musculus.
ProtoNet Q9EQX0.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Amidation; Direct protein sequencing; Hormone; Lipoprotein; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom  To Length Description FTId
SIGNAL   1    23  23      
PEPTIDE   24    51  28     Ghrelin. PRO_0000019205
PROPEP   52    75  24     Removed in mature form (By similarity). PRO_0000019206
PEPTIDE   76    98  23     Obestatin (By similarity). PRO_0000045142
PROPEP   99   117  19     Removed in mature form (By similarity). PRO_0000045143
MOD_RES   98    98        Leucine amide (By similarity). 
LIPID   26    26        O-decanoyl serine; alternate. 
LIPID   26    26        O-octanoyl serine; alternate. 
VAR_SEQ   37    37        Missing (in isoform 2). VSP_003246
Sequence information
Length: 117 AA [This is the length of the unprocessed precursor] Molecular weight: 13207 Da [This is the MW of the unprocessed precursor] CRC64: EACB49D2E3CA7203 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLSSGTICSL LLLSMLWMDM AMAGSSFLSP EHQKAQQRKE SKKPPAKLQP RALEGWLHPE 

        70         80         90        100        110 
DRGQAEETEE ELEIRFNAPF DVGIKLSGAQ YQQHGRALGK FLQDILWEEV KEAPADK 

Q9EQX0 in FASTA format

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