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Appetite-regulating hormone (Growth hormone secretagogue) (Growth hormone-releasing peptide) (Motilin-related peptide) [Cleaved into: Ghrelin; Obestatin-23; Obestatin-13]

 GHRL_RAT                Reviewed;         117 AA.
Q9QYH7; Q9ET69;
13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
27-SEP-2017, entry version 130.
RecName: Full=Appetite-regulating hormone;
AltName: Full=Growth hormone secretagogue;
AltName: Full=Growth hormone-releasing peptide;
AltName: Full=Motilin-related peptide;
Contains:
RecName: Full=Ghrelin;
Contains:
RecName: Full=Obestatin-23;
Contains:
RecName: Full=Obestatin-13;
Flags: Precursor;
Name=Ghrl;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 24-51,
MASS SPECTROMETRY, AND ACYLATION AT SER-26.
STRAIN=Sprague-Dawley; TISSUE=Stomach;
PubMed=10604470; DOI=10.1038/45230;
Kojima M., Hosoda H., Date Y., Nakazato M., Matsuo H., Kangawa K.;
"Ghrelin is a growth-hormone-releasing acylated peptide from
stomach.";
Nature 402:656-660(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF
24-51, MASS SPECTROMETRY, AND ACYLATION AT SER-26.
STRAIN=Sprague-Dawley; TISSUE=Stomach;
PubMed=10801861; DOI=10.1074/jbc.M002784200;
Hosoda H., Kojima M., Matsuo H., Kangawa K.;
"Purification and characterization of rat des-Gln14-ghrelin, a second
endogenous ligand for the growth hormone secretagogue receptor.";
J. Biol. Chem. 275:21995-22000(2000).
[3]
PROTEIN SEQUENCE OF 76-95, FUNCTION OF OBESTATIN, CHARACTERIZATION,
AMIDATION AT LEU-98, MASS SPECTROMETRY, AND INTERACTION WITH GPR39.
PubMed=16284174; DOI=10.1126/science.1117255;
Zhang J.V., Ren P.G., Avsian-Kretchmer O., Luo C.W., Rauch R.,
Klein C., Hsueh A.J.;
"Obestatin, a peptide encoded by the ghrelin gene, opposes ghrelin's
effects on food intake.";
Science 310:996-999(2005).
[4]
TISSUE SPECIFICITY.
PubMed=11162448; DOI=10.1006/bbrc.2000.4039;
Hosoda H., Kojima M., Matsuo H., Kangawa K.;
"Ghrelin and des-acyl ghrelin: two major forms of rat ghrelin peptide
in gastrointestinal tissue.";
Biochem. Biophys. Res. Commun. 279:909-913(2000).
[5]
STRUCTURE-ACTIVITY RELATIONSHIP.
PubMed=11549267; DOI=10.1006/bbrc.2001.5553;
Matsumoto M., Hosoda H., Kitajima Y., Morozumi N., Minamitake Y.,
Tanaka S., Matsuo H., Kojima M., Hayashi Y., Kangawa K.;
"Structure-activity relationship of ghrelin: pharmacological study of
ghrelin peptides.";
Biochem. Biophys. Res. Commun. 287:142-146(2001).
[6]
REVIEW.
PubMed=11306336; DOI=10.1016/S1043-2760(00)00362-3;
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).
[7]
FUNCTION OF OBESTATIN.
PubMed=17289961; DOI=10.1126/science.1135047;
Chartrel N., Alvear-Perez R., Leprince J., Iturrioz X.,
Reaux-Le Goazigo A., Audinot V., Chomarat P., Coge F., Nosjean O.,
Rodriguez M., Galizzi J.P., Boutin J.A., Vaudry H., Llorens-Cortes C.;
"Comment on 'Obestatin, a peptide encoded by the ghrelin gene, opposes
ghrelin's effects on food intake'.";
Science 315:766-766(2007).
-!- 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.
-!- SUBCELLULAR LOCATION: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Ghrelin;
IsoId=Q9QYH7-1; Sequence=Displayed;
Name=2; Synonyms=des-Gln14-ghrelin;
IsoId=Q9QYH7-2; Sequence=VSP_003248;
-!- TISSUE SPECIFICITY: Ghrelin is broadly expressed with higher
expression in the stomach. Very low levels are detected in the
hypothalamus, heart, lung, pancreas, intestine and adipose tissue.
Obestatin is most highly expressed in jejunum, and also found in
duodenum, stomach, pituitary, ileum, liver, hypothalamus and
heart. Expressed in low levels in pancreas, cerebellum, cerebrum,
kidney, testis, ovary colon and lung.
{ECO:0000269|PubMed:11162448}.
-!- PTM: O-octanoylation is essential for ghrelin activity. The
replacement of Ser-26 by aromatic tryptophan preserves ghrelin
activity (PubMed:10604470, PubMed:10801861).
{ECO:0000269|PubMed:10604470, ECO:0000269|PubMed:10801861}.
-!- PTM: Amidation of Leu-98 is essential for obestatin activity.
{ECO:0000269|PubMed:16284174}.
-!- MASS SPECTROMETRY: Mass=3314.9; Mass_error=0.7;
Method=Electrospray; Range=24-51 (Q9QYH7-1);
Evidence={ECO:0000269|PubMed:10604470};
-!- MASS SPECTROMETRY: Mass=3187.1; Mass_error=0.6;
Method=Electrospray; Range=24-50 (Q9QYH7-2);
Evidence={ECO:0000269|PubMed:10801861};
-!- MASS SPECTROMETRY: Mass=2516.3; Method=Unknown; Range=76-98;
Evidence={ECO:0000269|PubMed:16284174};
-!- SIMILARITY: Belongs to the motilin family. {ECO:0000305}.
-!- CAUTION: PubMed:16284174 reports obestatin as ligand of GPR39.
However, PubMed:17289961 and others are unable to reproduce these
results. It also seems to be unclear whether obestatin has
opposite effects on food intake compared with ghrelin.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Protein Spotlight; Note=Gut feelings - Issue 66
of January 2006;
URL="http://web.expasy.org/spotlight/back_issues/066";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB029433; BAA89370.1; -; mRNA.
EMBL; AB035699; BAB11956.1; -; mRNA.
PIR; B59316; B59316.
RefSeq; NP_067701.1; NM_021669.2. [Q9QYH7-1]
UniGene; Rn.42103; -.
STRING; 10116.ENSRNOP00000014103; -.
iPTMnet; Q9QYH7; -.
PhosphoSitePlus; Q9QYH7; -.
PaxDb; Q9QYH7; -.
Ensembl; ENSRNOT00000014103; ENSRNOP00000014103; ENSRNOG00000010349. [Q9QYH7-1]
GeneID; 59301; -.
KEGG; rno:59301; -.
UCSC; RGD:632283; rat. [Q9QYH7-1]
CTD; 51738; -.
RGD; 632283; Ghrl.
eggNOG; ENOG410IZYV; Eukaryota.
eggNOG; ENOG410ZG1B; LUCA.
GeneTree; ENSGT00390000004064; -.
HOGENOM; HOG000236303; -.
HOVERGEN; HBG018522; -.
InParanoid; Q9QYH7; -.
KO; K05254; -.
OMA; EIQFNAP; -.
OrthoDB; EOG091G0YG0; -.
PhylomeDB; Q9QYH7; -.
TreeFam; TF336219; -.
Reactome; R-RNO-375276; Peptide ligand-binding receptors.
Reactome; R-RNO-416476; G alpha (q) signalling events.
Reactome; R-RNO-422085; Synthesis, secretion, and deacylation of Ghrelin.
PRO; PR:Q9QYH7; -.
Proteomes; UP000002494; Chromosome 4.
Bgee; ENSRNOG00000010349; -.
Genevisible; Q9QYH7; RN.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
GO; GO:0098794; C:postsynapse; IEA:GOC.
GO; GO:0001664; F:G-protein coupled receptor binding; IPI:UniProtKB.
GO; GO:0031768; F:ghrelin receptor binding; IMP:RGD.
GO; GO:0016608; F:growth hormone-releasing hormone activity; IDA:UniProtKB.
GO; GO:0005179; F:hormone activity; IDA:RGD.
GO; GO:0030296; F:protein tyrosine kinase activator activity; ISS:UniProtKB.
GO; GO:0008154; P:actin polymerization or depolymerization; ISS:UniProtKB.
GO; GO:0000187; P:activation of MAPK activity; ISS:UniProtKB.
GO; GO:0008343; P:adult feeding behavior; ISS:HGNC.
GO; GO:0046697; P:decidualization; ISS:UniProtKB.
GO; GO:0016358; P:dendrite development; IEA:Ensembl.
GO; GO:0060079; P:excitatory postsynaptic potential; IEA:Ensembl.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IDA:UniProtKB.
GO; GO:0001696; P:gastric acid secretion; IDA:UniProtKB.
GO; GO:0035483; P:gastric emptying; IDA:RGD.
GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0042322; P:negative regulation of circadian sleep/wake cycle, REM sleep; IEA:Ensembl.
GO; GO:0001937; P:negative regulation of endothelial cell proliferation; ISS:UniProtKB.
GO; GO:2000506; P:negative regulation of energy homeostasis; IEA:Ensembl.
GO; GO:0050728; P:negative regulation of inflammatory response; ISS:UniProtKB.
GO; GO:0046676; P:negative regulation of insulin secretion; IDA:MGI.
GO; GO:0032691; P:negative regulation of interleukin-1 beta production; IDA:RGD.
GO; GO:0045409; P:negative regulation of interleukin-6 biosynthetic process; ISS:UniProtKB.
GO; GO:0040013; P:negative regulation of locomotion; IEA:Ensembl.
GO; GO:0042536; P:negative regulation of tumor necrosis factor biosynthetic process; ISS:UniProtKB.
GO; GO:1904468; P:negative regulation of tumor necrosis factor secretion; IDA:RGD.
GO; GO:1904179; P:positive regulation of adipose tissue development; IDA:RGD.
GO; GO:0032100; P:positive regulation of appetite; IMP:RGD.
GO; GO:1903012; P:positive regulation of bone development; IDA:RGD.
GO; GO:0046010; P:positive regulation of circadian sleep/wake cycle, non-REM sleep; IEA:Ensembl.
GO; GO:0051461; P:positive regulation of corticotropin secretion; IEA:Ensembl.
GO; GO:0051464; P:positive regulation of cortisol secretion; IEA:Ensembl.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:UniProtKB.
GO; GO:1904000; P:positive regulation of eating behavior; IDA:RGD.
GO; GO:2000507; P:positive regulation of energy homeostasis; IEA:Ensembl.
GO; GO:2000253; P:positive regulation of feeding behavior; IDA:RGD.
GO; GO:1904346; P:positive regulation of gastric mucosal blood circulation; IDA:RGD.
GO; GO:1904306; P:positive regulation of gastro-intestinal system smooth muscle contraction; IDA:RGD.
GO; GO:0045927; P:positive regulation of growth; IDA:RGD.
GO; GO:0060124; P:positive regulation of growth hormone secretion; IDA:CACAO.
GO; GO:0040010; P:positive regulation of growth rate; IDA:RGD.
GO; GO:0032024; P:positive regulation of insulin secretion; IDA:UniProtKB.
GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IDA:RGD.
GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IBA:GO_Central.
GO; GO:0032097; P:positive regulation of response to food; IDA:RGD.
GO; GO:0120058; P:positive regulation of small intestinal transit; IDA:RGD.
GO; GO:1904349; P:positive regulation of small intestine smooth muscle contraction; IDA:RGD.
GO; GO:1903672; P:positive regulation of sprouting angiogenesis; IDA:RGD.
GO; GO:0051965; P:positive regulation of synapse assembly; IEA:Ensembl.
GO; GO:1905564; P:positive regulation of vascular endothelial cell proliferation; IDA:RGD.
GO; GO:0042127; P:regulation of cell proliferation; ISS:UniProtKB.
GO; GO:1905333; P:regulation of gastric motility; IDA:RGD.
GO; GO:0032095; P:regulation of response to food; IDA:RGD.
GO; GO:0051969; P:regulation of transmission of nerve impulse; IDA:RGD.
GO; GO:0051602; P:response to electrical stimulus; IEP:RGD.
GO; GO:0043627; P:response to estrogen; ISS:UniProtKB.
GO; GO:0009725; P:response to hormone; ISS:UniProtKB.
GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
InterPro; IPR006737; Motilin_assoc.
InterPro; IPR006738; Motilin_ghrelin.
InterPro; IPR005441; Preproghrelin.
PANTHER; PTHR14122; PTHR14122; 1.
Pfam; PF04643; Motilin_assoc; 1.
Pfam; PF04644; Motilin_ghrelin; 1.
PRINTS; PR01624; GHRELIN.
1: Evidence at protein level;
Alternative splicing; Amidation; Complete proteome;
Direct protein sequencing; Hormone; Lipoprotein; Reference proteome;
Secreted; Signal.
SIGNAL 1 23 {ECO:0000269|PubMed:10604470,
ECO:0000269|PubMed:10801861}.
PEPTIDE 24 51 Ghrelin.
/FTId=PRO_0000019209.
PROPEP 52 75 Removed in mature form.
{ECO:0000269|PubMed:16284174}.
/FTId=PRO_0000019210.
PEPTIDE 76 98 Obestatin-23.
/FTId=PRO_0000045146.
PEPTIDE 86 98 Obestatin-13. {ECO:0000305}.
/FTId=PRO_0000045147.
PROPEP 99 117 Removed in mature form.
/FTId=PRO_0000045148.
MOD_RES 98 98 Leucine amide.
{ECO:0000269|PubMed:16284174}.
LIPID 26 26 O-octanoyl serine.
{ECO:0000269|PubMed:10604470,
ECO:0000269|PubMed:10801861}.
VAR_SEQ 37 37 Missing (in isoform 2).
{ECO:0000303|PubMed:10801861}.
/FTId=VSP_003248.
SEQUENCE 117 AA; 13176 MW; 8857546FE51A7691 CRC64;
MVSSATICSL LLLSMLWMDM AMAGSSFLSP EHQKAQQRKE SKKPPAKLQP RALEGWLHPE
DRGQAEEAEE ELEIRFNAPF DVGIKLSGAQ YQQHGRALGK FLQDILWEEV KEAPANK


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