GHRL_FELCA
ID GHRL_FELCA Reviewed; 117 AA.
AC Q6BEG6; Q6BEG5;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Appetite-regulating hormone;
DE AltName: Full=Growth hormone secretagogue;
DE AltName: Full=Growth hormone-releasing peptide;
DE AltName: Full=Motilin-related peptide;
DE Contains:
DE RecName: Full=Ghrelin;
DE Contains:
DE RecName: Full=Obestatin;
DE Flags: Precursor;
GN Name=GHRL;
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INDUCTION, ACYLATION AT
RP SER-26, AND MASS SPECTROMETRY.
RC TISSUE=Stomach;
RX PubMed=16466902; DOI=10.1016/j.domaniend.2006.01.002;
RA Ida T., Miyazato M., Naganobu K., Nakahara K., Sato M., Lin X.Z., Kaiya H.,
RA Doi K., Noda S., Kubo A., Murakami N., Kangawa K.;
RT "Purification and characterization of feline ghrelin and its possible
RT role.";
RL Domest. Anim. Endocrinol. 32:93-105(2007).
CC -!- FUNCTION: [Ghrelin]: Ghrelin is the ligand for growth hormone
CC secretagogue receptor type 1 (GHSR). Induces the release of growth
CC hormone from the pituitary. Has an appetite-stimulating effect, induces
CC adiposity and stimulates gastric acid secretion. Involved in growth
CC regulation (By similarity). {ECO:0000250}.
CC -!- FUNCTION: [Obestatin]: Obestatin may be the ligand for GPR39. May have
CC an appetite-reducing effect resulting in decreased food intake. May
CC reduce gastric emptying activity and jejunal motility (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Ghrelin;
CC IsoId=Q6BEG6-1; Sequence=Displayed;
CC Name=2; Synonyms=des-Gln14-ghrelin;
CC IsoId=Q6BEG6-2; Sequence=VSP_011626;
CC -!- INDUCTION: 2.5-fold increase in plasma level of ghrelin upon fasting.
CC {ECO:0000269|PubMed:16466902}.
CC -!- PTM: O-octanoylated by GOAT/MBOAT4 (By similarity). O-octanoylation or
CC O-decanoylation is essential for ghrelin activity. The O-decanoylated
CC forms Ghrelin-27-C10 and Ghrelin-28-C10 differ in the length of the
CC carbon backbone of the carboxylic acid bound to Ser-26. A small
CC fraction of ghrelin, ghrelin-27-C10:1, ghrelin-27-C10:2, ghrelin-28-
CC C8:1, ghrelin-28-C10:1, and ghrelin-28-C10:2, may be modified with
CC singly or doubly unsaturated carboxylic acids (PubMed:16466902).
CC {ECO:0000250|UniProtKB:Q9EQX0, ECO:0000269|PubMed:16466902}.
CC -!- PTM: Amidation of Leu-98 is essential for obestatin activity.
CC {ECO:0000250}.
CC -!- MASS SPECTROMETRY: [Ghrelin]: Mass=3372.77; Method=MALDI; Note=Ghrelin-
CC 28-C10, O-decanoylated form.; Evidence={ECO:0000269|PubMed:16466902};
CC -!- MASS SPECTROMETRY: [Ghrelin]: Mass=3371.22; Method=MALDI; Note=Ghrelin-
CC 28-C10:1, O-decenoylated form.; Evidence={ECO:0000269|PubMed:16466902};
CC -!- MASS SPECTROMETRY: [Ghrelin]: Mass=3367.10; Method=MALDI; Note=Ghrelin-
CC 28-C10:2, O-decadienoylated form.;
CC Evidence={ECO:0000269|PubMed:16466902};
CC -!- MASS SPECTROMETRY: [Ghrelin]: Mass=3344.88; Method=MALDI; Note=Ghrelin-
CC 28-C8, O-octanoylated form.; Evidence={ECO:0000269|PubMed:16466902};
CC -!- MASS SPECTROMETRY: [Ghrelin]: Mass=3343.21; Method=MALDI; Note=Ghrelin-
CC 28-C1, O-octenoylated form.; Evidence={ECO:0000269|PubMed:16466902};
CC -!- MASS SPECTROMETRY: [Ghrelin]: Mass=3215.90; Method=MALDI; Note=des-
CC Gln14-Ghrelin-28-C8, O-octanoylated form.;
CC Evidence={ECO:0000269|PubMed:16466902};
CC -!- MASS SPECTROMETRY: [Ghrelin]: Mass=3216.64; Method=MALDI; Note=Ghrelin-
CC 27-C10, O-decanoylated form.; Evidence={ECO:0000269|PubMed:16466902};
CC -!- MASS SPECTROMETRY: [Ghrelin]: Mass=3214.92; Method=MALDI; Note=Ghrelin-
CC 27-C10:1, O-decenoylated form.; Evidence={ECO:0000269|PubMed:16466902};
CC -!- MASS SPECTROMETRY: [Ghrelin]: Mass=3212.65; Method=MALDI; Note=Ghrelin-
CC 27-C10:2, O-decadienoylated form.;
CC Evidence={ECO:0000269|PubMed:16466902};
CC -!- MASS SPECTROMETRY: [Ghrelin]: Mass=3188.81; Method=MALDI; Note=Ghrelin-
CC 27-C8, O-octanoylated form.; Evidence={ECO:0000269|PubMed:16466902};
CC -!- MASS SPECTROMETRY: [Ghrelin]: Mass=3060.36; Method=MALDI; Note=des-
CC Gln14-Ghrelin-27-C8, O-octanoylated form.;
CC Evidence={ECO:0000269|PubMed:16466902};
CC -!- SIMILARITY: Belongs to the motilin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Gut feelings - Issue 66 of
CC January 2006;
CC URL="https://web.expasy.org/spotlight/back_issues/066";
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DR EMBL; AB089201; BAD34670.1; -; mRNA.
DR EMBL; AB089202; BAD34671.1; -; mRNA.
DR RefSeq; NP_001009853.1; NM_001009853.1. [Q6BEG6-2]
DR AlphaFoldDB; Q6BEG6; -.
DR SMR; Q6BEG6; -.
DR STRING; 9685.ENSFCAP00000010442; -.
DR Ensembl; ENSFCAT00000011246; ENSFCAP00000010442; ENSFCAG00000011244. [Q6BEG6-1]
DR GeneID; 493844; -.
DR KEGG; fca:493844; -.
DR CTD; 51738; -.
DR eggNOG; ENOG502SFY3; Eukaryota.
DR GeneTree; ENSGT00390000004064; -.
DR HOGENOM; CLU_168380_0_0_1; -.
DR InParanoid; Q6BEG6; -.
DR OrthoDB; 1600403at2759; -.
DR TreeFam; TF336219; -.
DR Proteomes; UP000011712; Chromosome A2.
DR Bgee; ENSFCAG00000011244; Expressed in spleen and 9 other tissues.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0031768; F:ghrelin receptor binding; ISS:UniProtKB.
DR GO; GO:0016608; F:growth hormone-releasing hormone activity; ISS:UniProtKB.
DR GO; GO:0005179; F:hormone activity; ISS:UniProtKB.
DR GO; GO:0030296; F:protein tyrosine kinase activator activity; IEA:Ensembl.
DR GO; GO:0008154; P:actin polymerization or depolymerization; IEA:Ensembl.
DR GO; GO:0046697; P:decidualization; IEA:Ensembl.
DR GO; GO:0016358; P:dendrite development; ISS:UniProtKB.
DR GO; GO:0060079; P:excitatory postsynaptic potential; IEA:Ensembl.
DR GO; GO:0001696; P:gastric acid secretion; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0042322; P:negative regulation of circadian sleep/wake cycle, REM sleep; IEA:Ensembl.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IEA:Ensembl.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IBA:GO_Central.
DR GO; GO:0046676; P:negative regulation of insulin secretion; ISS:UniProtKB.
DR GO; GO:0032691; P:negative regulation of interleukin-1 beta production; IEA:Ensembl.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; IEA:Ensembl.
DR GO; GO:0040013; P:negative regulation of locomotion; IEA:Ensembl.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IEA:Ensembl.
DR GO; GO:0032100; P:positive regulation of appetite; IEA:Ensembl.
DR GO; GO:0046010; P:positive regulation of circadian sleep/wake cycle, non-REM sleep; IEA:Ensembl.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IEA:Ensembl.
DR GO; GO:0051461; P:positive regulation of corticotropin secretion; IEA:Ensembl.
DR GO; GO:0051464; P:positive regulation of cortisol secretion; IEA:Ensembl.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
DR GO; GO:0060124; P:positive regulation of growth hormone secretion; IBA:GO_Central.
DR GO; GO:0032024; P:positive regulation of insulin secretion; ISS:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR GO; GO:0032097; P:positive regulation of response to food; ISS:UniProtKB.
DR GO; GO:0051965; P:positive regulation of synapse assembly; ISS:UniProtKB.
DR GO; GO:0032095; P:regulation of response to food; ISS:UniProtKB.
DR GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
DR GO; GO:0007416; P:synapse assembly; IEA:Ensembl.
DR InterPro; IPR006737; Motilin_assoc.
DR InterPro; IPR006738; Motilin_ghrelin.
DR InterPro; IPR005441; Preproghrelin.
DR PANTHER; PTHR14122; PTHR14122; 1.
DR Pfam; PF04643; Motilin_assoc; 1.
DR Pfam; PF04644; Motilin_ghrelin; 1.
DR PRINTS; PR01624; GHRELIN.
PE 1: Evidence at protein level;
KW Alternative splicing; Amidation; Hormone; Lipoprotein; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000250"
FT PEPTIDE 24..51
FT /note="Ghrelin"
FT /evidence="ECO:0000250"
FT /id="PRO_0000019200"
FT PROPEP 52..75
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000019201"
FT PEPTIDE 76..98
FT /note="Obestatin"
FT /evidence="ECO:0000250"
FT /id="PRO_0000045138"
FT PROPEP 99..117
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000045139"
FT REGION 29..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 98
FT /note="Leucine amide"
FT /evidence="ECO:0000250"
FT LIPID 26
FT /note="O-decanoyl serine; alternate"
FT /evidence="ECO:0000269|PubMed:16466902"
FT LIPID 26
FT /note="O-hexanoyl serine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9EQX0"
FT LIPID 26
FT /note="O-octanoyl serine; alternate"
FT /evidence="ECO:0000269|PubMed:16466902"
FT VAR_SEQ 37
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16466902"
FT /id="VSP_011626"
SQ SEQUENCE 117 AA; 12956 MW; 8235A51447FFF530 CRC64;
MPSPGTVCSL LLFSMLWADL AMAGSSFLSP EHQKVQQRKE SKKPPAKLQP RALEGLIHPE
DTSQVEGAED ELEIRFNAPF DVGIKLSGAQ YHQHGQALGK FLQDVLWEEA DEVLADE
