GHRL_CANLF
ID GHRL_CANLF Reviewed; 117 AA.
AC Q9BEF8; Q9BEF7;
DT 13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
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; Synonyms=MTLRP;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Gastric fundus;
RA Tomasetto C., Wendling C., Rio M.-C., Poitras P.;
RT "Identification of cDNA encoding MTLRP/ghrelin precursor from dog fundus.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Stomach;
RA Doi K., Kojima M., Hosoda H., Kaiya H., Matsuo H., Kangawa K.;
RT "Dog ghrelin.";
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
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=Q9BEF8-1; Sequence=Displayed;
CC Name=2; Synonyms=des-Gln14-ghrelin;
CC IsoId=Q9BEF8-2; Sequence=VSP_003244;
CC -!- PTM: O-octanoylated by GOAT/MBOAT4 (By similarity). O-octanoylation is
CC essential for ghrelin activity. {ECO:0000250,
CC ECO:0000250|UniProtKB:Q9EQX0}.
CC -!- PTM: Amidation of Leu-98 is essential for obestatin activity.
CC {ECO:0000250}.
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; AJ298295; CAC29155.1; -; mRNA.
DR EMBL; AJ298296; CAC29156.1; -; mRNA.
DR EMBL; AB060700; BAC75929.1; -; mRNA.
DR RefSeq; NP_001003052.1; NM_001003052.2. [Q9BEF8-1]
DR RefSeq; XP_005632067.1; XM_005632010.2. [Q9BEF8-2]
DR AlphaFoldDB; Q9BEF8; -.
DR SMR; Q9BEF8; -.
DR STRING; 9615.ENSCAFP00000007641; -.
DR PaxDb; Q9BEF8; -.
DR Ensembl; ENSCAFT00030009815; ENSCAFP00030008590; ENSCAFG00030005337. [Q9BEF8-1]
DR Ensembl; ENSCAFT00040043692; ENSCAFP00040038121; ENSCAFG00040023482. [Q9BEF8-1]
DR Ensembl; ENSCAFT00845013921; ENSCAFP00845010788; ENSCAFG00845007901. [Q9BEF8-1]
DR GeneID; 403587; -.
DR KEGG; cfa:403587; -.
DR CTD; 51738; -.
DR VEuPathDB; HostDB:ENSCAFG00845007901; -.
DR eggNOG; ENOG502SFY3; Eukaryota.
DR GeneTree; ENSGT00390000004064; -.
DR HOGENOM; CLU_168380_0_0_1; -.
DR InParanoid; Q9BEF8; -.
DR OMA; QYQQYGR; -.
DR OrthoDB; 1600403at2759; -.
DR TreeFam; TF336219; -.
DR Reactome; R-CFA-416476; G alpha (q) signalling events.
DR Reactome; R-CFA-422085; Synthesis, secretion, and deacylation of Ghrelin.
DR Proteomes; UP000002254; Chromosome 20.
DR Bgee; ENSCAFG00000005129; Expressed in stomach and 19 other tissues.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0008154; P:actin polymerization or depolymerization; ISS:UniProtKB.
DR GO; GO:0046697; P:decidualization; ISS:UniProtKB.
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; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0050728; P:negative regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:0046676; P:negative regulation of insulin secretion; ISS:UniProtKB.
DR GO; GO:0032691; P:negative regulation of interleukin-1 beta production; ISS:UniProtKB.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; ISS:UniProtKB.
DR GO; GO:0040013; P:negative regulation of locomotion; IEA:Ensembl.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISS:UniProtKB.
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; ISS:UniProtKB.
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:0042127; P:regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0032095; P:regulation of response to food; ISS:UniProtKB.
DR GO; GO:0043627; P:response to estrogen; ISS:UniProtKB.
DR GO; GO:0009725; P:response to hormone; ISS:UniProtKB.
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 3: Inferred from homology;
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_0000019196"
FT PROPEP 52..75
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000019197"
FT PEPTIDE 76..98
FT /note="Obestatin"
FT /evidence="ECO:0000250"
FT /id="PRO_0000045134"
FT PROPEP 99..117
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000045135"
FT REGION 30..68
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:0000250|UniProtKB:Q9EQX0"
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:0000250|UniProtKB:Q9EQX0"
FT VAR_SEQ 37
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_003244"
SQ SEQUENCE 117 AA; 13007 MW; 3E57FED9D1847CF7 CRC64;
MPSLGTMCSL LLFSVLWVDL AMAGSSFLSP EHQKLQQRKE SKKPPAKLQP RALEGSLGPE
DTSQVEEAED ELEIRFNAPF DVGIKLSGPQ YHQHGQALGK FLQEVLWEDT NEALADE
