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GHRL_CAPHI
ID   GHRL_CAPHI              Reviewed;         116 AA.
AC   Q6BEG7;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 78.
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   Capra hircus (Goat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Capra.
OX   NCBI_TaxID=9925;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Stomach;
RA   Lin X., Miyazato M., Kaiya H., Ida T., Kangawa K.;
RT   "cDNA cloning of feline and caprine ghrelin.";
RL   Submitted (JUL-2002) 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   -!- 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-97 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; AB089200; BAD34669.1; -; mRNA.
DR   RefSeq; XP_017893717.1; XM_018038228.1.
DR   AlphaFoldDB; Q6BEG7; -.
DR   STRING; 9925.ENSCHIP00000018945; -.
DR   iPTMnet; Q6BEG7; -.
DR   Ensembl; ENSCHIT00000026752; ENSCHIP00000018937; ENSCHIG00000018149.
DR   Ensembl; ENSCHIT00010040542; ENSCHIP00010028713; ENSCHIG00010021452.
DR   GeneID; 100861189; -.
DR   KEGG; chx:100861189; -.
DR   CTD; 51738; -.
DR   GeneTree; ENSGT00390000004064; -.
DR   OMA; QYQQYGR; -.
DR   OrthoDB; 1600403at2759; -.
DR   Proteomes; UP000291000; Chromosome 22.
DR   Bgee; ENSCHIG00000018149; Expressed in descending colon and 3 other tissues.
DR   GO; GO:0030424; C:axon; ISS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
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: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:0032720; P:negative regulation of tumor necrosis factor production; ISS:UniProtKB.
DR   GO; GO:0046010; P:positive regulation of circadian sleep/wake cycle, non-REM sleep; 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; IEA:Ensembl.
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   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   Amidation; Hormone; Lipoprotein; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000250"
FT   PEPTIDE         24..50
FT                   /note="Ghrelin"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000019198"
FT   PROPEP          51..74
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000019199"
FT   PEPTIDE         75..97
FT                   /note="Obestatin"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000045136"
FT   PROPEP          98..116
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000045137"
FT   REGION          29..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..48
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         97
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"
SQ   SEQUENCE   116 AA;  12935 MW;  CDA67971D72E3303 CRC64;
     MPAPRTICSL LLLSMLWMDL AMAGSSFLSP EHQKLQRKEP KKPSGRLKPR ALEGQFDPDV
     GSQEEGAEDE LEIRFNAPFN IGIKLSGAQS LQHGQTLGKF LQDILWEEAE ETLADE
 
 
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