GHRL_BOVIN
ID GHRL_BOVIN Reviewed; 116 AA.
AC Q9BDJ6; Q0VH85; Q9GKY6;
DT 13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kita K., Harada K., Yokota H.;
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Li C., Lobo S., Wang Z., Fu A., Meng Y., Murdoch B., Hansen C., Moore S.;
RT "A full length genomic sequence of the bovine ghrelin gene.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 24-99.
RA Kojima M.;
RL Submitted (DEC-1999) 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 {ECO:0000250}.
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; AF350329; AAK18612.1; -; mRNA.
DR EMBL; AY903701; AAX89508.1; -; Genomic_DNA.
DR EMBL; AB035702; BAB19047.1; -; mRNA.
DR RefSeq; NP_776492.1; NM_174067.2.
DR AlphaFoldDB; Q9BDJ6; -.
DR STRING; 9913.ENSBTAP00000041811; -.
DR PaxDb; Q9BDJ6; -.
DR Ensembl; ENSBTAT00000016350; ENSBTAP00000016350; ENSBTAG00000012328.
DR GeneID; 281192; -.
DR KEGG; bta:281192; -.
DR CTD; 51738; -.
DR VEuPathDB; HostDB:ENSBTAG00000012328; -.
DR VGNC; VGNC:29351; GHRL.
DR eggNOG; ENOG502SFY3; Eukaryota.
DR GeneTree; ENSGT00390000004064; -.
DR HOGENOM; CLU_168380_0_0_1; -.
DR InParanoid; Q9BDJ6; -.
DR OMA; QYQQYGR; -.
DR Reactome; R-BTA-416476; G alpha (q) signalling events.
DR Reactome; R-BTA-422085; Synthesis, secretion, and deacylation of Ghrelin.
DR Proteomes; UP000009136; Chromosome 22.
DR Bgee; ENSBTAG00000012328; Expressed in urinary bladder and 27 other tissues.
DR ExpressionAtlas; Q9BDJ6; baseline and differential.
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:0001696; P:gastric acid secretion; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
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: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 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_0000019194"
FT PROPEP 51..74
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000019195"
FT PEPTIDE 75..97
FT /note="Obestatin"
FT /evidence="ECO:0000250"
FT /id="PRO_0000045132"
FT PROPEP 98..116
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000045133"
FT REGION 30..62
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"
FT CONFLICT 34
FT /note="K -> E (in Ref. 3; BAB19047)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 116 AA; 12793 MW; F55536DAC5FA59B6 CRC64;
MPAPWTICSL LLLSVLCMDL AMAGSSFLSP EHQKLQRKEA KKPSGRLKPR TLEGQFDPEV
GSQAEGAEDE LEIRFNAPFN IGIKLAGAQS LQHGQTLGKF LQDILWEEAE ETLANE
