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   24-JAN-2024, entry version 119.
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   BindingDB; Q9BDJ6; -.
DR   ChEMBL; CHEMBL5169189; -.
DR   PaxDb; 9913-ENSBTAP00000041811; -.
DR   Ensembl; ENSBTAT00000016350.5; ENSBTAP00000016350.4; ENSBTAG00000012328.5.
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 cell types or 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: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:SF1; APPETITE-REGULATING HORMONE; 1.
DR   PANTHER; PTHR14122; GHRELIN PRECURSOR; 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
//