ID   GHRL_CARAU              Reviewed;         103 AA.
AC   Q8AUU1;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=Ghrelin;
DE   Contains:
DE     RecName: Full=Ghrelin-12;
DE   Contains:
DE     RecName: Full=Ghrelin-19;
DE   Flags: Precursor;
GN   Name=ghrl;
OS   Carassius auratus (Goldfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Carassius.
OX   NCBI_TaxID=7957;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAN16215.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, AMIDATION AT GLN-38 AND
RP   MET-45, AND TISSUE SPECIFICITY.
RC   TISSUE=Intestine {ECO:0000269|PubMed:12239128};
RX   PubMed=12239128; DOI=10.1210/en.2002-220644;
RA   Unniappan S., Lin X., Cervini L., Rivier J., Kaiya H., Kangawa K.,
RA   Peter R.E.;
RT   "Goldfish ghrelin: molecular characterization of the complementary
RT   deoxyribonucleic acid, partial gene structure and evidence for its
RT   stimulatory role in food intake.";
RL   Endocrinology 143:4143-4146(2002).
CC   -!- FUNCTION: Ligand for growth hormone secretagogue receptor type 1
CC       (GHSR). Induces the release of growth hormone from the pituitary.
CC       Induces adiposity and stimulates gastric acid secretion. Involved in
CC       growth regulation (By similarity). Has an appetite-stimulating effect.
CC       {ECO:0000250, ECO:0000269|PubMed:12239128}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8JFY4}.
CC   -!- TISSUE SPECIFICITY: Expressed in the telencephalon, hypothalamus,
CC       pituitary, intestine, liver, spleen and gill, with expression strongest
CC       in the intestine. {ECO:0000269|PubMed:12239128}.
CC   -!- PTM: O-octanoylated by GOAT/MBOAT4 (By similarity). O-octanoylation or
CC       O-decanoylation is essential for activity. The O-decanoylated form
CC       differs in the length of the carbon backbone of the carboxylic acid
CC       forming an ester bond with Ser-29 (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:Q9EQX0}.
CC   -!- SIMILARITY: Belongs to the motilin family. {ECO:0000255}.
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DR   EMBL; AF454389; AAN16215.1; -; mRNA.
DR   EMBL; AF454390; AAN16216.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8AUU1; -.
DR   Ensembl; ENSCART00000117806; ENSCARP00000105416; ENSCARG00000054031.
DR   Proteomes; UP000515129; Genome assembly.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0001664; F:G protein-coupled receptor binding; ISS:UniProtKB.
DR   GO; GO:0016608; F:growth hormone-releasing hormone activity; ISS:UniProtKB.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0030252; P:growth hormone secretion; ISS:UniProtKB.
DR   InterPro; IPR006737; Motilin_assoc.
DR   InterPro; IPR005441; Preproghrelin.
DR   PANTHER; PTHR14122; PTHR14122; 1.
DR   Pfam; PF04643; Motilin_assoc; 1.
PE   1: Evidence at protein level;
KW   Amidation; Cleavage on pair of basic residues; Hormone; Lipoprotein;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   PEPTIDE         27..45
FT                   /note="Ghrelin-19"
FT                   /evidence="ECO:0000303|PubMed:12239128"
FT                   /id="PRO_0000019213"
FT   PEPTIDE         27..38
FT                   /note="Ghrelin-12"
FT                   /evidence="ECO:0000303|PubMed:12239128"
FT                   /id="PRO_0000019214"
FT   PROPEP          49..103
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000303|PubMed:12239128"
FT                   /id="PRO_0000019215"
FT   REGION          27..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         38
FT                   /note="Glutamine amide"
FT                   /evidence="ECO:0000305|PubMed:12239128"
FT   MOD_RES         45
FT                   /note="Methionine amide"
FT                   /evidence="ECO:0000305|PubMed:12239128"
FT   LIPID           29
FT                   /note="O-decanoyl serine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9EQX0"
FT   LIPID           29
FT                   /note="O-hexanoyl serine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9EQX0"
FT   LIPID           29
FT                   /note="O-octanoyl serine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9EQX0"
SQ   SEQUENCE   103 AA;  11520 MW;  0881343BDCD0C012 CRC64;
     MPLRRRASHM FVLLCALSLC VESVKGGTSF LSPAQKPQGR RPPRMGRRDV AEPEIPVIKE
     DDQFMMSAPF ELSVSLSEAE YEKYGPVLQK VLVNLLGDSP LEF