ID   GHRL_ANGJA              Reviewed;         111 AA.
AC   Q8JFY4;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 51.
DE   RecName: Full=Ghrelin;
DE   AltName: Full=Ghrelin-21;
DE   Flags: Precursor;
GN   Name=ghrl;
OS   Anguilla japonica (Japanese eel).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Anguilliformes; Anguillidae;
OC   Anguilla.
OX   NCBI_TaxID=7937;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:BAB96565.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 27-47, FUNCTION, TISSUE
RP   SPECIFICITY, ACYLATION AT SER-29, AMIDATION AT VAL-47, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Stomach {ECO:0000312|EMBL:BAB96565.1};
RX   PubMed=12630926; DOI=10.1677/joe.0.1760415;
RA   Kaiya H., Kojima M., Hosoda H., Riley L.G., Hirano T., Grau E.G.,
RA   Kangawa K.;
RT   "Amidated fish ghrelin: purification, cDNA cloning in the Japanese eel and
RT   its biological activity.";
RL   J. Endocrinol. 176:415-423(2003).
CC   -!- FUNCTION: Ligand for growth hormone secretagogue receptor type 1
CC       (GHSR). Induces the release of growth hormone from the pituitary. Has
CC       an appetite-stimulating effect, induces adiposity and stimulates
CC       gastric acid secretion. Involved in growth regulation.
CC       {ECO:0000269|PubMed:12630926}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Highest levels in stomach and anterior intestine.
CC       Lower levels in posterior intestine, kidney and brain. Low levels in
CC       heart, head kidney and middle intestine. {ECO:0000269|PubMed:12630926}.
CC   -!- PTM: O-octanoylated by GOAT/MBOAT4 (By similarity). O-octanoylation or
CC       O-decanoylation is essential for activity. The O-decanoylated form
CC       ghrelin-21-C10 differs in the length of the carbon backbone of the
CC       carboxylic acid forming an ester bond with Ser-29. 44% of eel ghrelin
CC       is O-decanoylated (PubMed:12630926). {ECO:0000250|UniProtKB:Q9EQX0,
CC       ECO:0000269|PubMed:12630926}.
CC   -!- MASS SPECTROMETRY: Mass=2449.2; Method=MALDI; Note=Ghrelin-21-C10, O-
CC       decanoylated form.; Evidence={ECO:0000269|PubMed:12630926};
CC   -!- MASS SPECTROMETRY: Mass=2421.7; Method=MALDI; Note=Ghrelin-21-C8, O-
CC       octanoylated form.; Evidence={ECO:0000269|PubMed:12630926};
CC   -!- SIMILARITY: Belongs to the motilin family. {ECO:0000255}.
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DR   EMBL; AB062427; BAB96565.1; -; mRNA.
DR   AlphaFoldDB; Q8JFY4; -.
DR   GO; GO:0005615; C:extracellular space; IC:UniProtKB.
DR   GO; GO:0001664; F:G protein-coupled receptor binding; IPI:UniProtKB.
DR   GO; GO:0016608; F:growth hormone-releasing hormone activity; IDA:UniProtKB.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA: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; Direct protein sequencing;
KW   Hormone; Lipoprotein; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000269|PubMed:12630926"
FT   PEPTIDE         27..47
FT                   /note="Ghrelin"
FT                   /evidence="ECO:0000269|PubMed:12630926"
FT                   /id="PRO_0000019211"
FT   PROPEP          51..111
FT                   /note="Removed in mature form"
FT                   /id="PRO_0000019212"
FT   REGION          28..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..53
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         47
FT                   /note="Valine amide"
FT                   /evidence="ECO:0000269|PubMed:12630926"
FT   LIPID           29
FT                   /note="O-decanoyl serine; alternate"
FT                   /evidence="ECO:0000269|PubMed:12630926"
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:0000269|PubMed:12630926"
SQ   SEQUENCE   111 AA;  12831 MW;  7AF95E04DD22DE7B CRC64;
     MRQMKRTAYI ILLVCVLALW MDSVQAGSSF LSPSQRPQGK DKKPPRVGRR DSDGILDLFM
     RPPLQDEDIR HITFNTPFEI GITMTEELFQ QYGEVMQKIM QDLLMDTPAK E