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 22-FEB-2023, entry version 53. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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:SF1; APPETITE-REGULATING HORMONE; 1. DR PANTHER; PTHR14122; GHRELIN PRECURSOR; 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 //