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 19-OCT-2011, entry version 34. 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] RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 27-47, FUNCTION, RP TISSUE SPECIFICITY, ACYLATION AT SER-29, AND MASS SPECTROMETRY. RC TISSUE=Stomach; RX MEDLINE=22519143; 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 RT and 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. CC Has an appetite-stimulating effect, induces adiposity and CC stimulates gastric acid secretion. Involved in growth regulation. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Highest levels in stomach and anterior CC intestine. Lower levels in posterior intestine, kidney and brain. CC Low levels in heart, head kidney and middle intestine. CC -!- PTM: O-octanoylation or O-decanoylation is essential for activity. CC The O-decanoylated form ghrelin-21-C10 differs in the length of CC the carbon backbone of the carboxylic acid forming an ester bond CC with Ser-29. 44% of eel ghrelin is O-decanoylated. CC -!- MASS SPECTROMETRY: Mass=2449.2; Method=MALDI; Range=27-47; CC Note=Ghrelin-21-C10, O-decanoylated form; Source=PubMed:12630926; CC -!- MASS SPECTROMETRY: Mass=2421.7; Method=MALDI; Range=27-47; CC Note=Ghrelin-21-C8, O-octanoylated form; Source=PubMed:12630926; CC -!- SIMILARITY: Belongs to the motilin family. 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 HOVERGEN; HBG018522; -. 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 protein signaling pathway; IDA:UniProtKB. DR InterPro; IPR006737; Motilin_assoc. DR Pfam; PF04643; Motilin_assoc; 1. PE 1: Evidence at protein level; KW Amidation; Cleavage on pair of basic residues; KW Direct protein sequencing; Hormone; Lipoprotein; Secreted; Signal. FT SIGNAL 1 26 FT PEPTIDE 27 47 Ghrelin. FT /FTId=PRO_0000019211. FT PROPEP 51 111 Removed in mature form. FT /FTId=PRO_0000019212. FT MOD_RES 47 47 Valine amide (Probable). FT LIPID 29 29 O-decanoyl serine; alternate. FT LIPID 29 29 O-octanoyl serine; alternate. SQ SEQUENCE 111 AA; 12831 MW; 7AF95E04DD22DE7B CRC64; MRQMKRTAYI ILLVCVLALW MDSVQAGSSF LSPSQRPQGK DKKPPRVGRR DSDGILDLFM RPPLQDEDIR HITFNTPFEI GITMTEELFQ QYGEVMQKIM QDLLMDTPAK E //