GHRL_LITCT
ID GHRL_LITCT Reviewed; 114 AA.
AC Q90W22;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 45.
DE RecName: Full=Ghrelin;
DE Contains:
DE RecName: Full=Ghrelin-27;
DE Contains:
DE RecName: Full=Ghrelin-28;
DE Flags: Precursor;
GN Name=GHRL;
OS Lithobates catesbeianus (American bullfrog) (Rana catesbeiana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX NCBI_TaxID=8400;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAB71718.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-52, FUNCTION, TISSUE
RP SPECIFICITY, ACYLATION AT THR-27, AND MASS SPECTROMETRY.
RC TISSUE=Stomach {ECO:0000312|EMBL:BAB71718.1};
RX PubMed=11546772; DOI=10.1074/jbc.m105212200;
RA Kaiya H., Kojima M., Hosoda H., Koda A., Yamamoto K., Kitajima Y.,
RA Matsumoto M., Minamitake Y., Kikuyama S., Kangawa K.;
RT "Bullfrog ghrelin is modified by n-octanoic acid at its third threonine
RT residue.";
RL J. Biol. Chem. 276:40441-40448(2001).
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:11546772}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: High levels in stomach. Moderate levels in small
CC intestine, pancreas and testis. Low levels in heart, lung and gall
CC bladder. {ECO:0000269|PubMed:11546772}.
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-27-C10 differs in the length of the carbon backbone of the
CC carboxylic acid bound to Thr-27. 33% of frog ghrelin is O-decanoylated
CC (PubMed:11546772). {ECO:0000250|UniProtKB:Q9EQX0,
CC ECO:0000269|PubMed:11546772}.
CC -!- PTM: 80% of frog ghrelin has Asn-52 cleaved from its C-terminus giving
CC rise to ghrelin-27. {ECO:0000269|PubMed:11546772}.
CC -!- MASS SPECTROMETRY: [Ghrelin-28]: Mass=3308.5; Mass_error=0.9;
CC Method=Electrospray; Note=Ghrelin-28-C8, O-octanoylated form.;
CC Evidence={ECO:0000269|PubMed:11546772};
CC -!- MASS SPECTROMETRY: [Ghrelin-27]: Mass=3225.3; Mass_error=1.7;
CC Method=Electrospray; Note=Ghrelin-27-C10, O-decanoylated form.;
CC Evidence={ECO:0000269|PubMed:11546772};
CC -!- MASS SPECTROMETRY: [Ghrelin-27]: Mass=3196.1; Mass_error=0.9;
CC Method=Electrospray; Note=Ghrelin-28-C8, O-octanoylated form.;
CC Evidence={ECO:0000269|PubMed:11546772};
CC -!- SIMILARITY: Belongs to the motilin family. {ECO:0000255}.
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DR EMBL; AB058510; BAB71718.1; -; mRNA.
DR AlphaFoldDB; Q90W22; -.
DR SMR; Q90W22; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Direct protein sequencing; Hormone;
KW Lipoprotein; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:11546772"
FT PEPTIDE 25..52
FT /note="Ghrelin-28"
FT /evidence="ECO:0000269|PubMed:11546772"
FT /id="PRO_0000019219"
FT PEPTIDE 25..51
FT /note="Ghrelin-27"
FT /evidence="ECO:0000269|PubMed:11546772"
FT /id="PRO_0000019220"
FT PROPEP 55..114
FT /note="Removed in mature form"
FT /id="PRO_0000019221"
FT LIPID 27
FT /note="O-decanoyl threonine; alternate"
FT /evidence="ECO:0000269|PubMed:11546772"
FT LIPID 27
FT /note="O-octanoyl threonine; alternate"
FT /evidence="ECO:0000269|PubMed:11546772"
SQ SEQUENCE 114 AA; 12756 MW; 1FE419ACB30AA141 CRC64;
MNFGKAAIFG VVLFCLLWTE GAQAGLTFLS PADMQKIAER QSQNKLRHGN MNRRGVEDDL
AGEEIGVTFP LDMKMTQEQF QKQRAAVQDF LYSSLLSLGS VQDTEDKNEN PQSQ
