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GHRL_ONCMY
ID   GHRL_ONCMY              Reviewed;         111 AA.
AC   Q76IQ4; Q76HE2;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Ghrelin;
DE   Contains:
DE     RecName: Full=Ghrelin-23;
DE   Contains:
DE     RecName: Full=Ghrelin-24;
DE   Flags: Precursor;
GN   Name=ghrl;
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:BAD02979.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), PROTEIN
RP   SEQUENCE OF 27-47 (ISOFORM 1), PROTEIN SEQUENCE OF 27-44 (ISOFORM 2),
RP   AMIDATION AT VAL-49, FUNCTION, TISSUE SPECIFICITY, ACYLATION AT SER-29, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Stomach {ECO:0000312|EMBL:BAD02979.1};
RX   PubMed=12970156; DOI=10.1210/en.2003-1085;
RA   Kaiya H., Kojima M., Hosoda H., Moriyama S., Takahashi A., Kawauchi H.,
RA   Kangawa K.;
RT   "Peptide purification, complementary deoxyribonucleic acid (DNA) and
RT   genomic DNA cloning, and functional characterization of ghrelin in rainbow
RT   trout.";
RL   Endocrinology 144:5215-5226(2003).
CC   -!- FUNCTION: Ligand for growth hormone secretagogue receptor type 1
CC       (GHSR). Has an appetite-stimulating effect, induces adiposity and
CC       stimulates gastric acid secretion. Involved in growth regulation (By
CC       similarity). Induces the release of growth hormone from the pituitary.
CC       {ECO:0000250, ECO:0000269|PubMed:12970156}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1 {ECO:0000269|PubMed:12970156};
CC         IsoId=Q76IQ4-1; Sequence=Displayed;
CC       Name=2 {ECO:0000269|PubMed:12970156}; Synonyms=des-VRQ-ghrelin
CC       {ECO:0000303|PubMed:12970156};
CC         IsoId=Q76IQ4-2; Sequence=VSP_051754;
CC   -!- TISSUE SPECIFICITY: Highest levels in the stomach. Moderate levels in
CC       the brain, hypothalamus and intestinal tracts.
CC       {ECO:0000269|PubMed:12970156}.
CC   -!- PTM: O-octanoylated by GOAT/MBOAT4 (By similarity). O-octanoylation or
CC       O-decanoylation is essential for activity. The O-decanoylated forms
CC       differ in the length of the carbon backbone of the carboxylic acid
CC       forming an ester bond with Ser-29 (By similarity). The majority of
CC       trout ghrelin is Ghrelin-20 modified with unsaturated decanoic acid
CC       (PubMed:12970156). {ECO:0000250, ECO:0000250|UniProtKB:Q9EQX0,
CC       ECO:0000269|PubMed:12970156}.
CC   -!- PTM: Ghrelin-20 and Ghrelin-23 are amidated. In some cases, Gly-50 is
CC       retained after dibasic amino acid cleavage, to produce non-amidated
CC       Ghrelin-21 and Ghrelin-24. {ECO:0000269|PubMed:12970156}.
CC   -!- MASS SPECTROMETRY: [Isoform 2]: Mass=2204.8; Method=MALDI; Note=With
CC       amidation and (C8:1) O-octanoylation. The measured range is 27-49.;
CC       Evidence={ECO:0000269|PubMed:12970156};
CC   -!- MASS SPECTROMETRY: [Isoform 2]: Mass=2206.6; Method=MALDI; Note=With
CC       amidation and (C8:0) O-octanoylation. The measured range is 27-49.;
CC       Evidence={ECO:0000269|PubMed:12970156};
CC   -!- MASS SPECTROMETRY: [Isoform 2]: Mass=2230.7; Method=MALDI; Note=With
CC       amidation and (C10:2) O-decanoylation. Major form. The measured range
CC       is 27-49.; Evidence={ECO:0000269|PubMed:12970156};
CC   -!- MASS SPECTROMETRY: [Isoform 2]: Mass=2232.5; Method=MALDI; Note=With
CC       amidation and (C10:1) O-decanoylation. The measured range is 27-49.;
CC       Evidence={ECO:0000269|PubMed:12970156};
CC   -!- MASS SPECTROMETRY: [Isoform 2]: Mass=2235.0; Method=MALDI; Note=With
CC       amidation and (C10:0) O-decanoylation. The measured range is 27-49.;
CC       Evidence={ECO:0000269|PubMed:12970156};
CC   -!- MASS SPECTROMETRY: [Isoform 2]: Mass=2264.1; Method=MALDI; Note=With
CC       glycine retention and (C8:0) O-octanoylation. The measured range is 27-
CC       50.; Evidence={ECO:0000269|PubMed:12970156};
CC   -!- MASS SPECTROMETRY: [Isoform 2]: Mass=2288.4; Method=MALDI; Note=With
CC       glycine retention and (C10:2) O-decanoylation. The measured range is
CC       27-50.; Evidence={ECO:0000269|PubMed:12970156};
CC   -!- MASS SPECTROMETRY: [Isoform 2]: Mass=2291.1; Method=MALDI; Note=With
CC       glycine retention and (C10:1) O-decanoylation. The measured range is
CC       27-50.; Evidence={ECO:0000269|PubMed:12970156};
CC   -!- MASS SPECTROMETRY: [Isoform 1]: Mass=2590.0; Method=MALDI; Note=With
CC       amidation and (C8:0) O-octanoylation. The measured range is 27-49.;
CC       Evidence={ECO:0000269|PubMed:12970156};
CC   -!- MASS SPECTROMETRY: [Isoform 1]: Mass=2613.9; Method=MALDI; Note=With
CC       amidation and (C10:1) O-decanoylation. The measured range is 27-49.;
CC       Evidence={ECO:0000269|PubMed:12970156};
CC   -!- MASS SPECTROMETRY: [Isoform 1]: Mass=2648.2; Method=MALDI; Note=With
CC       glycine retention and (C8:0) O-octanoylation. The measured range is 27-
CC       50.; Evidence={ECO:0000269|PubMed:12970156};
CC   -!- MASS SPECTROMETRY: [Isoform 1]: Mass=2672.3; Method=MALDI; Note=With
CC       glycine retention and (C10:2) O-decanoylation. The measured range is
CC       27-50.; Evidence={ECO:0000269|PubMed:12970156};
CC   -!- SIMILARITY: Belongs to the motilin family. {ECO:0000255}.
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DR   EMBL; AB096919; BAD02979.1; -; mRNA.
DR   EMBL; AB100839; BAD02980.1; -; Genomic_DNA.
DR   EMBL; AB100839; BAD02981.1; -; Genomic_DNA.
DR   EMBL; AB101443; BAD02982.1; -; mRNA.
DR   RefSeq; NP_001118060.1; NM_001124588.1. [Q76IQ4-1]
DR   AlphaFoldDB; Q76IQ4; -.
DR   Ensembl; ENSOMYT00000159004; ENSOMYP00000114948; ENSOMYG00000008000. [Q76IQ4-1]
DR   GeneID; 100136596; -.
DR   KEGG; omy:100136596; -.
DR   CTD; 51738; -.
DR   OrthoDB; 1600403at2759; -.
DR   GO; GO:0005615; C:extracellular space; IDA:AgBase.
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; IDA:AgBase.
DR   GO; GO:0032099; P:negative regulation of appetite; IDA:AgBase.
DR   GO; GO:0010628; P:positive regulation of gene expression; IDA:AgBase.
DR   GO; GO:1901671; P:positive regulation of superoxide dismutase activity; IDA:AgBase.
DR   GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IMP:AgBase.
DR   GO; GO:0042594; P:response to starvation; IDA:AgBase.
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   Alternative splicing; Amidation; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Hormone; Lipoprotein; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000269|PubMed:12970156"
FT   PEPTIDE         27..50
FT                   /note="Ghrelin-24"
FT                   /evidence="ECO:0000269|PubMed:12970156"
FT                   /id="PRO_0000019216"
FT   PEPTIDE         27..49
FT                   /note="Ghrelin-23"
FT                   /evidence="ECO:0000269|PubMed:12970156"
FT                   /id="PRO_0000019217"
FT   PROPEP          53..111
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000269|PubMed:12970156"
FT                   /id="PRO_0000019218"
FT   REGION          28..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         49
FT                   /note="Valine amide"
FT                   /evidence="ECO:0000269|PubMed:12970156"
FT   LIPID           29
FT                   /note="O-decanoyl serine; alternate"
FT                   /evidence="ECO:0000269|PubMed:12970156"
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:12970156"
FT   VAR_SEQ         39..41
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12970156"
FT                   /id="VSP_051754"
SQ   SEQUENCE   111 AA;  12304 MW;  28CE572EA3BD3F96 CRC64;
     MPLKRNTGLM ILMLCTLALW AKSVSAGSSF LSPSQKPQVR QGKGKPPRVG RRDIESFAEL
     FEGPLHQEDK HNTIKAPFEM GITMSEEEFQ EYGAVLQKIL QDVLGDTATA E
 
 
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