GDF8_EPICO
ID GDF8_EPICO Reviewed; 376 AA.
AC Q5I3Q2;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Growth/differentiation factor 8 {ECO:0000303|PubMed:17048071, ECO:0000303|PubMed:20483295};
DE AltName: Full=Myostatin {ECO:0000303|PubMed:17048071, ECO:0000303|PubMed:20483295};
DE Short=MSTN {ECO:0000303|PubMed:17048071};
DE Flags: Precursor;
GN Name=gdf-8 {ECO:0000303|PubMed:20483295};
OS Epinephelus coioides (Orange-spotted grouper) (Epinephelus nebulosus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Serranoidei; Serranidae; Epinephelinae;
OC Epinephelini; Epinephelus.
OX NCBI_TaxID=94232 {ECO:0000312|EMBL:AAW47740.1};
RN [1] {ECO:0000312|EMBL:AAW47740.1}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP PHYLOGENETIC ANALYSIS.
RX PubMed=20483295; DOI=10.1016/j.cbd.2007.04.003;
RA Chen Y.M., Wei C.Y., Chien C.H., Chang H.W., Huang S.I., Yang H.L.,
RA Chen T.Y.;
RT "Myostatin gene organization and nodavirus-influenced expression in orange-
RT spotted grouper (Epinephelus coioides).";
RL Comp. Biochem. Physiol. 2:215-227(2007).
RN [2] {ECO:0000312|EMBL:ABF48090.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND PHYLOGENETIC ANALYSIS.
RX PubMed=17048071; DOI=10.1007/s10126-006-6059-8;
RA Ko C.F., Chiou T.T., Chen T.T., Wu J.L., Chen J.C., Lu J.K.;
RT "Molecular cloning of myostatin gene and characterization of tissue-
RT specific and developmental stage-specific expression of the gene in orange
RT spotted grouper, Epinephelus coioides.";
RL Mar. Biotechnol. 9:20-32(2007).
CC -!- FUNCTION: Acts specifically as a negative regulator of skeletal muscle
CC growth. {ECO:0000250|UniProtKB:O42222}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250|UniProtKB:O08689}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255,
CC ECO:0000269|PubMed:20483295}.
CC -!- TISSUE SPECIFICITY: Highly expressed in muscle (PubMed:20483295,
CC PubMed:17048071). Also expressed in other tissues such as eye, brain,
CC gill, heart, head kidney, stomach and intestine. Low levels in spleen
CC and liver (PubMed:17048071). {ECO:0000269|PubMed:17048071,
CC ECO:0000269|PubMed:20483295}.
CC -!- DEVELOPMENTAL STAGE: Low levels detected in the unfertilized eggs,
CC newly fertilized eggs, 16-cell stage and morula stage embryos. Higher
CC levels detected in the blastula, gastrula and neurula stages. Higher
CC levels also detected during the lens formation stage, somite and
CC hatching stage. The expression levels continue to increase during
CC development and peaks at 30 day old larvae, and then gradually
CC decreases to lower levels again in day 60 larval stage.
CC {ECO:0000269|PubMed:17048071}.
CC -!- INDUCTION: (Microbial infection) Myostatin concentrations are decreased
CC in serum of fish infected with nodavirus as compared to serum from
CC uninfected fish (at protein level). {ECO:0000269|PubMed:20483295}.
CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000255,
CC ECO:0000255|RuleBase:RU000354, ECO:0000305}.
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DR EMBL; AY856860; AAW47740.1; -; mRNA.
DR EMBL; DQ493889; ABF48090.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5I3Q2; -.
DR SMR; Q5I3Q2; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0048632; P:negative regulation of skeletal muscle tissue growth; ISS:UniProtKB.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
DR Gene3D; 2.10.90.10; -; 1.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR015616; GDF_8.
DR InterPro; IPR001839; TGF-b_C.
DR InterPro; IPR001111; TGF-b_propeptide.
DR InterPro; IPR015615; TGF-beta-rel.
DR InterPro; IPR017948; TGFb_CS.
DR PANTHER; PTHR11848; PTHR11848; 1.
DR PANTHER; PTHR11848:SF150; PTHR11848:SF150; 1.
DR Pfam; PF00019; TGF_beta; 1.
DR Pfam; PF00688; TGFb_propeptide; 1.
DR SMART; SM00204; TGFB; 1.
DR SUPFAM; SSF57501; SSF57501; 1.
DR PROSITE; PS00250; TGF_BETA_1; 1.
DR PROSITE; PS51362; TGF_BETA_2; 1.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Cytokine; Disulfide bond;
KW Growth factor; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..267
FT /evidence="ECO:0000255"
FT /id="PRO_0000438150"
FT CHAIN 268..376
FT /note="Growth/differentiation factor 8"
FT /evidence="ECO:0000255"
FT /id="PRO_5007705924"
FT DISULFID 273..283
FT /evidence="ECO:0000250|UniProtKB:O08689"
FT DISULFID 282..341
FT /evidence="ECO:0000250|UniProtKB:O08689"
FT DISULFID 310..373
FT /evidence="ECO:0000250|UniProtKB:O08689"
FT DISULFID 314..375
FT /evidence="ECO:0000250|UniProtKB:O08689"
FT DISULFID 340
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:O08689"
SQ SEQUENCE 376 AA; 42615 MW; 63CC1AACB228BC56 CRC64;
MHLSQIVLYL GLLIALGPVV LSDQETHQQP SATSPEDTEQ CATCEVRQQI KTMRLNAIKS
QILSKLRMKE APNISRDIVK QLLPKAPPLQ QLLDQYDVLG DDNKDVVMEE DDEHATTETI
MMMATEPESV VQADGEPKCC LFSFTQKFQA NRIVRAQLWV HLRPADEATT VFLQISRLMP
VTDGNRHIRI RSLKIDVNAG VSSWQSIDVK QVLTVWLRQP ETNWGIEINA FDSRGNDLAV
TSAEPGEDGL QPFMEVKISE GPRRVRRDSG LDCDENSPES RCCRYPLTVD FEDFGWDWII
APKRYKANYC SGECEYMHLQ KYPHTHLVNK ANPRGTAGPC CTPTKMSPIN MLYFNRKEQI
IYGKIPSMVV DRCGCS