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Growth/differentiation factor 8 (GDF-8) (Myostatin)

 GDF8_CAPHI              Reviewed;         375 AA.
Q6T5B8; Q3S4A8;
12-APR-2005, integrated into UniProtKB/Swiss-Prot.
25-JUL-2006, sequence version 2.
20-JUN-2018, entry version 60.
RecName: Full=Growth/differentiation factor 8;
Short=GDF-8;
AltName: Full=Myostatin;
Flags: Precursor;
Name=MSTN; Synonyms=GDF8;
Capra hircus (Goat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Caprinae; Capra.
NCBI_TaxID=9925;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Golding M.C., Long C.R., Westhusin M.E.;
"siRNA knock down of goat myostatin.";
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Blood;
Liu Z.Z., Li X.L., Gong Y.F.;
"Cloning and expression of the goat myostatin gene.";
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Acts specifically as a negative regulator of skeletal
muscle growth. {ECO:0000250|UniProtKB:O08689}.
-!- SUBUNIT: Homodimer; disulfide-linked. Interacts with WFIKKN2,
leading to inhibit its activity. Interacts with FSTL3.
{ECO:0000250|UniProtKB:O08689}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O08689}.
-!- PTM: Synthesized as large precursor molecule that undergoes
proteolytic cleavage to generate an N-terminal propeptide and a
disulfide linked C-terminal dimer, which is the biologically
active molecule. The circulating form consists of a latent complex
of the C-terminal dimer and other proteins, including its
propeptide, which maintain the C-terminal dimer in a latent,
inactive state. Ligand activation requires additional cleavage of
the prodomain by a tolloid-like metalloproteinase.
{ECO:0000250|UniProtKB:O08689}.
-!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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EMBL; AY436347; AAR12161.1; -; mRNA.
EMBL; DQ167575; AAZ95183.2; -; Genomic_DNA.
RefSeq; NP_001272666.1; NM_001285737.1.
UniGene; Chi.5130; -.
ProteinModelPortal; Q6T5B8; -.
SMR; Q6T5B8; -.
Ensembl; ENSCHIT00000034681; ENSCHIP00000026815; ENSCHIG00000022964.
GeneID; 100860887; -.
KEGG; chx:100860887; -.
CTD; 2660; -.
HOVERGEN; HBG000217; -.
KO; K05497; -.
OrthoDB; EOG091G078V; -.
GO; GO:0005623; C:cell; IEA:GOC.
GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:Ensembl.
GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IEA:Ensembl.
GO; GO:0033673; P:negative regulation of kinase activity; IEA:Ensembl.
GO; GO:0045662; P:negative regulation of myoblast differentiation; IEA:Ensembl.
GO; GO:0051898; P:negative regulation of protein kinase B signaling; IEA:Ensembl.
GO; GO:0048632; P:negative regulation of skeletal muscle tissue growth; IEA:Ensembl.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
Gene3D; 2.10.90.10; -; 1.
InterPro; IPR029034; Cystine-knot_cytokine.
InterPro; IPR015616; GDF_8.
InterPro; IPR001839; TGF-b_C.
InterPro; IPR001111; TGF-b_propeptide.
InterPro; IPR015615; TGF-beta-rel.
InterPro; IPR017948; TGFb_CS.
PANTHER; PTHR11848; PTHR11848; 1.
PANTHER; PTHR11848:SF150; PTHR11848:SF150; 1.
Pfam; PF00019; TGF_beta; 1.
Pfam; PF00688; TGFb_propeptide; 1.
SMART; SM00204; TGFB; 1.
SUPFAM; SSF57501; SSF57501; 1.
PROSITE; PS00250; TGF_BETA_1; 1.
PROSITE; PS51362; TGF_BETA_2; 1.
2: Evidence at transcript level;
Cleavage on pair of basic residues; Cytokine; Disulfide bond;
Glycoprotein; Growth factor; Heparin-binding; Secreted; Signal.
SIGNAL 1 18 {ECO:0000255}.
PROPEP 19 266 {ECO:0000255}.
/FTId=PRO_0000033944.
CHAIN 267 375 Growth/differentiation factor 8.
/FTId=PRO_0000033945.
SITE 98 99 Cleavage. {ECO:0000250|UniProtKB:O08689}.
CARBOHYD 48 48 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 71 71 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 272 282 {ECO:0000250|UniProtKB:O14793}.
DISULFID 281 340 {ECO:0000250|UniProtKB:O14793}.
DISULFID 309 372 {ECO:0000250|UniProtKB:O14793}.
DISULFID 313 374 {ECO:0000250|UniProtKB:O14793}.
DISULFID 339 339 Interchain.
{ECO:0000250|UniProtKB:O14793}.
CONFLICT 7 7 F -> S (in Ref. 1; AAR12161).
{ECO:0000305}.
CONFLICT 16 16 L -> I (in Ref. 1; AAR12161).
{ECO:0000305}.
CONFLICT 29 29 Q -> H (in Ref. 1; AAR12161).
{ECO:0000305}.
CONFLICT 195 195 D -> A (in Ref. 1; AAR12161).
{ECO:0000305}.
CONFLICT 293 293 F -> V (in Ref. 1; AAR12161).
{ECO:0000305}.
SEQUENCE 375 AA; 42827 MW; 1C36F3833BB11241 CRC64;
MQKLQIFVYI YLFMLLVAGP VDLNENSEQK ENVEKKGLCN ACLWRQNNKS SRLEAIKIQI
LSKLRLETAP NISKDAIRQL LPKAPPLREL IDQYDVQRDD SSDGSLEDDD YHVTTETVIT
MPTESDLLAE VQEKPKCCFF KFSSKIQHNK VVKAQLWIYL RPVKTPTTVF VQILRLIKPM
KDGTRYTGIR SLKLDMNPGT GIWQSIDVKT VLQNWLKQPE SNLGIEIKAL DENGHDLAVT
FPEPGEEGLN PFLEVKVTDT PKRSRRDFGL DCDEHSTESR CCRYPLTVDF EAFGWDWIIA
PKRYKANYCS GECEFLFLQK YPHTHLVHQA NPKGSAGPCC TPTKMSPINM LYFNGKEQII
YGKIPGMVVD RCGCS


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