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Database: UniProt
Entry: O18831
LinkDB: O18831
Original site: O18831 
ID   GDF8_PIG                Reviewed;         375 AA.
AC   O18831; Q540D6;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 133.
DE   RecName: Full=Growth/differentiation factor 8;
DE            Short=GDF-8;
DE   AltName: Full=Myostatin;
DE   Flags: Precursor;
GN   Name=MSTN; Synonyms=GDF8;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Skeletal muscle;
RX   PubMed=9356471; DOI=10.1073/pnas.94.23.12457;
RA   McPherron A.C., Lee S.-J.;
RT   "Double muscling in cattle due to mutations in the myostatin gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:12457-12461(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15986890; DOI=10.1007/bf02879670;
RA   Yu Z., Li Y., Meng Q., Yuan J., Zhao Z., Li W., Hu X., Yan B., Fan B.,
RA   Yu S., Li N.;
RT   "Comparative analysis of the pig BAC sequence involved in the regulation of
RT   myostatin gene.";
RL   Sci. China, Ser. C, Life Sci. 48:168-180(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Duroc, Hampshire, Meishan, and Yorkshire; TISSUE=Skeletal muscle;
RA   Voelker G.R., Conroy J.C., Wheeler M.B.;
RT   "Porcine myostatin cDNA sequences: Duroc, Hampshire, Meishan and Yorkshire
RT   pigs.";
RL   Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Landrace, Large white, Meishan, and Pietrain;
RA   Stinckens A., Luyten T., Bijttebier J., Van den Maagdenberg K.,
RA   Dieltiens D., Janssens S., De Smet S., Georges M., Buys N.;
RT   "Characterization of the porcine MSTN gene in different pig breeds.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10, AND NUCLEOTIDE SEQUENCE [MRNA]
RP   OF 36-375.
RC   TISSUE=Muscle;
RA   Daneau I., Silversides D.W.;
RL   Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts specifically as a negative regulator of skeletal muscle
CC       growth. {ECO:0000250|UniProtKB:O08689}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with WFIKKN2, leading
CC       to inhibit its activity. Interacts with FSTL3.
CC       {ECO:0000250|UniProtKB:O08689}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O08689}.
CC   -!- PTM: Synthesized as large precursor molecule that undergoes proteolytic
CC       cleavage to generate an N-terminal propeptide and a disulfide linked C-
CC       terminal dimer, which is the biologically active molecule. The
CC       circulating form consists of a latent complex of the C-terminal dimer
CC       and other proteins, including its propeptide, which maintain the C-
CC       terminal dimer in a latent, inactive state. Ligand activation requires
CC       additional cleavage of the prodomain by a tolloid-like
CC       metalloproteinase. {ECO:0000250|UniProtKB:O08689}.
CC   -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR   EMBL; AF019623; AAB86690.1; -; mRNA.
DR   EMBL; AY208121; AAO31983.1; -; Genomic_DNA.
DR   EMBL; AF188635; AAF02770.1; -; mRNA.
DR   EMBL; AF188636; AAF02771.1; -; mRNA.
DR   EMBL; AF188637; AAF02772.1; -; mRNA.
DR   EMBL; AF188638; AAF02773.1; -; mRNA.
DR   EMBL; EF490986; ABO64638.1; -; Genomic_DNA.
DR   EMBL; EF490987; ABO64639.1; -; Genomic_DNA.
DR   EMBL; EF490988; ABO64640.1; -; Genomic_DNA.
DR   EMBL; EF490989; ABO64641.1; -; Genomic_DNA.
DR   EMBL; EF490990; ABO64642.1; -; Genomic_DNA.
DR   EMBL; AF033855; AAC08035.1; -; mRNA.
DR   EMBL; AF093798; AAC62489.1; -; Genomic_DNA.
DR   AlphaFoldDB; O18831; -.
DR   SMR; O18831; -.
DR   STRING; 9823.ENSSSCP00000017001; -.
DR   GlyCosmos; O18831; 1 site, No reported glycans.
DR   PaxDb; 9823-ENSSSCP00000017001; -.
DR   PeptideAtlas; O18831; -.
DR   Ensembl; ENSSSCT00000017472.5; ENSSSCP00000017001.2; ENSSSCG00000016047.5.
DR   Ensembl; ENSSSCT00015002832.1; ENSSSCP00015000900.1; ENSSSCG00015002286.1.
DR   Ensembl; ENSSSCT00025067980.1; ENSSSCP00025029196.1; ENSSSCG00025049835.1.
DR   Ensembl; ENSSSCT00030023330.1; ENSSSCP00030010461.1; ENSSSCG00030016859.1.
DR   Ensembl; ENSSSCT00035037306.1; ENSSSCP00035014874.1; ENSSSCG00035028194.1.
DR   Ensembl; ENSSSCT00040025633.1; ENSSSCP00040010829.1; ENSSSCG00040018971.1.
DR   Ensembl; ENSSSCT00045018814.1; ENSSSCP00045012947.1; ENSSSCG00045011070.1.
DR   Ensembl; ENSSSCT00050016408.1; ENSSSCP00050006740.1; ENSSSCG00050012141.1.
DR   Ensembl; ENSSSCT00055042989.1; ENSSSCP00055034200.1; ENSSSCG00055021878.1.
DR   Ensembl; ENSSSCT00060094644.1; ENSSSCP00060040929.1; ENSSSCG00060069269.1.
DR   Ensembl; ENSSSCT00065034252.1; ENSSSCP00065014182.1; ENSSSCG00065025598.1.
DR   Ensembl; ENSSSCT00070018169.1; ENSSSCP00070015094.1; ENSSSCG00070009359.1.
DR   VGNC; VGNC:96320; MSTN.
DR   eggNOG; KOG3900; Eukaryota.
DR   GeneTree; ENSGT00940000160657; -.
DR   HOGENOM; CLU_020515_6_1_1; -.
DR   InParanoid; O18831; -.
DR   OMA; TDQCATC; -.
DR   TreeFam; TF318514; -.
DR   Proteomes; UP000008227; Chromosome 15.
DR   Proteomes; UP000314985; Chromosome 15.
DR   Proteomes; UP000694570; Unplaced.
DR   Proteomes; UP000694571; Unplaced.
DR   Proteomes; UP000694720; Unplaced.
DR   Proteomes; UP000694722; Unplaced.
DR   Proteomes; UP000694723; Unplaced.
DR   Proteomes; UP000694724; Unplaced.
DR   Proteomes; UP000694725; Unplaced.
DR   Proteomes; UP000694726; Unplaced.
DR   Proteomes; UP000694727; Unplaced.
DR   Proteomes; UP000694728; Unplaced.
DR   Bgee; ENSSSCG00000016047; Expressed in skeletal muscle tissue and 16 other cell types or tissues.
DR   ExpressionAtlas; O18831; baseline.
DR   Genevisible; O18831; SS.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
DR   GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:Ensembl.
DR   GO; GO:0014839; P:myoblast migration involved in skeletal muscle regeneration; ISS:UniProtKB.
DR   GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0045662; P:negative regulation of myoblast differentiation; IEA:Ensembl.
DR   GO; GO:2000818; P:negative regulation of myoblast proliferation; ISS:AgBase.
DR   GO; GO:0051898; P:negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR   GO; GO:1902725; P:negative regulation of satellite cell differentiation; ISS:AgBase.
DR   GO; GO:1902723; P:negative regulation of skeletal muscle satellite cell proliferation; ISS:AgBase.
DR   GO; GO:0048632; P:negative regulation of skeletal muscle tissue growth; IEA:Ensembl.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:Ensembl.
DR   GO; GO:0010592; P:positive regulation of lamellipodium assembly; ISS:UniProtKB.
DR   GO; GO:0010759; P:positive regulation of macrophage chemotaxis; ISS:UniProtKB.
DR   GO; GO:0014816; P:skeletal muscle satellite cell differentiation; IEA:Ensembl.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR   CDD; cd19388; TGF_beta_GDF8; 1.
DR   Gene3D; 2.60.120.970; -; 1.
DR   Gene3D; 2.10.90.10; Cystine-knot cytokines; 1.
DR   InterPro; IPR029034; Cystine-knot_cytokine.
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:SF150; GROWTH_DIFFERENTIATION FACTOR 8; 1.
DR   PANTHER; PTHR11848; TGF-BETA FAMILY; 1.
DR   Pfam; PF00019; TGF_beta; 1.
DR   Pfam; PF00688; TGFb_propeptide; 1.
DR   SMART; SM00204; TGFB; 1.
DR   SUPFAM; SSF57501; Cystine-knot cytokines; 1.
DR   PROSITE; PS00250; TGF_BETA_1; 1.
DR   PROSITE; PS51362; TGF_BETA_2; 1.
PE   2: Evidence at transcript level;
KW   Cleavage on pair of basic residues; Cytokine; Disulfide bond; Glycoprotein;
KW   Growth factor; Heparin-binding; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PROPEP          24..266
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000033960"
FT   CHAIN           267..375
FT                   /note="Growth/differentiation factor 8"
FT                   /id="PRO_0000033961"
FT   SITE            98..99
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000250|UniProtKB:O08689"
FT   CARBOHYD        71
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        272..282
FT                   /evidence="ECO:0000250|UniProtKB:O14793"
FT   DISULFID        281..340
FT                   /evidence="ECO:0000250|UniProtKB:O14793"
FT   DISULFID        309..372
FT                   /evidence="ECO:0000250|UniProtKB:O14793"
FT   DISULFID        313..374
FT                   /evidence="ECO:0000250|UniProtKB:O14793"
FT   DISULFID        339
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250|UniProtKB:O14793"
SQ   SEQUENCE   375 AA;  42791 MW;  0F658685EFDA3418 CRC64;
     MQKLQIYVYI YLFMLIVAGP VDLNENSEQK ENVEKEGLCN ACMWRQNTKS SRLEAIKIQI
     LSKLRLETAP NISKDAIRQL LPKAPPLREL IDQYDVQRDD SSDGSLEDDD YHATTETIIT
     MPTESDLLMQ VEGKPKCCFF KFSSKIQYNK VVKAQLWIYL RPVKTPTTVF VQILRLIKPM
     KDGTRYTGIR SLKLDMNPGT GIWQSIDVKT VLQNWLKQPE SNLGIEIKAL DENGHDLAVT
     FPGPGEDGLN PFLEVKVTDT PKRSRRDFGL DCDEHSTESR CCRYPLTVDF EAFGWDWIIA
     PKRYKANYCS GECEFVFLQK YPHTHLVHQA NPRGSAGPCC TPTKMSPINM LYFNGKEQII
     YGKIPAMVVD RCGCS
//
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