ID   GDF8_PAPHA              Reviewed;         375 AA.
AC   O18828;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Growth/differentiation factor 8;
DE            Short=GDF-8;
DE   AltName: Full=Myostatin;
DE   Flags: Precursor;
GN   Name=MSTN; Synonyms=GDF8;
OS   Papio hamadryas (Hamadryas baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9557;
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).
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; AF019619; AAB86686.1; -; mRNA.
DR   AlphaFoldDB; O18828; -.
DR   SMR; O18828; -.
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:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0014839; P:myoblast migration involved in skeletal muscle regeneration; ISS:UniProtKB.
DR   GO; GO:2000818; P:negative regulation of myoblast proliferation; ISS:AgBase.
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:0010592; P:positive regulation of lamellipodium assembly; ISS:UniProtKB.
DR   GO; GO:0010759; P:positive regulation of macrophage chemotaxis; 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   2: Evidence at transcript level;
KW   Cleavage on pair of basic residues; Cytokine; Disulfide bond; Glycoprotein;
KW   Growth factor; Heparin-binding; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PROPEP          24..266
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000033958"
FT   CHAIN           267..375
FT                   /note="Growth/differentiation factor 8"
FT                   /id="PRO_0000033959"
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;  42688 MW;  7B49B90ACAB926EA CRC64;
     MQKLQLCVYI YLFMLIVAGP VDLNENSEQK ENVEKEGLCN ACTWRQNTKS SRIEAIKIQI
     LSKLRLETAP NISKDAIRQL LPKAPPLREL IDQYDVQRDD SSDGSLEDDD YHATTETIIT
     MPTESDFLMQ VDGKPKCCFF KFSSKIQYNK VVKAQLWIYL RPVETPTTVF VQILRLIKPM
     KDGTRYTGIR SLKLDMNPGT GIWQSIDVKT VLQNWLKQPE SNLGIEIKAL DENGHDLAVT
     FPGPGEDGLN PFLEVKVTDT PKRSRRDFGL DCDEHSTESR CCRYPLTVDF EALGWDWIIA
     PKRYKANYCS GECEFVFLQK YPHTHLVHQA NPRGSAGPCC TPTKMSPINM LYFNGKEQII
     YGKIPAMVVD RCGCS