ID   GDF8_TAUDE              Reviewed;         375 AA.
AC   Q5USW0;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Growth/differentiation factor 8;
DE            Short=GDF-8;
DE   AltName: Full=Myostatin;
DE   Flags: Precursor;
GN   Name=MSTN; Synonyms=GDF8;
OS   Taurotragus derbianus (Giant eland) (Derby eland).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Taurotragus.
OX   NCBI_TaxID=303930;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15522803; DOI=10.1016/j.ympev.2004.07.004;
RA   Tellgren S., Berglund A.C., Savolainen P., Janis C.M., Liberles D.A.;
RT   "Myostatin rapid sequence evolution in ruminants predates domestication.";
RL   Mol. Phylogenet. Evol. 33:782-790(2004).
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; AY629304; AAT40568.1; -; mRNA.
DR   AlphaFoldDB; Q5USW0; -.
DR   SMR; Q5USW0; -.
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: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..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..266
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000033968"
FT   CHAIN           267..375
FT                   /note="Growth/differentiation factor 8"
FT                   /id="PRO_0000033969"
FT   CARBOHYD        47
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
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;  42487 MW;  052A9B8161C29CB0 CRC64;
     MQKLQISVYI YLFMLIVAGP VDLNEKSEQK ENVEKEGLCN ACLWRENTTS SRLEAIKIQI
     LSKLRLETAP NISKDAIRQL LPKAPPLLEL IDQFDVQGDA SSDGSLEDDD YHARTETVIT
     MPTESDLLTQ VEGKPKCCFF KFSSKIQYNK LVKAQLWIYL RPVKTPTTVF AQILRLIKPM
     KDGTRYTGIR SLKLDMNPGT GIWQSIDVKT VLQNWLKQPE SNLGIEIKAL DENGRDLAVT
     FPEPGEDGLT PFLEVKVTDT PKRSRRDFGL DCDEHSTESR CCRYPLTVDF EAFGWDWIIA
     PKRYKANYCS GECEFVFLQK YPHTHLVHQA NPRGSAGPCC TPTKMSPINM LYFNGEGQII
     YGKIPAMVVD RCGCS