ID   GDF8_ANSAN              Reviewed;         375 AA.
AC   Q8UWD9;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Growth/differentiation factor 8;
DE            Short=GDF-8;
DE   AltName: Full=Myostatin;
DE   Flags: Precursor;
GN   Name=MSTN; Synonyms=GDF8;
OS   Anser anser anser (Western greylag goose).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC   Anserinae; Anser.
OX   NCBI_TaxID=8844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Gu Z., Yang W., Cheng Z., Li H., Zhu D.;
RT   "Molecular cloning and tissue distribution of the myostatin gene in duck,
RT   goose, pigeon and quail.";
RL   Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts specifically as a negative regulator of skeletal muscle
CC       growth. {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR   EMBL; AF440862; AAL35276.1; -; mRNA.
DR   AlphaFoldDB; Q8UWD9; -.
DR   SMR; Q8UWD9; -.
DR   GO; GO:0005615; C:extracellular space; ISS:AgBase.
DR   GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0033002; P:muscle cell proliferation; ISS:AgBase.
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   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; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PROPEP          24..266
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000247000"
FT   CHAIN           267..375
FT                   /note="Growth/differentiation factor 8"
FT                   /id="PRO_0000247001"
FT   CARBOHYD        71
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        272..282
FT                   /evidence="ECO:0000250|UniProtKB:O08689"
FT   DISULFID        281..340
FT                   /evidence="ECO:0000250"
FT   DISULFID        309..372
FT                   /evidence="ECO:0000250"
FT   DISULFID        313..374
FT                   /evidence="ECO:0000250"
FT   DISULFID        339
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   375 AA;  42667 MW;  57DDE49D3AA2978C CRC64;
     MQKLAVYVYI YLFMLISVDP VALDDGSQPT ENAEKDGLCN ACTWRQNTKS SRIEAIKIQI
     LSKLRLEQAP NISRDVIKQL LPKAPPLQEL IDQYDVQRDD SSDGSLEDDD YHATTETIIT
     MPTESDFLVQ MEGKPKCCFF KFSSKIQYNK VVKAQLWIYL RQVQKPTTVF VQILRLIKPM
     KDGTRYTGIR SLKLDIDPGA GFGQSIDVKT VLQNWLKQPE SNLGIEIKAF DENGRDLAVT
     FPGPGEDGLN PFLEVRVTDT PKRSRRDFGL DCDEHSTESR CCRYPLTVDF EAFGWDWIIA
     PKRYKANYCF GECEFVFLQK YPHTHLVHQA NPRGSAGPCC TPTKMSPINM LYFNGKEQII
     YGKIPAMVVD RCGCS