ID   GDF8_COTCO              Reviewed;         375 AA.
AC   Q8AVB2;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Growth/differentiation factor 8;
DE            Short=GDF-8;
DE   AltName: Full=Myostatin;
DE   Flags: Precursor;
GN   Name=MSTN; Synonyms=GDF8;
OS   Coturnix coturnix (Common quail) (Tetrao coturnix).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Perdicinae; Coturnix.
OX   NCBI_TaxID=9091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pectoralis muscle;
RA   Mott I.W., Ivarie R.D.;
RT   "Expression of myostatin is not altered in growth-selected lines of poultry
RT   exhibiting myofiber hyper- and hypoplasia.";
RL   Submitted (AUG-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; AF407340; AAN63522.1; -; mRNA.
DR   AlphaFoldDB; Q8AVB2; -.
DR   SMR; Q8AVB2; -.
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_0000247006"
FT   CHAIN           267..375
FT                   /note="Growth/differentiation factor 8"
FT                   /id="PRO_0000247007"
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;  42775 MW;  769B93A5364DD7ED CRC64;
     MQKIVVYVYI YLFVQISVDP VALDGSSQPT ENTEKDGLCN ACTWRQNTKS SRIEAIKIQI
     LSKLRLEQAP NISRDVIKQL LPKAPPLQEL IDQYDVQRDD SSDGSLEDDD YHATTETIIT
     MPTESDFLVQ MEGKPKCCFF KFSSKIQYNK VVKAQLWIYL RQVQKPTTVF VQILRLIKPM
     KDGTRYTGIR SLKLDMNPGN GIWQSIDVKT VLQNWLKQPE SNLGIEIKAF DENGRDLAVT
     FPGPGEDGLN PFLEVRVTDT PKRSRRDFGL DCDEHSTESR CCRYPLTVDF EAFGWDWIIA
     PKRYKANYCS GECEFVFLQK YPHTHLVHQA NPRGSAGPCC TPTKMSPINM LYFNGKEQII
     YGKIPAMVVD RCGCS