ID   GDF8_GORGO              Reviewed;         375 AA.
AC   A1C2V5;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Growth/differentiation factor 8;
DE            Short=GDF-8;
DE   AltName: Full=Myostatin;
DE   Flags: Precursor;
GN   Name=MSTN; Synonyms=GDF8;
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=17186467; DOI=10.1086/509707;
RA   Saunders M.A., Good J.M., Lawrence E.C., Ferrell R.E., Li W.H.,
RA   Nachman M.W.;
RT   "Human adaptive evolution at myostatin (GDF8), a regulator of muscle
RT   growth.";
RL   Am. J. Hum. Genet. 79:1089-1097(2006).
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; DQ927204; ABI48527.1; -; Genomic_DNA.
DR   EMBL; DQ927205; ABI48528.1; -; Genomic_DNA.
DR   RefSeq; XP_018877573.1; XM_019022028.1.
DR   AlphaFoldDB; A1C2V5; -.
DR   SMR; A1C2V5; -.
DR   STRING; 9593.ENSGGOP00000022753; -.
DR   GeneID; 101135255; -.
DR   KEGG; ggo:101135255; -.
DR   CTD; 2660; -.
DR   eggNOG; KOG3900; Eukaryota.
DR   HOGENOM; CLU_020515_6_1_1; -.
DR   InParanoid; A1C2V5; -.
DR   OMA; QICVYIY; -.
DR   OrthoDB; 892873at2759; -.
DR   Proteomes; UP000001519; Unplaced.
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: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   GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IBA:GO_Central.
DR   GO; GO:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
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   3: Inferred from homology;
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_0000285560"
FT   CHAIN           267..375
FT                   /note="Growth/differentiation factor 8"
FT                   /id="PRO_0000285561"
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;  42722 MW;  2149B46AC7D446E7 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 EAFGWDWIIA
     PKRYKANYCS GECEFVFLQK YPHTHLVHQA NPRGSAGPCC TPTKMSPINM LYFNGKEQII
     YGKIPAMVVD RCGCS