GDF8_MELGA
ID GDF8_MELGA Reviewed; 375 AA.
AC O42221;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Growth/differentiation factor 8;
DE Short=GDF-8;
DE AltName: Full=Myostatin;
DE Flags: Precursor;
GN Name=MSTN; Synonyms=GDF8;
OS Meleagris gallopavo (Wild turkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Meleagridinae; Meleagris.
OX NCBI_TaxID=9103;
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.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB86692.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF019625; AAB86692.1; ALT_INIT; mRNA.
DR RefSeq; NP_001290090.1; NM_001303161.1.
DR AlphaFoldDB; O42221; -.
DR SMR; O42221; -.
DR Ensembl; ENSMGAT00000007052; ENSMGAP00000006304; ENSMGAG00000006288.
DR GeneID; 100303659; -.
DR KEGG; mgp:100303659; -.
DR CTD; 2660; -.
DR GeneTree; ENSGT00940000160657; -.
DR HOGENOM; CLU_020515_6_1_1; -.
DR InParanoid; O42221; -.
DR OMA; QICVYIY; -.
DR OrthoDB; 892873at2759; -.
DR TreeFam; TF318514; -.
DR Proteomes; UP000001645; Chromosome 7.
DR Bgee; ENSMGAG00000006288; Expressed in pectoralis major and 8 other tissues.
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:0008201; F:heparin binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:Ensembl.
DR GO; GO:0033002; P:muscle cell proliferation; ISS:AgBase.
DR GO; GO:0014839; P:myoblast migration involved in skeletal muscle regeneration; ISS:UniProtKB.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0033673; P:negative regulation of kinase activity; IEA:Ensembl.
DR GO; GO:0045662; P:negative regulation of myoblast differentiation; IEA:Ensembl.
DR GO; GO:2000818; P:negative regulation of myoblast proliferation; IDA:AgBase.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; IEA:Ensembl.
DR GO; GO:1902725; P:negative regulation of satellite cell differentiation; IDA:AgBase.
DR GO; GO:1902723; P:negative regulation of skeletal muscle satellite cell proliferation; IDA:AgBase.
DR GO; GO:0048632; P:negative regulation of skeletal muscle tissue growth; IEA:Ensembl.
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:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
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; Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..266
FT /evidence="ECO:0000255"
FT /id="PRO_0000033974"
FT CHAIN 267..375
FT /note="Growth/differentiation factor 8"
FT /id="PRO_0000033975"
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; 42784 MW; D2AEAB732AEB4E77 CRC64;
MQKLAVYVYI YLFMQILVHP VALDGSSQPT ENAEKDGLCN ACTWRQNTKS SRIEAIKIQI
LSKLRLEQAP NISRDVIKQL LPKAPPLQEL IDQYDVQRDD SSDGSLEDDD YHATTETIIT
MPTESDFLVQ MEGKPKCCFF KFSSKIQYNK VVKAQLWIYL RQVQKPTTVF VQILRLIKPM
KDGTRYTGIR SLKLDMNPGT GIWQSIDVKT VLQNWLKQPE SNLGIEIKAF DENGRDLAVT
FPGPGEDGLN PFLEVRVTDT PKRSRRDFGL DCDEHSTESR CCRYPLTVDF EAFGWDWIIA
PKRYKANYCS GECEFVFLQK YPHTHLVHQA NPRGSAGPCC TPTKMSPINM LYFNGKEQII
YGKIPAMVVD RCGCS
