GDF8_ANAPL
ID GDF8_ANAPL Reviewed; 375 AA.
AC Q8UWE0;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Growth/differentiation factor 8;
DE Short=GDF-8;
DE AltName: Full=Myostatin;
DE Flags: Precursor;
GN Name=MSTN; Synonyms=GDF8;
OS Anas platyrhynchos (Mallard) (Anas boschas).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8839;
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; AF440861; AAL35275.1; -; mRNA.
DR AlphaFoldDB; Q8UWE0; -.
DR SMR; Q8UWE0; -.
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 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; 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_0000246998"
FT CHAIN 267..375
FT /note="Growth/differentiation factor 8"
FT /id="PRO_0000246999"
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; 42817 MW; 1BA7FF5225C23620 CRC64;
MQKLAVYVYI YLFMLISVDP VALDDGSQPT ENAEKDGLCN ACTWRQNTKS SRIEAIKIQI
LSKLRLEQAP NISRDVIKQL LPKAPPLQEL IDQYDVQRDD SSDGSLEDDD YHATTETIIT
MPTESDFLVQ MEGKPKCCFF KFSSKIQYNK VVKAQLWIYL RQVQKPTTVF VQILRLIKPM
KDGPRYTGIR SLKLDMNPGT GIWQSIDVKT VLQNWLKQPE SNLGIEIKAF DENGRDLAVT
FPGPGEDGLN PFLEVRVTDT PKRSRRDFGL DCDEHSTESR CCRYPLTVDF EAFGWDWIIA
PKRYKANYCS EECEFVFLQK YPHTHLVHQA NPRGSAGPCC TPTKMSPINM LYFNGKEQII
YGKIPAMVVD RCGCS
