GDF8_COLLI
ID GDF8_COLLI Reviewed; 375 AA.
AC Q8UWD8;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Growth/differentiation factor 8;
DE Short=GDF-8;
DE AltName: Full=Myostatin;
DE Flags: Precursor;
GN Name=MSTN; Synonyms=GDF8;
OS Columba livia (Rock dove).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX NCBI_TaxID=8932;
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; AF440863; AAL35277.1; -; mRNA.
DR RefSeq; NP_001269738.1; NM_001282809.1.
DR AlphaFoldDB; Q8UWD8; -.
DR SMR; Q8UWD8; -.
DR STRING; 8932.XP_005501772.1; -.
DR GeneID; 102098948; -.
DR KEGG; clv:102098948; -.
DR CTD; 2660; -.
DR eggNOG; KOG3900; Eukaryota.
DR OrthoDB; 892873at2759; -.
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_0000247002"
FT CHAIN 267..375
FT /note="Growth/differentiation factor 8"
FT /id="PRO_0000247003"
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; 42739 MW; 88296F0AE779476E CRC64;
MQKLAVYVYI YLCMLISVHP LALDDGSQPT ENSEKDGLCN ACTWRQNTKS SRIEAIKIQI
LSKLRLEQAP NISRDLIKQP LPKAPPLQEL IDLYDVQRDD SSNGSLEDDD 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
