Detail Information for IndEnz0002018478
IED ID IndEnz0002018478
Enzyme Type ID protease018478
Protein Name Growth/differentiation factor 8
GDF-8
Myostatin
Gene Name MSTN GDF8
Organism Homo sapiens (Human)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MQKLQLCVYIYLFMLIVAGPVDLNENSEQKENVEKEGLCNACTWRQNTKSSRIEAIKIQILSKLRLETAPNISKDVIRQLLPKAPPLRELIDQYDVQRDDSSDGSLEDDDYHATTETIITMPTESDFLMQVDGKPKCCFFKFSSKIQYNKVVKAQLWIYLRPVETPTTVFVQILRLIKPMKDGTRYTGIRSLKLDMNPGTGIWQSIDVKTVLQNWLKQPESNLGIEIKALDENGHDLAVTFPGPGEDGLNPFLEVKVTDTPKRSRRDFGLDCDEHSTESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGECEFVFLQKYPHTHLVHQANPRGSAGPCCTPTKMSPINMLYFNGKEQIIYGKIPAMVVDRCGCS
Enzyme Length 375
Uniprot Accession Number O14793
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Acts specifically as a negative regulator of skeletal muscle growth. {ECO:0000250|UniProtKB:O08689}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (18); Chain (1); Disulfide bond (5); Glycosylation (1); Helix (8); Mutagenesis (10); Natural variant (4); Propeptide (1); Signal peptide (1); Site (1); Turn (1)
Keywords 3D-structure;Cleavage on pair of basic residues;Cytokine;Disulfide bond;Glycoprotein;Growth factor;Heparin-binding;Reference proteome;Secreted;Signal
Interact With Q13705; P13497; P09958; Itself; Q96NZ8; O14793
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O08689}.
Modified Residue
Post Translational Modification PTM: Synthesized as large precursor molecule that undergoes proteolytic cleavage to generate an N-terminal propeptide and a disulfide linked C-terminal dimer, which is the biologically active molecule. The circulating form consists of a latent complex of the C-terminal dimer and other proteins, including its propeptide, which maintain the C-terminal dimer in a latent, inactive state. Ligand activation requires additional cleavage of the prodomain by a tolloid-like metalloproteinase. {ECO:0000250|UniProtKB:O08689}.
Signal Peptide SIGNAL 1..23; /evidence=ECO:0000255
Structure 3D X-ray crystallography (5)
Cross Reference PDB 5F3B; 5F3H; 5NTU; 5NXS; 6UMX;
Mapped Pubmed ID 11555072; 12060865; 12165013; 12175483; 12194980; 15083369; 15181048; 15567067; 16437538; 16464946; 16849634; 16885393; 17609255; 17673556; 17703271; 17711997; 17823296; 18175804; 18203713; 18240972; 18284920; 18335407; 18535106; 18563849; 18567511; 18596030; 18801770; 18835929; 19147968; 19232494; 19237423; 19277943; 19299575; 19346981; 19422651; 19453261; 19533653; 19591015; 19751112; 19828686; 19918890; 20026378; 20044471; 20161792; 20186835; 20237496; 20536908; 20640547; 20648054; 20734064; 20801187; 20884321; 21104587; 21164115; 21228768; 21273059; 21283721; 21450574; 21463333; 21507246; 21508334; 21605155; 21665986; 21900687; 21900845; 21931616; 22052913; 22081442; 22209717; 22324844; 22395277; 22426697; 22476926; 22568578; 22615949; 22802085; 22818745; 22916099; 22968486; 23291166; 23354683; 23687104; 23829672; 23861230; 23967261; 24145431; 24215591; 24479661; 24680839; 25093622; 25108351; 25254550; 25443639; 25543063; 25591711; 25641196; 25736326; 25915890; 25936293; 26046327; 26086422; 26138721; 26305594; 26393401; 26438394; 26502079; 26572800; 26577677; 26607022; 26998756; 27034275; 27144806; 27165248; 27304512; 27323660; 27390974; 27392496; 27467217; 27481097; 27559042; 27878995; 28007336; 28074267; 28345488; 28406165; 28465115; 28472635; 28627027; 29192144; 29247983; 29330193; 29343545; 29348202; 29409020; 29546591; 29558345; 29718700; 29794429; 30152416; 30165829; 30241032; 30317402; 30370618; 30463070; 31302645; 31442362; 31526145; 31539882; 31582541; 31829144; 32027955; 32035222; 32075906; 32173683; 32272446; 32286342; 32645967; 32751455; 32838566; 33020908; 33044569; 33173958; 33348054; 33546034; 33554779; 33874963; 33876824; 34067816; 34131275; 34319830; 34469188;
Motif
Gene Encoded By
Mass 42,750
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda