| 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 |