IED ID | IndEnz0002003884 |
Enzyme Type ID | protease003884 |
Protein Name |
Stromelysin-2 SL-2 EC 3.4.24.22 Matrix metalloproteinase-10 MMP-10 Transin-2 |
Gene Name | MMP10 STMY2 |
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 | MMHLAFLVLLCLPVCSAYPLSGAAKEEDSNKDLAQQYLEKYYNLEKDVKQFRRKDSNLIVKKIQGMQKFLGLEVTGKLDTDTLEVMRKPRCGVPDVGHFSSFPGMPKWRKTHLTYRIVNYTPDLPRDAVDSAIEKALKVWEEVTPLTFSRLYEGEADIMISFAVKEHGDFYSFDGPGHSLAHAYPPGPGLYGDIHFDDDEKWTEDASGTNLFLVAAHELGHSLGLFHSANTEALMYPLYNSFTELAQFRLSQDDVNGIQSLYGPPPASTEEPLVPTKSVPSGSEMPAKCDPALSFDAISTLRGEYLFFKDRYFWRRSHWNPEPEFHLISAFWPSLPSYLDAAYEVNSRDTVFIFKGNEFWAIRGNEVQAGYPRGIHTLGFPPTIRKIDAAVSDKEKKKTYFFAADKYWRFDENSQSMEQGFPRLIADDFPGVEPKVDAVLQAFGFFYFFSGSSQFEFDPNARMVTHILKSNSWLHC |
Enzyme Length | 476 |
Uniprot Accession Number | P09238 |
Absorption | |
Active Site | ACT_SITE 218; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:15095982" |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Similar to stromelysin 1, but action on collagen types III, IV and V is weak.; EC=3.4.24.22; Evidence={ECO:0000269|PubMed:15095982}; |
DNA Binding | |
EC Number | 3.4.24.22 |
Enzyme Function | FUNCTION: Can degrade fibronectin, gelatins of type I, III, IV, and V; weakly collagens III, IV, and V. Activates procollagenase. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Beta strand (11); Chain (1); Disulfide bond (1); Helix (4); Metal binding (8); Motif (1); Natural variant (8); Propeptide (1); Repeat (4); Signal peptide (1); Turn (1) |
Keywords | 3D-structure;Calcium;Collagen degradation;Disulfide bond;Extracellular matrix;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Repeat;Secreted;Signal;Zinc;Zymogen |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..17; /evidence=ECO:0000305 |
Structure 3D | X-ray crystallography (3) |
Cross Reference PDB | 1Q3A; 3V96; 4ILW; |
Mapped Pubmed ID | 10986281; 1311314; 1371271; 1480033; 15288123; 15371548; 15375490; 15944607; 16054593; 16331256; 1649600; 16516860; 16580524; 1698775; 17009259; 17088321; 17543340; 17695449; 18035073; 18427549; 18617643; 1874716; 19317417; 19489686; 19601983; 19695094; 19762781; 19913121; 19921252; 19935709; 20142769; 20215736; 20432469; 20452482; 20453000; 20484597; 20584750; 20587546; 20628086; 20673868; 20936527; 21410539; 2169257; 2169335; 21925226; 21998657; 22022614; 22104553; 22121946; 22382088; 22427646; 22492089; 22524815; 2253219; 22545096; 22821423; 23098370; 23742289; 24009192; 24073280; 24077220; 24078057; 24122885; 24327153; 24413984; 24576976; 24884523; 24885595; 25441671; 2548603; 25742789; 25808184; 26415518; 26419737; 26625808; 26861993; 27072580; 27172796; 27316687; 27351228; 27567711; 27654284; 28005267; 28379489; 28510611; 28805015; 28939077; 29016666; 30949574; 31192258; 31913319; 32188274; 3223920; 32325785; 32650441; 33436543; 33548006; 34175352; 34418671; 6258630; 7669817; 7780967; 7896811; 7981201; 8226919; 8631328; 8920930; 9346290; 9578462; |
Motif | MOTIF 89..96; /note=Cysteine switch; /evidence=ECO:0000250 |
Gene Encoded By | |
Mass | 54,151 |
Kinetics | |
Metal Binding | METAL 91; /note=Zinc; in inhibited form; /evidence=ECO:0000250; METAL 167; /note=Zinc 1; METAL 169; /note=Zinc 1; METAL 182; /note=Zinc 1; METAL 195; /note=Zinc 1; METAL 217; /note=Zinc 2; catalytic; METAL 221; /note=Zinc 2; catalytic; METAL 227; /note=Zinc 2; catalytic |
Rhea ID | |
Cross Reference Brenda | 3.4.24.22; |