| IED ID | IndEnz0002001695 |
| Enzyme Type ID | protease001695 |
| Protein Name |
Metalloproteinase inhibitor 3 Protein MIG-5 Tissue inhibitor of metalloproteinases 3 TIMP-3 |
| Gene Name | TIMP3 |
| 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 | MTPWLGLIVLLGSWSLGDWGAEACTCSPSHPQDAFCNSDIVIRAKVVGKKLVKEGPFGTLVYTIKQMKMYRGFTKMPHVQYIHTEASESLCGLKLEVNKYQYLLTGRVYDGKMYTGLCNFVERWDQLTLSQRKGLNYRYHLGCNCKIKSCYYLPCFVTSKNECLWTDMLSNFGYPGYQSKHYACIRQKGGYCSWYRGWAPPDKSIINATDP |
| Enzyme Length | 211 |
| Uniprot Accession Number | P35625 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. May form part of a tissue-specific acute response to remodeling stimuli. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-9, MMP-13, MMP-14 and MMP-15. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (8); Chain (1); Disulfide bond (6); Domain (1); Helix (3); Metal binding (1); Natural variant (5); Region (3); Sequence conflict (2); Signal peptide (1); Site (1); Turn (3) |
| Keywords | 3D-structure;Direct protein sequencing;Disease variant;Disulfide bond;Extracellular matrix;Metal-binding;Metalloenzyme inhibitor;Metalloprotease inhibitor;Protease inhibitor;Reference proteome;Secreted;Sensory transduction;Signal;Vision;Zinc |
| Interact With | P50052 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000269|PubMed:7795886 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 3CKI; |
| Mapped Pubmed ID | 11353449; 11821400; 11827969; 11879143; 11988096; 12372614; 12388270; 12652295; 12654640; 12687014; 12845640; 12969699; 1435334; 14532978; 14605322; 14632160; 15203191; 15223866; 15225209; 15297175; 15313474; 15387372; 15467768; 15468069; 15538971; 15592495; 15599946; 15688381; 15714128; 15879156; 15944607; 16079149; 16223891; 16225775; 16259644; 16771712; 16858683; 16908447; 16989765; 17030988; 17033924; 17080297; 17130843; 17202148; 17206475; 17209433; 17376651; 17470431; 17488654; 17592394; 17657847; 17676308; 17897911; 17901377; 18006877; 18186556; 18291374; 18316197; 18344519; 18383040; 18471442; 18516293; 18566294; 18636124; 18818748; 18955737; 19019335; 19020732; 19082505; 19148529; 19296468; 19299578; 19406980; 19431211; 19438747; 19478078; 19536307; 19543729; 19581416; 19633828; 19643179; 19666115; 19799609; 19834535; 19835597; 19913121; 19922547; 19962668; 20140262; 20346171; 20385819; 20388016; 20417062; 20484597; 20587546; 20598922; 20606036; 20628086; 20628624; 20672350; 20682640; 20801516; 20941363; 21102583; 21339735; 21421877; 21613373; 21730794; 21779788; 21809381; 21983937; 21984580; 22171703; 22183341; 22194599; 22228635; 22272343; 22291969; 22378045; 22383695; 22406378; 22415751; 22492871; 22510504; 22550340; 22735305; 22888638; 22982189; 23023527; 23023649; 23042095; 23109338; 23166318; 23172037; 23313877; 23379820; 23401241; 23422939; 23468994; 23504349; 23527119; 23575435; 23636268; 23649698; 23794948; 23797704; 23819566; 23830872; 23872201; 23991023; 24011615; 24048576; 24129822; 24132606; 24195505; 24221409; 24359512; 24487965; 24495020; 24804215; 24903383; 24973455; 25041782; 25065733; 25128867; 25171061; 25300296; 25357107; 25449074; 25467143; 25558000; 25563468; 25609649; 25766588; 25819812; 26068512; 26123869; 26304100; 26493035; 26579821; 26676407; 26686417; 26707830; 26749283; 26872030; 26979530; 27058897; 27075707; 27084377; 27191265; 27222429; 27291149; 27314542; 27314831; 27476612; 27488105; 27543695; 27545813; 27582494; 27601084; 27610455; 27706614; 27746079; 27966779; 28005406; 28081267; 28138307; 28236165; 28550172; 28672103; 28740544; 28935174; 29177591; 29304854; 29393355; 29467412; 29498555; 29523219; 29524167; 29745091; 30212710; 30218185; 30279425; 30281655; 30362332; 30388611; 30450736; 30668888; 30715128; 30781538; 30915776; 30988064; 31026378; 31185764; 31298305; 31397536; 31558368; 31588243; 31624299; 31773698; 31815654; 31887330; 31917155; 31927006; 32071343; 32107793; 32143276; 32271187; 32306499; 32309847; 32502021; 32542727; 32631441; 32896063; 32968163; 33121296; 33126605; 33131351; 33349112; 33379361; 33504102; 33634991; 33653378; 33725949; 33760178; 33831331; 33960555; 34240668; 34390329; 34459016; 34781885; |
| Motif | |
| Gene Encoded By | |
| Mass | 24,145 |
| Kinetics | |
| Metal Binding | METAL 24; /note="Zinc; via amino nitrogen and carbonyl oxygen; shared with metalloproteinase partner"; /evidence="ECO:0000269|PubMed:18638486, ECO:0007744|PDB:3CKI" |
| Rhea ID | |
| Cross Reference Brenda |