IED ID | IndEnz0002001684 |
Enzyme Type ID | protease001684 |
Protein Name |
Metalloproteinase inhibitor 2 Tissue inhibitor of metalloproteinases 2 TIMP-2 |
Gene Name | TIMP2 |
Organism | Cavia porcellus (Guinea pig) |
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 Glires (Rodents and rabbits) Rodentia Hystricomorpha Caviidae (cavies) Cavia (guinea pigs) Cavia porcellus (Guinea pig) |
Enzyme Sequence | MGATARSLRLALGLLLLGTLPRGADACSCSPVHPQQAFCNADVVIRAKAVSEKEVDSGNDIYGNPIKRIQYEIKQIKMFKGPEKDIEFIYTAPSSAVCGVSLDVGGKKEYLIAGKAEGDGKMHITLCDFIVPWDTLSTTQKKSLNHRYQMGCECKITRCPMIPCYISSPDECLWMDWVTEKSINGHQAKFFACIKRSDGSCAWYRGAAPPKQEFLDIEDP |
Enzyme Length | 220 |
Uniprot Accession Number | Q9WUC6 |
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. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Disulfide bond (6); Domain (1); Metal binding (1); Region (2); Signal peptide (1); Site (3) |
Keywords | Disulfide bond;Metal-binding;Metalloenzyme inhibitor;Metalloprotease inhibitor;Protease inhibitor;Reference proteome;Secreted;Signal;Zinc |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
Modified Residue | |
Post Translational Modification | PTM: The activity of TIMP2 is dependent on the presence of disulfide bonds. |
Signal Peptide | SIGNAL 1..26; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 24,318 |
Kinetics | |
Metal Binding | METAL 27; /note=Zinc; via amino nitrogen and carbonyl oxygen; shared with metalloproteinase partner; /evidence=ECO:0000250|UniProtKB:P16035 |
Rhea ID | |
Cross Reference Brenda |