Detail Information for IndEnz0002001686
IED ID IndEnz0002001686
Enzyme Type ID protease001686
Protein Name Metalloproteinase inhibitor 2
Tissue inhibitor of metalloproteinases 2
TIMP-2
Fragment
Gene Name TIMP2
Organism Cricetulus longicaudatus (Long-tailed dwarf hamster) (Chinese hamster)
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 Myomorpha (mice and others) Muroidea Cricetidae Cricetinae (hamsters) Cricetulus Cricetulus longicaudatus (Long-tailed dwarf hamster) (Chinese hamster)
Enzyme Sequence RACSCSPVHPQQAFCNADVVIRAKAVSEKEVDSGNDIYGNPIKRIQYEIKQIKMFKGPDKDIEFIYTAPSSAVCGVSLDVGGKKEYLIAGKAEGDGKMHITLCDFIVPWDTLSTTQKKSLNHRYQMGCECKITRCPMIPCYISSPDECLWMDWVTEKSINGHQAKFFACIKRSDGSCAWYRGAAPPKQEFLDIEDP
Enzyme Length 196
Uniprot Accession Number Q60453
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. {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Disulfide bond (6); Domain (1); Metal binding (1); Non-terminal residue (1); Region (2); Signal peptide (1); Site (3)
Keywords Disulfide bond;Metal-binding;Metalloenzyme inhibitor;Metalloprotease inhibitor;Protease inhibitor;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. {ECO:0000250}.
Signal Peptide SIGNAL <1..2; /evidence=ECO:0000250
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 21,941
Kinetics
Metal Binding METAL 3; /note=Zinc; via amino nitrogen and carbonyl oxygen; shared with metalloproteinase partner; /evidence=ECO:0000250|UniProtKB:P16035
Rhea ID
Cross Reference Brenda