Detail Information for IndEnz0002010162
IED ID IndEnz0002010162
Enzyme Type ID protease010162
Protein Name Metalloproteinase inhibitor 2
Tissue inhibitor of metalloproteinases 2
TIMP-2
Gene Name TIMP2
Organism Canis lupus familiaris (Dog) (Canis familiaris)
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 Laurasiatheria Carnivora Caniformia Canidae (dog coyote wolf fox) Canis Canis lupus (Gray wolf) Canis lupus familiaris (Dog) (Canis familiaris)
Enzyme Sequence MGAAARSLRLALGLLLLATLPRPADACSCSPVHPQQAFCNADVVIRAKAVSVKEVDSGNDIYGNPIKRIQYEIKQIKMFKGPDKDIEFIYTAPSSAVCGVSLDIGGKKEYLIAGKAEGNGKMHITLCDFIVPWDTLSSTQKKSLNHRYQMGCECKITRCPMIPCYISSPDECLWMDWVTEKSINGHQAKFFACIKRSDGSCAWYRGAAPPKQEFLDIEDP
Enzyme Length 220
Uniprot Accession Number Q9TTY1
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); Region (2); Sequence conflict (1); 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. {ECO:0000250}.
Signal Peptide SIGNAL 1..26; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 24,297
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