Detail Information for IndEnz0002010161
IED ID IndEnz0002010161
Enzyme Type ID protease010161
Protein Name Metalloproteinase inhibitor 2
Collagenase inhibitor
Tissue inhibitor of metalloproteinases 2
TIMP-2
Gene Name TIMP2
Organism Bos taurus (Bovine)
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 Artiodactyla Ruminantia Pecora Bovidae Bovinae Bos (oxen cattle) Bos taurus (Bovine)
Enzyme Sequence MGAAARSLPLAFCLLLLGTLLPRADACSCSPVHPQQAFCNADIVIRAKAVNKKEVDSGNDIYGNPIKRIQYEIKQIKMFKGPDQDIEFIYTAPAAAVCGVSLDIGGKKEYLIAGKAEGNGNMHITLCDFIVPWDTLSATQKKSLNHRYQMGCECKITRCPMIPCYISSPDECLWMDWVTEKNINGHQAKFFACIKRSDGSCAWYRGAAPPKQEFLDIEDP
Enzyme Length 220
Uniprot Accession Number P16368
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 Beta strand (15); Chain (1); Disulfide bond (6); Domain (1); Helix (7); Metal binding (1); Region (1); Sequence conflict (6); Signal peptide (1); Site (4); Turn (1)
Keywords 3D-structure;Direct protein sequencing;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:0000269|PubMed:2551903, ECO:0000269|PubMed:3005321"
Structure 3D X-ray crystallography (3)
Cross Reference PDB 1BQQ; 1BUV; 2E2D;
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 24,355
Kinetics
Metal Binding METAL 27; /note="Zinc; via amino nitrogen and carbonyl oxygen; shared with metalloproteinase partner"; /evidence="ECO:0000269|PubMed:17196980, ECO:0007744|PDB:2E2D"
Rhea ID
Cross Reference Brenda