Detail Information for IndEnz0002012184
IED ID IndEnz0002012184
Enzyme Type ID protease012184
Protein Name Metalloproteinase inhibitor 1
Tissue inhibitor of metalloproteinases 1
TIMP-1
Gene Name TIMP1
Organism Sus scrofa (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 Laurasiatheria Artiodactyla Suina Suidae (pigs) Sus Sus scrofa (Pig)
Enzyme Sequence MSPFAPLASGILLLLWLTAPSRACTCVPPHPQTAFCSSDLVIRAKFVGAPEFNQTASYKRYEIKMTKMFKGFNALGDAPDIRFIYTPAMESVCGYFHRSQNRSQEFLIAGQLWNGHLHITTCSFVAPWNSLSSAQRQGFTEIYAAGCEECTVFPCTSIPCKLQSDTHCLWTDQLLTGSDKGFQSRHLACMPREPGMCTWQSLRPRVA
Enzyme Length 207
Uniprot Accession Number P35624
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Metalloproteinase inhibitor that functions by forming one to one complexes with target metalloproteinases, such as collagenases, and irreversibly inactivates them by binding to their catalytic zinc cofactor. Acts on MMP1, MMP2, MMP3, MMP7, MMP8, MMP9, MMP10, MMP11, MMP12, MMP13 and MMP16. Does not act on MMP14. Also functions as a growth factor that regulates cell differentiation, migration and cell death and activates cellular signaling cascades via CD63 and ITGB1. Plays a role in integrin signaling (By similarity). {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Disulfide bond (6); Domain (1); Glycosylation (2); Metal binding (1); Modified residue (1); Region (2); Sequence conflict (6); Signal peptide (1)
Keywords Disulfide bond;Glycoprotein;Growth factor;Metal-binding;Metalloenzyme inhibitor;Metalloprotease inhibitor;Phosphoprotein;Protease inhibitor;Reference proteome;Secreted;Signal;Zinc
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1312961}.
Modified Residue MOD_RES 178; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P01033
Post Translational Modification PTM: The activity of TIMP1 is dependent on the presence of disulfide bonds. {ECO:0000250}.; PTM: N-glycosylated. {ECO:0000250}.
Signal Peptide SIGNAL 1..23; /evidence=ECO:0000250
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 23,099
Kinetics
Metal Binding METAL 24; /note=Zinc; via amino nitrogen and carbonyl oxygen; shared with metalloproteinase partner; /evidence=ECO:0000250|UniProtKB:P16035
Rhea ID
Cross Reference Brenda