| Primary information |
|---|
| ID | 12264 |
| Uniprot ID | P30120 |
| Description | Metalloproteinase inhibitor 1 (Tissue inhibitor of metalloproteinases 1) (TIMP-1) |
| Organism | Rattus norvegicus |
| Txonomy | 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; Muridae; Murinae; Rattus; Rattus norvegicus (Rat) |
| Subcellular Location | Secreted |
| Developmental Stage | NA |
| Similarity | Belongs to the protease inhibitor I35 (TIMP) family. |
| Tissue Specificity | NA |
| Post Translational Modification | The activity of TIMP1 is dependent on the presence of disulfide bonds. |
| 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. Also stimulates steroidogenesis by Leydig and ovarian granuloma cells; procathepsin L is required for maximal activity. |
| Length | 217 |
| Molecular Weight | 23 |
| Name | Metalloproteinase inhibitor 1 |
| Sequence | SCAPTHPQTAFCNSDLVIRAKFMGSPEIIETTLYQRYEIKMTKMLKGFDAVGNATGFRFAYTPAMESLCGYVHKSQNRSEEFLIAGRLRNGNLHITACSFLVPWHNLSPAQQKAFVKTYSAGCGVCTVFPCSAIPCKLESDSHCLWTDQILMGSEKGYQSDHFACLPRNPDLCTWQYLGVSMTRSLPLAKAEA |
| Sequence map | 27-37 |
| PDB ID | NA |
| Drugpedia | NA |
| Receptor | NA |
| Domain | NA |
| Pharmaceutical Use | NA
|