| IED ID | IndEnz0002001683 |
| Enzyme Type ID | protease001683 |
| Protein Name |
Metalloproteinase inhibitor 1 Tissue inhibitor of metalloproteinases 1 TIMP-1 |
| Gene Name | Timp1 Timp-1 |
| Organism | Rattus norvegicus (Rat) |
| 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 Muridae Murinae Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MAPFASLASGILLLLSLIASSKACSCAPTHPQTAFCNSDLVIRAKFMGSPEIIETTLYQRYEIKMTKMLKGFDAVGNATGFRFAYTPAMESLCGYVHKSQNRSEEFLIAGRLRNGNLHITACSFLVPWHNLSPAQQKAFVKTYSAGCGVCTVFPCSAIPCKLESDSHCLWTDQILMGSEKGYQSDHFACLPRNPDLCTWQYLGVSMTRSLPLAKAEA |
| Enzyme Length | 217 |
| Uniprot Accession Number | P30120 |
| 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. Also stimulates steroidogenesis by Leydig and ovarian granuloma cells; procathepsin L is required for maximal activity. {ECO:0000269|PubMed:1309971, ECO:0000269|PubMed:7777858}. |
| 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 (12); Signal peptide (1); Site (1) |
| Keywords | Direct protein sequencing;Disulfide bond;Glycoprotein;Growth factor;Metal-binding;Metalloenzyme inhibitor;Metalloprotease inhibitor;Phosphoprotein;Protease inhibitor;Reference proteome;Secreted;Signal;Steroidogenesis;Zinc |
| Interact With | |
| Induction | INDUCTION: By follicle-stimulating hormone (FSH). {ECO:0000269|PubMed:7777858}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1309971, ECO:0000269|PubMed:7777858}. |
| 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:0000269|PubMed:1309971}. |
| Signal Peptide | SIGNAL 1..23; /evidence="ECO:0000269|PubMed:1309971, ECO:0000269|PubMed:7777858" |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10435007; 10719361; 10773234; 12081564; 1327205; 15128910; 15375341; 15389776; 16208432; 16683235; 17555880; 17569353; 17569694; 17569872; 17977875; 18278151; 19063844; 19134282; 21846328; 22633097; 23318412; 25842729; 28659595; 9472898; 9579471; |
| Motif | |
| Gene Encoded By | |
| Mass | 23,794 |
| 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 |