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Details on Person UniProt:P03956 MMP1
| Class:Id | ReferenceGeneProduct:59385 |
|---|---|
| _chainChangeLog | signal peptide:1-19 added on Fri February 6 2015;propeptide:20-99 added on Fri February 6 2015;chain:100-469 added on Fri February 6 2015;chain:100-269 added on Fri February 6 2015;chain:270-469 added on Fri February 6 2015 |
| _displayName | UniProt:P03956 MMP1 |
| _timestamp | 2024-11-03 19:52:37 |
| chain | signal peptide:1-19 propeptide:20-99 chain:100-469 chain:100-269 chain:270-469 |
| checksum | 4B1361DCF4C54B20 |
| comment | FUNCTION Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X (PubMed:1645757, PubMed:2153297, PubMed:2557822). In case of HIV infection, interacts and cleaves the secreted viral Tat protein, leading to a decrease in neuronal Tat's mediated neurotoxicity (PubMed:16807369).CATALYTIC ACTIVITY Cleavage of the triple helix of collagen at about three-quarters of the length of the molecule from the N-terminus, at 775-Gly-|-Ile-776 in the alpha1(I) chain. Cleaves synthetic substrates and alpha-macroglobulins at bonds where P1' is a hydrophobic residue.COFACTOR Binds 4 Ca(2+) ions per subunit.COFACTOR Binds 2 Zn(2+) ions per subunit.ACTIVITY REGULATION Can be activated without removal of the activation peptide.SUBUNIT (Microbial infection) Interacts with HIV-1 Tat.SUBCELLULAR LOCATION There are two distinct domains in this protein; the catalytic N-terminal, and the C-terminal which is involved in substrate specificity and in binding TIMP (tissue inhibitor of metalloproteinases).DOMAIN The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.PTM Undergoes autolytic cleavage to two major forms (22 kDa and 27 kDa). A minor form (25 kDa) is the glycosylated form of the 22 kDa form. The 27 kDa form has no activity while the 22/25 kDa form can act as activator for collagenase.PTM Tyrosine phosphorylated in platelets by PKDCC/VLK.SIMILARITY Belongs to the peptidase M10A family.ONLINE INFORMATION Collagenase entry |
| description | recommendedName: Interstitial collagenase ecNumber evidence="4 5 6 8"3.4.24.7 alternativeName: Fibroblast collagenase alternativeName: Matrix metalloproteinase-1 shortName: MMP-1 component recommendedName: 22 kDa interstitial collagenase /component component recommendedName: 27 kDa interstitial collagenase /component |
| geneName | MMP1 CLG |
| identifier | P03956 |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Autocatalytic cleavage Calcium Collagen degradation Direct protein sequencing Disulfide bond Extracellular matrix Glycoprotein Host-virus interaction Hydrolase Metal-binding Metalloprotease Phosphoprotein Protease Proteomics identification Reference proteome Repeat Secreted Signal Zinc Zymogen |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9917590] Weiser, Joel, 2024-08-09 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 |
| name | MMP1 |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:6793959] ENSEMBL:ENSG00000196611 MMP1 [Homo sapiens] |
| secondaryIdentifier | MMP1_HUMAN P08156 |
| sequenceLength | 469 |
| species | [Species:48887] Homo sapiens |
| (referenceEntity) | [EntityWithAccessionedSequence:375064] MMP1(100-469) [extracellular region] [Homo sapiens] [EntityWithAccessionedSequence:1602455] MMP1(20-469) [extracellular region] [Homo sapiens] [EntityWithAccessionedSequence:1602470] MMP1(54-469) [extracellular region] [Homo sapiens] [EntityWithAccessionedSequence:1602471] MMP1(20-53) [extracellular region] [Homo sapiens] [EntityWithAccessionedSequence:1604355] MMP1(84-469) [extracellular region] [Homo sapiens] [EntityWithAccessionedSequence:1604367] MMP1(54-83) [extracellular region] [Homo sapiens] [EntityWithAccessionedSequence:8958548] MMP1 [extracellular region] [Homo sapiens] |
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No pathways have been reviewed or authored by UniProt:P03956 MMP1 (59385)
