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Interstitial collagenase



Rattus norvegicus (Rat)
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli


Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X. May play a role in the deterioration of the heart wall extracellular matrix proteins during the onset of dilated cardiomyopathy.

Catalytic activityi

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 alpha-1(I) chain. Cleaves synthetic substrates and alpha-macroglobulins at bonds where P1' is a hydrophobic residue.


Protein has several cofactor binding sites:
  • Ca2+By similarityNote: Binds 4 Ca2+ ions per subunit.By similarity
  • Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Enzyme regulationi

Can be activated without removal of the activation peptide.

GO - Molecular functioni

GO - Biological processi


Molecular functionHydrolase, Metalloprotease, Protease
Biological processCollagen degradation
LigandCalcium, Zinc

Enzyme and pathway databases

BRENDAi3.4.24.7. 5301.

Names & Taxonomyi

Protein namesi
Recommended name:
Interstitial collagenase (EC:
Alternative name(s):
Fibroblast collagenase
Matrix metalloproteinase-1
Short name:
Myocardial collagenase
Gene namesi
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
  • UP000002494 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000078182‹1 – ›15Interstitial collagenaseAdd BLAST›15

Post-translational modificationi

The N-terminus is blocked.
Tyrosine phosphorylated in platelets by PKDCC/VLK.By similarity

Keywords - PTMi


Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M10A family.Curated


Sequence statusi: Fragment.

Mass (Da):1,787
Last modified:May 30, 2000 - v1

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11
Non-terminal residuei151

Sequence databases


Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiMMP1_RAT
AccessioniPrimary (citable) accession number: P81563
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: May 10, 2017
This is version 61 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program


Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome


  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families