Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

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



Sequence databases


3D structure databases


Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.4.24.7. 5301.

Family and domain databases


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

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.