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P81563 (MMP1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Interstitial collagenase

EC=3.4.24.7
Alternative name(s):
Fibroblast collagenase
Matrix metalloproteinase-1
Short name=MMP-1
Myocardial collagenase
Gene names
Name:Mmp1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length15 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Cofactor

Binds 4 calcium ions per subunit By similarity.

Binds 2 zinc ions per subunit By similarity.

Enzyme regulation

Can be activated without removal of the activation peptide.

Subcellular location

Secretedextracellular spaceextracellular matrix By similarity.

Post-translational modification

The N-terminus is blocked.

Sequence similarities

Belongs to the peptidase M10A family.

Ontologies

Keywords
   Biological processCollagen degradation
   Cellular componentExtracellular matrix
Secreted
   LigandCalcium
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcollagen catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentproteinaceous extracellular matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetallopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – ›15›15Interstitial collagenase
PRO_0000078182

Experimental info

Non-terminal residue11
Non-terminal residue151

Sequences

Sequence LengthMass (Da)Tools
P81563 [UniParc].

Last modified May 30, 2000. Version 1.
Checksum: 15A57D24C0F6FD80

FASTA151,787
        10 
DTLKSEKNAD FKDLY 

« Hide

References

[1]"Myocardial collagenase: purification and structural characterization."
Tyagi S.C., Cleutjens J.P.M.
Can. J. Cardiol. 12:165-171(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Heart.

Cross-references

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Gene expression databases

GenevestigatorP81563.

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameMMP1_RAT
AccessionPrimary (citable) accession number: P81563
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: May 14, 2014
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries