P81563 (MMP1_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 48.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Interstitial collagenase EC=3.4.24.7 Alternative name(s): Fibroblast collagenase Matrix metalloproteinase-1 Short name=MMP-1 Myocardial collagenase | ||
| Gene names |
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| Organism | Rattus norvegicus (Rat) | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 15 AA. |
| Sequence status | Fragment. |
| Protein existence | Evidence 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 | Secreted › extracellular space › extracellular matrix By similarity. |
| Post-translational modification | The N-terminus is blocked. |
| Sequence similarities | Belongs to the peptidase M10A family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Collagen degradation |
| Cellular component | Extracellular matrix Secreted |
| Ligand | Calcium Zinc |
| Molecular function | Hydrolase Metalloprotease Protease |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological process | collagen catabolic process Inferred from electronic annotation. Source: UniProtKB-KW proteolysisInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | proteinaceous extracellular matrix Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | metallopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
References
| [1] | "Myocardial collagenase: purification and structural characterization." Tyagi S.C., Cleutjens J.P.M. Can. J. Cardiol. 12:165-171(1996) [PubMed: 8605638] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Heart. |
Cross-references
Sequence databases | |
|---|---|
| IPI | IPI00202367. |
3D structure databases | |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Gene expression databases | |
| Genevestigator | P81563. |
Family and domain databases | |
| ProtoNet | Search... |
Entry information
| Entry name | MMP1_RAT | ||||||||
| Accession | Primary (citable) accession number: P81563 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with