Version 5.4
Homo sapiens Gene: MMP8
Summary
InnateDB Gene IDBG-69164.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol MMP8
Gene Name matrix metallopeptidase 8 (neutrophil collagenase)
Synonyms CLG1; HNC; MMP-8; PMNL-CL
Species Homo sapiens
Ensembl Gene ENSG00000118113
Encoded Proteins
IDBP-69166
matrix metallopeptidase 8 (neutrophil collagenase)
IDBP-382508
matrix metallopeptidase 8 (neutrophil collagenase)
IDBP-593108
matrix metallopeptidase 8 (neutrophil collagenase)
IDBP-600268
matrix metallopeptidase 8 (neutrophil collagenase)
IDBP-591671
matrix metallopeptidase 8 (neutrophil collagenase)
IDBP-589598
matrix metallopeptidase 8 (neutrophil collagenase)
Protein Structure
Useful resources Stemformatics EHFPI ImmGen
Entrez Gene
Summary Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. However, the enzyme encoded by this gene is stored in secondary granules within neutrophils and is activated by autolytic cleavage. Its function is degradation of type I, II and III collagens. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. [provided by RefSeq, Jul 2008]
Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP\'s are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. However, the enzyme encoded by this gene is stored in secondary granules within neutrophils and is activated by autolytic cleavage. Its function is degradation of type I, II and III collagens. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. [provided by RefSeq, Jul 2008]
Gene Information
Type Protein coding
Genomic Location Chromosome 11:102711795-102727050
Strand Reverse strand
Band q22.2
Transcripts
ENST00000236826 ENSP00000236826
ENST00000438475 ENSP00000401004
ENST00000528662 ENSP00000431431
ENST00000533258 ENSP00000437173
ENST00000531168 ENSP00000433812
ENST00000532799 ENSP00000431938
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 8 experimentally validated interaction(s) in this database.
Experimentally validated
Total 8 [view]
Protein-Protein 6 [view]
Protein-DNA 2 [view]
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Gene Ontology

Molecular Function
Accession GO Term
GO:0004222 metalloendopeptidase activity
GO:0004252 serine-type endopeptidase activity
GO:0005509 calcium ion binding
GO:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
Biological Process
GO:0006508 proteolysis
GO:0022617 extracellular matrix disassembly
GO:0030198 extracellular matrix organization
GO:0030574 collagen catabolic process
GO:0045087 innate immune response
Cellular Component
GO:0005576 extracellular region
GO:0005578 proteinaceous extracellular matrix
GO:0005615 extracellular space
GO:0031012 extracellular matrix
Orthologs
Species
Mus musculus
Bos taurus
Gene ID
Gene Order
ENSMUSG00000005800
View Gene Order
ENSBTAG00000046732
Not yet available
Pathways
NETPATH
REACTOME
REACT_118682
Activation of Matrix Metalloproteinases pathway
REACT_150401
Collagen degradation pathway
REACT_118779
Extracellular matrix organization pathway
REACT_118572
Degradation of the extracellular matrix pathway
KEGG
INOH
PID NCI
Cross-References
SwissProt
TrEMBL E9PJB3
UniProt Splice Variant
Entrez Gene 4317
UniGene Hs.161839
RefSeq NM_002424 XM_006718841
HUGO HGNC:7175
OMIM 120355
CCDS CCDS8320
HPRD 00385
IMGT
EMBL AP000647
GenPept
RNA Seq Atlas 4317

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca