Version 5.4
Homo sapiens Gene: MMP17
Summary
InnateDB Gene IDBG-65039.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol MMP17
Gene Name matrix metallopeptidase 17 (membrane-inserted)
Synonyms MT4-MMP
Species Homo sapiens
Ensembl Gene ENSG00000198598
Encoded Proteins
IDBP-65041
matrix metallopeptidase 17 (membrane-inserted)
IDBP-600863
matrix metallopeptidase 17 (membrane-inserted)
IDBP-592560
matrix metallopeptidase 17 (membrane-inserted)
IDBP-597679
matrix metallopeptidase 17 (membrane-inserted)
IDBP-590879
matrix metallopeptidase 17 (membrane-inserted)
IDBP-585057
matrix metallopeptidase 17 (membrane-inserted)
IDBP-590020
matrix metallopeptidase 17 (membrane-inserted)
IDBP-599448
matrix metallopeptidase 17 (membrane-inserted)
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. The protein encoded by this gene is considered a member of the membrane-type MMP (MT-MMP) subfamily. However, this protein is unique among the MT-MMP's in that it is a GPI-anchored protein rather than a transmembrane protein. The protein activates MMP-2 by cleavage. [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. The protein encoded by this gene is considered a member of the membrane-type MMP (MT-MMP) subfamily. However, this protein is unique among the MT-MMP\'s in that it is a GPI-anchored protein rather than a transmembrane protein. The protein activates MMP-2 by cleavage. [provided by RefSeq, Jul 2008]
Gene Information
Type Protein coding
Genomic Location Chromosome 12:131828393-131851783
Strand Forward strand
Band q24.33
Transcripts
ENST00000360564 ENSP00000353767
ENST00000545671 ENSP00000444603
ENST00000545790 ENSP00000441710
ENST00000535291 ENSP00000441106
ENST00000534865 ENSP00000442104
ENST00000535182
ENST00000542142
ENST00000537848 ENSP00000443727
ENST00000542648 ENSP00000439542
ENST00000535004 ENSP00000445620
ENST00000535271
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 0 experimentally validated interaction(s) in this database.
Gene Ontology

Molecular Function
Accession GO Term
GO:0004222 metalloendopeptidase activity
GO:0005509 calcium ion binding
GO:0008047 enzyme activator activity
GO:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
Biological Process
GO:0006508 proteolysis
GO:0043085 positive regulation of catalytic activity
Cellular Component
GO:0005578 proteinaceous extracellular matrix
GO:0005887 integral component of plasma membrane
GO:0031012 extracellular matrix
GO:0031225 anchored component of membrane
Orthologs
Species
Mus musculus
Bos taurus
Gene ID
Gene Order
ENSMUSG00000029436
View Gene Order
ENSBTAG00000002145
Not yet available
Pathways
NETPATH
REACTOME
REACT_118682
Activation of Matrix Metalloproteinases pathway
REACT_118779
Extracellular matrix organization pathway
REACT_118572
Degradation of the extracellular matrix pathway
KEGG
INOH
PID NCI
Cross-References
SwissProt Q9ULZ9
TrEMBL F5GWR3 F5GZA7 F5H209 F5H249 F5H881
UniProt Splice Variant
Entrez Gene 4326
UniGene Hs.709245
RefSeq NM_016155
HUGO HGNC:7163
OMIM 602285
CCDS CCDS31927
HPRD 03793
IMGT
EMBL AB021225 AC131009 X89576
GenPept BAA82707 CAA61753
RNA Seq Atlas 4326

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