Version 5.4
Homo sapiens Gene: MMP11
Summary
InnateDB Gene IDBG-2572.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol MMP11
Gene Name matrix metallopeptidase 11 (stromelysin 3)
Synonyms SL-3; ST3; STMY3
Species Homo sapiens
Ensembl Gene ENSG00000099953
Encoded Proteins
IDBP-2574
matrix metallopeptidase 11 (stromelysin 3)
IDBP-366374
matrix metallopeptidase 11 (stromelysin 3)
IDBP-366388
matrix metallopeptidase 11 (stromelysin 3)
IDBP-366397
matrix metallopeptidase 11 (stromelysin 3)
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 activated intracellularly by furin within the constitutive secretory pathway. Also in contrast to other MMP's, this enzyme cleaves alpha 1-proteinase inhibitor but weakly degrades structural proteins of the extracellular matrix. [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 activated intracellularly by furin within the constitutive secretory pathway. Also in contrast to other MMP\'s, this enzyme cleaves alpha 1-proteinase inhibitor but weakly degrades structural proteins of the extracellular matrix. [provided by RefSeq, Jul 2008]
Gene Information
Type Protein coding
Genomic Location Chromosome 22:23768226-23784316
Strand Forward strand
Band q11.23
Transcripts
ENST00000215743 ENSP00000215743
ENST00000428253 ENSP00000409860
ENST00000437086 ENSP00000408070
ENST00000434318 ENSP00000412107
ENST00000465385
ENST00000477567
ENST00000489582
ENST00000465730
ENST00000460352
ENST00000493132
ENST00000492464
ENST00000488363
ENST00000480185
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:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
Biological Process
GO:0006508 proteolysis
GO:0007275 multicellular organismal development
GO:0022617 extracellular matrix disassembly
GO:0030198 extracellular matrix organization
GO:0030199 collagen fibril organization
GO:0030574 collagen catabolic process
GO:0045599 negative regulation of fat cell differentiation
GO:0071711 basement membrane organization
Cellular Component
GO:0005576 extracellular region
GO:0005578 proteinaceous extracellular matrix
GO:0005796 Golgi lumen
GO:0031012 extracellular matrix
Orthologs
Species
Mus musculus
Bos taurus
Gene ID
Gene Order
ENSMUSG00000000901
View Gene Order
ENSBTAG00000006108
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 F8WDI7
UniProt Splice Variant
Entrez Gene 4320
UniGene Hs.143751
RefSeq NM_005940
HUGO HGNC:7157
OMIM 185261
CCDS CCDS13816
HPRD 01705
IMGT
EMBL AP000349
GenPept
RNA Seq Atlas 102725056 4320

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