MMP15
Matrix metalloproteinase-15
Also known as: MMP15_HUMAN, MT2-MMP, MTMMP2, SMCP-2
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- P51511
- Gene
- MMP15
- Ensembl
- ENSG00000102996
- Chromosome
- 16
- Canonical length
- 669 aa
- Protein class
- Cancer-related genes, Enzymes, Plasma proteins, Predicted intracellular proteins, Predicted membrane proteins
- Subcellular location
- Nucleoplasm,Plasma membrane,Cytosol
OverviewNCBI Gene
This gene encodes a member of the peptidase M10 family and membrane-type subfamily of matrix metalloproteinases (MMPs). Proteins in this 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. Members of this subfamily contain a transmembrane domain suggesting that these proteins are expressed at the cell surface rather than secreted. The encoded preproprotein is proteolytically processed to generate the mature protease. This protein may play a role in cancer progression. [provided by RefSeq, Jan 2016]
Canonical amino-acid sequenceUniProt
669 residues, UniProt reviewed canonical sequence.
>P51511|MMP15
1 MGSDPSAPGR PGWTGSLLGD REEAARPRLL PLLLVLLGCL GLGVAAEDAE VHAENWLRLY
61 GYLPQPSRHM STMRSAQILA SALAEMQRFY GIPVTGVLDE ETKEWMKRPR CGVPDQFGVR
121 VKANLRRRRK RYALTGRKWN NHHLTFSIQN YTEKLGWYHS MEAVRRAFRV WEQATPLVFQ
181 EVPYEDIRLR RQKEADIMVL FASGFHGDSS PFDGTGGFLA HAYFPGPGLG GDTHFDADEP
241 WTFSSTDLHG NNLFLVAVHE LGHALGLEHS SNPNAIMAPF YQWKDVDNFK LPEDDLRGIQ
301 QLYGTPDGQP QPTQPLPTVT PRRPGRPDHR PPRPPQPPPP GGKPERPPKP GPPVQPRATE
361 RPDQYGPNIC DGDFDTVAML RGEMFVFKGR WFWRVRHNRV LDNYPMPIGH FWRGLPGDIS
421 AAYERQDGRF VFFKGDRYWL FREANLEPGY PQPLTSYGLG IPYDRIDTAI WWEPTGHTFF
481 FQEDRYWRFN EETQRGDPGY PKPISVWQGI PASPKGAFLS NDAAYTYFYK GTKYWKFDNE
541 RLRMEPGYPK SILRDFMGCQ EHVEPGPRWP DVARPPFNPH GGAEPGADSA EGDVGDGDGD
601 FGAGVNKDGG SRVVVQMEEV ARTVNVVMVL VPLLLLLCVL GLTYALVQMQ RKGAPRVLLY
661 CKRSLQEWVLocalizationUniProt · AlphaFold · HPA
Whether an antibody against MMP15 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Cell surface
- Secreted
- No
- Transmembrane segments
- 1
- Mean surface accessibility (rSASA)
- 0.39
- Highest tissue expression
- 51 nTPM
Expression across tissuesHPA
Tissue
- liver: 51 nTPM
- thyroid gland: 46 nTPM
- heart muscle: 41 nTPM
- duodenum: 38 nTPM
- testis: 35 nTPM
- small intestine: 31 nTPM
Single-cell type
- extravillous trophoblasts: 87 nCPM
- colonocytes: 86 nCPM
- enterocytes: 69 nCPM
- cytotrophoblasts: 64 nCPM
- cholangiocytes: 60 nCPM
- syncytiotrophoblasts: 53 nCPM
Immune cell
- plasmacytoid DC: 0.6 nTPM
- basophil: 0 nTPM
- classical monocyte: 0 nTPM
- eosinophil: 0 nTPM
- gdT-cell: 0 nTPM
- intermediate monocyte: 0 nTPM
Brain region
- thalamus: 39 nTPM
- pons: 35 nTPM
- medulla oblongata: 22 nTPM
- cerebral cortex: 22 nTPM
- midbrain: 21 nTPM
- amygdala: 18 nTPM
DiseaseUniProt · ClinVar · IEDB · PubMed
Four sources answering four different questions about MMP15.
Disease | GeneticClinVar
1 pathogenic / likely-pathogenic of 144 ClinVar records.
Conditions with pathogenic or likely-pathogenic variants.
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 0.48
- gnomAD pLI
- 0.07
- gnomAD missense Z
- 1.33
- DepMap mean gene effect
- -0.1
- DepMap dependency class
- selective
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 4% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- collagen catabolic process
- endodermal cell differentiation
- extracellular matrix disassembly
- extracellular matrix organization
- protein modification process
- proteolysis
- response to estradiol
Molecular functions
- enzyme activator activity
- metalloaminopeptidase activity
- metalloendopeptidase activity
- zinc ion binding
Cellular components
Protein domainsUniProt · Pfam · InterPro
- Hemopexin-like domain
- Peptidase M10, metallopeptidase
- Peptidoglycan binding-like
- Peptidase, metallopeptidase
- Hemopexin, conserved site
- Hemopexin-like repeats
- Peptidase M10A, cysteine switch, zinc binding site
- Peptidase M10A
- Peptidase M10A, matrix metallopeptidase, C-terminal
- Metallopeptidase, catalytic domain superfamily
- Peptidase M10A, catalytic domain
- PGBD-like superfamily
- Hemopexin-like domain superfamily
- Hemopexin
- Matrixin
- Putative peptidoglycan binding domain
- Domain of unknown function (DUF3377)
KeywordsUniProt
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads MMP15 as an antibody target. Whether an autoantibody or antibody against MMP15 could matter depends on whether native MMP15 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
MMP15 is annotated at the cell surface, where native MMP15 is exposed to circulating antibodies and is a prime autoantibody target that could block, deplete, or overstimulate it.
Annotation status
The present source text does not explicitly label MMP15 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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