MMP20
Matrix metalloproteinase-20
Also known as: MMP20_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- O60882
- Gene
- MMP20
- Ensembl
- ENSG00000137674
- Chromosome
- 11
- Canonical length
- 483 aa
- Protein class
- Disease related genes, Enzymes, Human disease related genes, Potential drug targets, Predicted secreted proteins
- Secretome location
- Secreted to extracellular matrix
OverviewNCBI Gene
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 degrades amelogenin, the major protein component of dental enamel matrix, and thus thought to play a role in tooth enamel formation. A mutation in this gene, which alters the normal splice pattern and results in premature termination of the encoded protein, has been associated with amelogenesis imperfecta. This gene is part of a cluster of MMP genes located on chromosome 11q22.3. [provided by RefSeq, Aug 2011]
Canonical amino-acid sequenceUniProt
483 residues, UniProt reviewed canonical sequence.
>O60882|MMP20
1 MKVLPASGLA VFLIMALKFS TAAPSLVAAS PRTWRNNYRL AQAYLDKYYT NKEGHQIGEM
61 VARGSNSMIR KIKELQAFFG LQVTGKLDQT TMNVIKKPRC GVPDVANYRL FPGEPKWKKN
121 TLTYRISKYT PSMSSVEVDK AVEMALQAWS SAVPLSFVRI NSGEADIMIS FENGDHGDSY
181 PFDGPRGTLA HAFAPGEGLG GDTHFDNAEK WTMGTNGFNL FTVAAHEFGH ALGLAHSTDP
241 SALMYPTYKY KNPYGFHLPK DDVKGIQALY GPRKVFLGKP TLPHAPHHKP SIPDLCDSSS
301 SFDAVTMLGK ELLLFKDRIF WRRQVHLRTG IRPSTITSSF PQLMSNVDAA YEVAERGTAY
361 FFKGPHYWIT RGFQMQGPPR TIYDFGFPRH VQQIDAAVYL REPQKTLFFV GDEYYSYDER
421 KRKMEKDYPK NTEEEFSGVN GQIDAAVELN GYIYFFSGPK TYKYDTEKED VVSVVKSSSW
481 IGCLocalizationUniProt · AlphaFold · HPA
Whether an antibody against MMP20 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
- Secreted
- Secreted
- Yes
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.31
- Highest tissue expression
- 0.6 nTPM
Expression across tissuesHPA
Tissue
- testis: 0.6 nTPM
- breast: 0.1 nTPM
- kidney: 0.1 nTPM
- tonsil: 0.1 nTPM
- adipose tissue: 0 nTPM
- adrenal gland: 0 nTPM
Single-cell type
- early spermatids: 94 nCPM
- late primary spermatocytes: 77 nCPM
- epididymal efferent duct absorptive cells: 15 nCPM
- late spermatids: 12 nCPM
- fallopian secretory cells: 9.4 nCPM
- epididymal efferent duct ciliated cells: 7.1 nCPM
Immune cell
- basophil: 0 nTPM
- classical monocyte: 0 nTPM
- eosinophil: 0 nTPM
- gdT-cell: 0 nTPM
- intermediate monocyte: 0 nTPM
- MAIT T-cell: 0 nTPM
Brain region
- amygdala: 0 nTPM
- basal ganglia: 0 nTPM
- cerebellum: 0 nTPM
- cerebral cortex: 0 nTPM
- choroid plexus: 0 nTPM
- hippocampal formation: 0 nTPM
DiseaseUniProt · ClinVar · IEDB · PubMed
Four sources answering four different questions about MMP20.
Disease | AllUniProt
Conditions MMP20 is implicated in, by any mechanism.
- Amelogenesis imperfecta, hypomaturation type, 2A2 (AI2A2) MIM:612529
Disease | GeneticClinVar
12 pathogenic / likely-pathogenic of 210 ClinVar records.
Conditions with pathogenic or likely-pathogenic variants.
- Amelogenesis imperfecta hypomaturation type 2A2
- MMP20-related disorder
- Inborn genetic diseases
- Gastric cancer
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)
- 1.37
- gnomAD pLI
- 0
- gnomAD missense Z
- -0.57
- DepMap mean gene effect
- -0.03
- DepMap dependency class
- selective
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 3% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- amelogenesis
- collagen catabolic process
- extracellular matrix disassembly
- extracellular matrix organization
- protein catabolic process
- proteolysis
- regulation of enamel mineralization
Molecular functions
Cellular components
Protein domainsUniProt · Pfam · InterPro
- Hemopexin-like domain
- Peptidase M10, metallopeptidase
- Peptidoglycan binding-like
- Peptidase, metallopeptidase
- Hemopexin-like repeats
- Peptidase M10A, cysteine switch, zinc binding site
- Peptidase M10A
- Metallopeptidase, catalytic domain superfamily
- Peptidase M10A, catalytic domain
- PGBD-like superfamily
- Hemopexin-like domain superfamily
- Hemopexin
- Matrixin
- Putative peptidoglycan binding domain
KeywordsUniProt
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads MMP20 as an antibody target. Whether an autoantibody or antibody against MMP20 could matter depends on whether native MMP20 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
MMP20 is annotated as secreted, so native MMP20 circulates and is directly accessible to antibodies. Secreted and cell-surface proteins are the autoantibody targets most likely to act like drugs, blocking or depleting the native protein.
Annotation status
The present source text does not explicitly label MMP20 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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