MMP28
Matrix metalloproteinase-28
Also known as: EPILYSIN, MM28, MMP-25, MMP-28, MMP28_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q9H239
- Gene
- MMP28
- Ensembl
- ENSG00000271447
- Chromosome
- 17
- Canonical length
- 520 aa
- Protein class
- Enzymes, Plasma proteins, Predicted intracellular proteins, 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 for both normal physiological processes, such as embryonic development, reproduction and tissue remodeling, and disease processes, such as asthma and metastasis. This gene encodes a secreted enzyme that degrades casein. Its expression pattern suggests that it plays a role in tissue homeostasis and in wound repair. Alternative splicing of this gene results in multiple transcript variants. [provided by RefSeq, Apr 2014]
Canonical amino-acid sequenceUniProt
520 residues, UniProt reviewed canonical sequence.
>Q9H239|MMP28
1 MVARVGLLLR ALQLLLWGHL DAQPAERGGQ ELRKEAEAFL EKYGYLNEQV PKAPTSTRFS
61 DAIRAFQWVS QLPVSGVLDR ATLRQMTRPR CGVTDTNSYA AWAERISDLF ARHRTKMRRK
121 KRFAKQGNKW YKQHLSYRLV NWPEHLPEPA VRGAVRAAFQ LWSNVSALEF WEAPATGPAD
181 IRLTFFQGDH NDGLGNAFDG PGGALAHAFL PRRGEAHFDQ DERWSLSRRR GRNLFVVLAH
241 EIGHTLGLTH SPAPRALMAP YYKRLGRDAL LSWDDVLAVQ SLYGKPLGGS VAVQLPGKLF
301 TDFETWDSYS PQGRRPETQG PKYCHSSFDA ITVDRQQQLY IFKGSHFWEV AADGNVSEPR
361 PLQERWVGLP PNIEAAAVSL NDGDFYFFKG GRCWRFRGPK PVWGLPQLCR AGGLPRHPDA
421 ALFFPPLRRL ILFKGARYYV LARGGLQVEP YYPRSLQDWG GIPEEVSGAL PRPDGSIIFF
481 RDDRYWRLDQ AKLQATTSGR WATELPWMGC WHANSGSALFLocalizationUniProt · AlphaFold · HPA
Whether an antibody against MMP28 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)
- 0.29
- Highest tissue expression
- 29 nTPM
Expression across tissuesHPA
Tissue
- skin: 29 nTPM
- testis: 28 nTPM
- basal ganglia: 22 nTPM
- amygdala: 21 nTPM
- colon: 20 nTPM
- urinary bladder: 19 nTPM
Single-cell type
- astrocytes: 100 nCPM
- papillary tip epithelial cells: 79 nCPM
- late spermatids: 55 nCPM
- podocytes: 50 nCPM
- renal collecting duct principal cells: 34 nCPM
- early spermatids: 33 nCPM
Immune cell
- naive CD4 T-cell: 6.3 nTPM
- naive CD8 T-cell: 3.8 nTPM
- MAIT T-cell: 1.1 nTPM
- memory CD8 T-cell: 1 nTPM
- NK-cell: 0.9 nTPM
- plasmacytoid DC: 0.9 nTPM
Brain region
- thalamus: 23 nTPM
- amygdala: 22 nTPM
- basal ganglia: 20 nTPM
- midbrain: 20 nTPM
- cerebral cortex: 16 nTPM
- hippocampal formation: 16 nTPM
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)
- 1.85
- gnomAD pLI
- 0
- gnomAD missense Z
- 0.57
- DepMap mean gene effect
- -0.08
- 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
- extracellular matrix organization
- negative regulation of macrophage chemotaxis
- proteolysis
Molecular functions
Cellular components
Protein domainsUniProt · Pfam · InterPro
- Hemopexin-like domain
- Peptidase M10, metallopeptidase
- Peptidoglycan binding-like
- Peptidase, metallopeptidase
- Hemopexin-like repeats
- 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 MMP28 as an antibody target. Whether an autoantibody or antibody against MMP28 could matter depends on whether native MMP28 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
MMP28 is annotated as secreted, so native MMP28 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 MMP28 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
Loading the interactive Seroatlas protein explorer...