MMP3
Stromelysin-1
Also known as: MMP3_HUMAN, STMY, STMY1
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- P08254
- Gene
- MMP3
- Ensembl
- ENSG00000149968
- Chromosome
- 11
- Canonical length
- 477 aa
- Protein class
- Cancer-related genes, Candidate cardiovascular disease genes, Disease related genes, Enzymes, Human disease related genes, Plasma proteins, Potential drug targets, Predicted intracellular proteins, Predicted secreted proteins
- Subcellular location
- Vesicles
- 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. This gene encodes an enzyme which degrades fibronectin, laminin, collagens III, IV, IX, and X, and cartilage proteoglycans. The enzyme is thought to be involved in wound repair, progression of atherosclerosis, and tumor initiation. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. [provided by RefSeq, Jul 2008]
Canonical amino-acid sequenceUniProt
477 residues, UniProt reviewed canonical sequence.
>P08254|MMP3
1 MKSLPILLLL CVAVCSAYPL DGAARGEDTS MNLVQKYLEN YYDLKKDVKQ FVRRKDSGPV
61 VKKIREMQKF LGLEVTGKLD SDTLEVMRKP RCGVPDVGHF RTFPGIPKWR KTHLTYRIVN
121 YTPDLPKDAV DSAVEKALKV WEEVTPLTFS RLYEGEADIM ISFAVREHGD FYPFDGPGNV
181 LAHAYAPGPG INGDAHFDDD EQWTKDTTGT NLFLVAAHEI GHSLGLFHSA NTEALMYPLY
241 HSLTDLTRFR LSQDDINGIQ SLYGPPPDSP ETPLVPTEPV PPEPGTPANC DPALSFDAVS
301 TLRGEILIFK DRHFWRKSLR KLEPELHLIS SFWPSLPSGV DAAYEVTSKD LVFIFKGNQF
361 WAIRGNEVRA GYPRGIHTLG FPPTVRKIDA AISDKEKNKT YFFVEDKYWR FDEKRNSMEP
421 GFPKQIAEDF PGIDSKIDAV FEEFGFFYFF TGSSQLEFDP NAKKVTHTLK SNSWLNCLocalizationUniProt · AlphaFold · HPA
Whether an antibody against MMP3 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)
- 0.27
- Highest tissue expression
- 286 nTPM
Expression across tissuesHPA
Tissue
- salivary gland: 286 nTPM
- adipose tissue: 99 nTPM
- skin: 72 nTPM
- breast: 46 nTPM
- skeletal muscle: 41 nTPM
- endometrium: 36 nTPM
Single-cell type
- fibroblasts: 89 nCPM
- smooth muscle cells: 27 nCPM
- early spermatids: 23 nCPM
- extravillous trophoblasts: 21 nCPM
- late primary spermatocytes: 21 nCPM
- ocular epithelial cells: 18 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
- thalamus: 15 nTPM
- hypothalamus: 3.1 nTPM
- cerebral cortex: 2.8 nTPM
- medulla oblongata: 0.6 nTPM
- midbrain: 0.6 nTPM
- basal ganglia: 0.5 nTPM
DiseaseUniProt · ClinVar · IEDB · PubMed
Four sources answering four different questions about MMP3.
Disease | AllUniProt
Conditions MMP3 is implicated in, by any mechanism.
- Coronary heart disease 6 (CHDS6) MIM:614466
ReferencesPubMed · IEDB
Publications for MMP3 from three distinct lines of evidence, kept separate because they answer different questions: whether antibodies are directed at the protein, whether a B-cell epitope has been mapped on it, and whether a T-cell epitope has. Each is labelled with its source.
Reference: AutoantibodyPubMed
1 publication
- Autoantibody against matrix metalloproteinase-3 in patients with systemic sclerosis.
2004 · Clin Exp Immunol · RCR 1.7 · 70 citations
Sources: PubMed — antigen-level antibody evidence from a custom retrieval. Records matching a controlled set of autoantibody terms (the MeSH descriptors Autoantibodies and Autoantigens, with title and abstract term variants) were obtained through NCBI E-utilities, and their titles and abstracts parsed for constructions that direct an antibody at a named protein rather than for co-occurrence. Captured names were resolved against UniProt nomenclature and each antigen adjudicated individually against the source text. Bibliographic records from PubMed and MeSH, U.S. National Library of Medicine; citation metrics from NIH iCite (Hutchins et al., PLoS Biology 2016). Titles link to PubMed; abstracts are not reproduced here. The NLM does not endorse this analysis.
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)
- 1.42
- gnomAD pLI
- 0
- gnomAD missense Z
- -0.64
- DepMap mean gene effect
- 0.04
- 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
- cellular response to amino acid stimulus
- cellular response to lipopolysaccharide
- cellular response to nitric oxide
- cellular response to reactive oxygen species
- cellular response to UV-A
- collagen catabolic process
- extracellular matrix disassembly
- extracellular matrix organization
- innate immune response
- negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
- negative regulation of reactive oxygen species metabolic process
- positive regulation of protein-containing complex assembly
- protein catabolic process
- proteolysis
- regulation of cell migration
- regulation of neuroinflammatory response
- response to amyloid-beta
Molecular functions
- endopeptidase activity
- metalloendopeptidase activity
- metallopeptidase activity
- peptidase activity
- serine-type endopeptidase 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
- Metallopeptidase, catalytic domain superfamily
- Peptidase M10A, catalytic domain
- PGBD-like superfamily
- Hemopexin-like domain superfamily
- Hemopexin
- Matrixin
- Putative peptidoglycan binding domain
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of MMP3 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads MMP3 as an antibody target. Whether an autoantibody or antibody against MMP3 could matter depends on whether native MMP3 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
MMP3 is annotated as secreted, so native MMP3 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 MMP3 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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