MMP8
Neutrophil collagenase
Also known as: CLG1, MMP8_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- P22894
- Gene
- MMP8
- Ensembl
- ENSG00000118113
- Chromosome
- 11
- Canonical length
- 467 aa
- Protein class
- Cancer-related genes, Enzymes, Plasma proteins, Predicted intracellular proteins, Predicted secreted proteins
- Subcellular location
- Vesicles
- Secretome location
- Secreted to extracellular matrix
OverviewNCBI Gene
This gene encodes a member of the matrix metalloproteinase (MMP) family of proteins. These proteins are involved in the breakdown of extracellular matrix in embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Proteolysis at different sites on this protein results in multiple active forms of the enzyme with distinct N-termini. This protein functions in the degradation of type I, II and III collagens. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2015]
Canonical amino-acid sequenceUniProt
467 residues, UniProt reviewed canonical sequence.
>P22894|MMP8
1 MFSLKTLPFL LLLHVQISKA FPVSSKEKNT KTVQDYLEKF YQLPSNQYQS TRKNGTNVIV
61 EKLKEMQRFF GLNVTGKPNE ETLDMMKKPR CGVPDSGGFM LTPGNPKWER TNLTYRIRNY
121 TPQLSEAEVE RAIKDAFELW SVASPLIFTR ISQGEADINI AFYQRDHGDN SPFDGPNGIL
181 AHAFQPGQGI GGDAHFDAEE TWTNTSANYN LFLVAAHEFG HSLGLAHSSD PGALMYPNYA
241 FRETSNYSLP QDDIDGIQAI YGLSSNPIQP TGPSTPKPCD PSLTFDAITT LRGEILFFKD
301 RYFWRRHPQL QRVEMNFISL FWPSLPTGIQ AAYEDFDRDL IFLFKGNQYW ALSGYDILQG
361 YPKDISNYGF PSSVQAIDAA VFYRSKTYFF VNDQFWRYDN QRQFMEPGYP KSISGAFPGI
421 ESKVDAVFQQ EHFFHVFSGP RYYAFDLIAQ RVTRVARGNK WLNCRYGLocalizationUniProt · AlphaFold · HPA
Whether an antibody against MMP8 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)
- 0.28
- Highest tissue expression
- 474 nTPM
Expression across tissuesHPA
Tissue
- bone marrow: 474 nTPM
- spleen: 14 nTPM
- lung: 4.1 nTPM
- thymus: 2.4 nTPM
- endometrium: 1.8 nTPM
- placenta: 0.6 nTPM
Single-cell type
- neutrophil progenitors: 2,301 nCPM
- neutrophils: 609 nCPM
- erythrocytes: 7.4 nCPM
- megakaryocyte-erythroid progenitors: 2.8 nCPM
- hematopoietic stem cells: 2.4 nCPM
- monocytes: 1.5 nCPM
Immune cell
- non-classical monocyte: 1.7 nTPM
- total PBMC: 0.9 nTPM
- neutrophil: 0.4 nTPM
- basophil: 0 nTPM
- classical monocyte: 0 nTPM
- eosinophil: 0 nTPM
Brain region
- thalamus: 1.6 nTPM
- cerebral cortex: 0.6 nTPM
- choroid plexus: 0.5 nTPM
- pons: 0.5 nTPM
- medulla oblongata: 0.4 nTPM
- basal ganglia: 0.3 nTPM
DiseaseUniProt · ClinVar · IEDB · PubMed
Four sources answering four different questions about MMP8.
Disease | ImmuneIEDB
Conditions an epitope on MMP8 was assayed in.
- rheumatoid arthritis B cell
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)
- 1.76
- gnomAD pLI
- 0
- gnomAD missense Z
- -0.61
- DepMap mean gene effect
- -0.08
- 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 lipopolysaccharide
- collagen catabolic process
- endodermal cell differentiation
- extracellular matrix disassembly
- extracellular matrix organization
- positive regulation of microglial cell activation
- positive regulation of neuroinflammatory response
- positive regulation of tumor necrosis factor production
- positive regulation of tumor necrosis factor-mediated signaling pathway
- proteolysis
Molecular functions
- endopeptidase activity
- metalloendopeptidase activity
- peptidase activity
- serine-type endopeptidase activity
- tumor necrosis factor binding
- 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
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads MMP8 as an antibody target. Whether an autoantibody or antibody against MMP8 could matter depends on whether native MMP8 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
MMP8 is annotated as secreted, so native MMP8 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 MMP8 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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