MMP12
Macrophage metalloelastase
Also known as: HME, MMP12_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- P39900
- Gene
- MMP12
- Ensembl
- ENSG00000262406
- Chromosome
- 11
- Canonical length
- 470 aa
- Protein class
- Cancer-related genes, Enzymes, Predicted secreted proteins
- Secretome location
- Secreted to extracellular matrix
OverviewNCBI Gene
This gene encodes a member of the peptidase M10 family 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. The encoded preproprotein is proteolytically processed to generate the mature protease. This protease degrades soluble and insoluble elastin. This gene may play a role in aneurysm formation and mutations in this gene are associated with lung function and chronic obstructive pulmonary disease (COPD). This gene is part of a cluster of MMP genes on chromosome 11. [provided by RefSeq, Jan 2016]
Canonical amino-acid sequenceUniProt
470 residues, UniProt reviewed canonical sequence.
>P39900|MMP12
1 MKFLLILLLQ ATASGALPLN SSTSLEKNNV LFGERYLEKF YGLEINKLPV TKMKYSGNLM
61 KEKIQEMQHF LGLKVTGQLD TSTLEMMHAP RCGVPDVHHF REMPGGPVWR KHYITYRINN
121 YTPDMNREDV DYAIRKAFQV WSNVTPLKFS KINTGMADIL VVFARGAHGD FHAFDGKGGI
181 LAHAFGPGSG IGGDAHFDED EFWTTHSGGT NLFLTAVHEI GHSLGLGHSS DPKAVMFPTY
241 KYVDINTFRL SADDIRGIQS LYGDPKENQR LPNPDNSEPA LCDPNLSFDA VTTVGNKIFF
301 FKDRFFWLKV SERPKTSVNL ISSLWPTLPS GIEAAYEIEA RNQVFLFKDD KYWLISNLRP
361 EPNYPKSIHS FGFPNFVKKI DAAVFNPRFY RTYFFVDNQY WRYDERRQMM DPGYPKLITK
421 NFQGIGPKID AVFYSKNKYY YFFQGSNQFE YDFLLQRITK TLKSNSWFGCLocalizationUniProt · AlphaFold · HPA
Whether an antibody against MMP12 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
- 38 nTPM
Expression across tissuesHPA
Tissue
- appendix: 38 nTPM
- tonsil: 18 nTPM
- urinary bladder: 15 nTPM
- rectum: 15 nTPM
- colon: 13 nTPM
- small intestine: 7.4 nTPM
Single-cell type
- extravillous trophoblasts: 562 nCPM
- cdc: 31 nCPM
- macrophages: 31 nCPM
- smooth muscle cells: 22 nCPM
- monocytes: 6.7 nCPM
- distal convoluted tubule cells: 3 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
- hypothalamus: 0.6 nTPM
- thalamus: 0.3 nTPM
- basal ganglia: 0.2 nTPM
- medulla oblongata: 0.2 nTPM
- midbrain: 0.2 nTPM
- pons: 0.2 nTPM
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
- bronchiole development
- cellular response to virus
- collagen catabolic process
- elastin catabolic process
- extracellular matrix disassembly
- extracellular matrix organization
- lung alveolus development
- negative regulation of transcription by RNA polymerase II
- negative regulation of type I interferon-mediated signaling pathway
- positive regulation of epithelial cell proliferation involved in wound healing
- positive regulation of interferon-alpha production
- positive regulation of transcription by RNA polymerase II
- positive regulation of type I interferon-mediated signaling pathway
- protein import into nucleus
- proteolysis
- regulation of defense response to virus by host
- response to amyloid-beta
- wound healing, spreading of epidermal cells
- negative regulation of endothelial cell-matrix adhesion via fibronectin
Molecular functions
- calcium ion binding
- collagen binding
- core promoter sequence-specific DNA binding
- endopeptidase activity
- metalloendopeptidase activity
- sequence-specific DNA binding
- 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
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads MMP12 as an antibody target. Whether an autoantibody or antibody against MMP12 could matter depends on whether native MMP12 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
MMP12 is annotated as secreted, so native MMP12 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 MMP12 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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