MMP24
Matrix metalloproteinase-24
Also known as: MMP24_HUMAN, MT5-MMP
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q9Y5R2
- Gene
- MMP24
- Ensembl
- ENSG00000125966
- Chromosome
- 20
- Canonical length
- 645 aa
- Protein class
- Enzymes, Predicted membrane proteins, Predicted secreted proteins
- Subcellular location
- Nucleoli,Plasma membrane
- 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. Unlike most MMPs, which are secreted, this protease is a member of the membrane-type MMP (MT-MMP) subfamily, contains a transmembrane domain and is expressed at the cell surface. Substrates of this protease include the proteins cadherin 2 and matrix metallopeptidase 2 (also known as 72 kDa type IV collagenase). The gene has previously been referred to as MMP25 but has been renamed matrix metallopeptidase 24 (MMP24). [provided by RefSeq, Oct 2019]
Canonical amino-acid sequenceUniProt
645 residues, UniProt reviewed canonical sequence.
>Q9Y5R2|MMP24
1 MPRSRGGRAA PGPPPPPPPP GQAPRWSRWR VPGRLLLLLL PALCCLPGAA RAAAAAAGAG
61 NRAAVAVAVA RADEAEAPFA GQNWLKSYGY LLPYDSRASA LHSAKALQSA VSTMQQFYGI
121 PVTGVLDQTT IEWMKKPRCG VPDHPHLSRR RRNKRYALTG QKWRQKHITY SIHNYTPKVG
181 ELDTRKAIRQ AFDVWQKVTP LTFEEVPYHE IKSDRKEADI MIFFASGFHG DSSPFDGEGG
241 FLAHAYFPGP GIGGDTHFDS DEPWTLGNAN HDGNDLFLVA VHELGHALGL EHSSDPSAIM
301 APFYQYMETH NFKLPQDDLQ GIQKIYGPPA EPLEPTRPLP TLPVRRIHSP SERKHERQPR
361 PPRPPLGDRP STPGTKPNIC DGNFNTVALF RGEMFVFKDR WFWRLRNNRV QEGYPMQIEQ
421 FWKGLPARID AAYERADGRF VFFKGDKYWV FKEVTVEPGY PHSLGELGSC LPREGIDTAL
481 RWEPVGKTYF FKGERYWRYS EERRATDPGY PKPITVWKGI PQAPQGAFIS KEGYYTYFYK
541 GRDYWKFDNQ KLSVEPGYPR NILRDWMGCN QKEVERRKER RLPQDDVDIM VTINDVPGSV
601 NAVAVVIPCI LSLCILVLVY TIFQFKNKTG PQPVTYYKRP VQEWVLocalizationUniProt · AlphaFold · HPA
Whether an antibody against MMP24 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
- Cell surface
- Secreted
- No
- Transmembrane segments
- 1
- Mean surface accessibility (rSASA)
- 0.38
- Highest tissue expression
- 68 nTPM
Expression across tissuesHPA
Tissue
- cerebellum: 68 nTPM
- cerebral cortex: 8.6 nTPM
- kidney: 7.3 nTPM
- basal ganglia: 6 nTPM
- pancreas: 5.5 nTPM
- hypothalamus: 5.3 nTPM
Single-cell type
- enterocytes: 111 nCPM
- suprabasal keratinocytes: 96 nCPM
- brain excitatory neurons: 92 nCPM
- epicardial cells: 86 nCPM
- basal keratinocytes: 80 nCPM
- cholangiocytes: 71 nCPM
Immune cell
- neutrophil: 0.3 nTPM
- basophil: 0.1 nTPM
- gdT-cell: 0.1 nTPM
- MAIT T-cell: 0.1 nTPM
- memory CD8 T-cell: 0.1 nTPM
- naive B-cell: 0.1 nTPM
Brain region
- cerebellum: 89 nTPM
- cerebral cortex: 22 nTPM
- thalamus: 21 nTPM
- amygdala: 18 nTPM
- hippocampal formation: 18 nTPM
- midbrain: 18 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)
- 0.41
- gnomAD pLI
- 0.68
- gnomAD missense Z
- 2.28
- DepMap mean gene effect
- -0.08
- DepMap dependency class
- selective
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 7% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- cell-cell adhesion mediated by cadherin
- cell-cell adhesion via plasma-membrane adhesion molecules
- collagen catabolic process
- detection of temperature stimulus involved in sensory perception of pain
- extracellular matrix organization
- glial cell differentiation
- neuronal stem cell population maintenance
- proteolysis
Molecular functions
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
- Peptidase M10A, matrix metallopeptidase, C-terminal
- Metallopeptidase, catalytic domain superfamily
- Peptidase M10A, catalytic domain
- PGBD-like superfamily
- Hemopexin-like domain superfamily
- Hemopexin
- Matrixin
- Putative peptidoglycan binding domain
- Domain of unknown function (DUF3377)
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of MMP24 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 MMP24 as an antibody target. Whether an autoantibody or antibody against MMP24 could matter depends on whether native MMP24 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
MMP24 is annotated at the cell surface, where native MMP24 is exposed to circulating antibodies and is a prime autoantibody target that could block, deplete, or overstimulate it.
Annotation status
The present source text does not explicitly label MMP24 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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