MMP16
Matrix metalloproteinase-16
Also known as: C8orf57, DKFZp761D112, MMP16_HUMAN, MT3-MMP
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- P51512
- Gene
- MMP16
- Ensembl
- ENSG00000156103
- Chromosome
- 8
- Canonical length
- 607 aa
- Protein class
- Cancer-related genes, Enzymes, Predicted intracellular proteins, Predicted membrane proteins, Predicted secreted proteins
- Subcellular location
- Vesicles,Cytosol
- 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. The encoded protein activates MMP2 by cleavage. This gene was once referred to as MT-MMP2, but was renamed as MT-MMP3 or MMP16. [provided by RefSeq, Oct 2010]
Canonical amino-acid sequenceUniProt
607 residues, UniProt reviewed canonical sequence.
>P51512|MMP16
1 MILLTFSTGR RLDFVHHSGV FFLQTLLWIL CATVCGTEQY FNVEVWLQKY GYLPPTDPRM
61 SVLRSAETMQ SALAAMQQFY GINMTGKVDR NTIDWMKKPR CGVPDQTRGS SKFHIRRKRY
121 ALTGQKWQHK HITYSIKNVT PKVGDPETRK AIRRAFDVWQ NVTPLTFEEV PYSELENGKR
181 DVDITIIFAS GFHGDSSPFD GEGGFLAHAY FPGPGIGGDT HFDSDEPWTL GNPNHDGNDL
241 FLVAVHELGH ALGLEHSNDP TAIMAPFYQY METDNFKLPN DDLQGIQKIY GPPDKIPPPT
301 RPLPTVPPHR SIPPADPRKN DRPKPPRPPT GRPSYPGAKP NICDGNFNTL AILRREMFVF
361 KDQWFWRVRN NRVMDGYPMQ ITYFWRGLPP SIDAVYENSD GNFVFFKGNK YWVFKDTTLQ
421 PGYPHDLITL GSGIPPHGID SAIWWEDVGK TYFFKGDRYW RYSEEMKTMD PGYPKPITVW
481 KGIPESPQGA FVHKENGFTY FYKGKEYWKF NNQILKVEPG YPRSILKDFM GCDGPTDRVK
541 EGHSPPDDVD IVIKLDNTAS TVKAIAIVIP CILALCLLVL VYTVFQFKRK GTPRHILYCK
601 RSMQEWVLocalizationUniProt · AlphaFold · HPA
Whether an antibody against MMP16 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)
- 0.36
- Highest tissue expression
- 5.3 nTPM
Expression across tissuesHPA
Tissue
- cerebral cortex: 5.3 nTPM
- amygdala: 2.7 nTPM
- hypothalamus: 2.5 nTPM
- gallbladder: 2.4 nTPM
- hippocampal formation: 2.4 nTPM
- blood vessel: 2.2 nTPM
Single-cell type
- oligodendrocyte progenitor cells: 2,339 nCPM
- other brain neurons: 381 nCPM
- brain excitatory neurons: 358 nCPM
- oligodendrocytes: 312 nCPM
- brain inhibitory neurons: 265 nCPM
- pancreatic islet cells: 236 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
- cerebral cortex: 20 nTPM
- basal ganglia: 18 nTPM
- hypothalamus: 17 nTPM
- white matter: 15 nTPM
- amygdala: 15 nTPM
- cerebellum: 13 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)
- 0.35
- gnomAD pLI
- 0.92
- gnomAD missense Z
- 3.52
- DepMap mean gene effect
- 0.06
- DepMap dependency class
- none
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 5% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- chondrocyte proliferation
- collagen catabolic process
- craniofacial suture morphogenesis
- embryonic cranial skeleton morphogenesis
- endochondral ossification
- extracellular matrix organization
- protein processing
- proteolysis
- skeletal system development
Molecular functions
- enzyme activator activity
- metalloaminopeptidase activity
- metalloendopeptidase 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
- 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 MMP16 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 MMP16 as an antibody target. Whether an autoantibody or antibody against MMP16 could matter depends on whether native MMP16 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
MMP16 is annotated at the cell surface, where native MMP16 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 MMP16 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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