MMP10

Protein identityUniProt · HPA

UniProt accession

P09238

Gene

MMP10

Ensembl

ENSG00000166670

Chromosome

11

Canonical length

476 aa

Protein class

Cancer-related genes, Enzymes, Predicted secreted proteins

Subcellular location

Plasma membrane,Cytosol

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 secreted protease breaks down fibronectin, laminin, elastin, proteoglycan core protein, gelatins, and several types of collagen. The gene is part of a cluster of MMP genes on chromosome 11. [provided by RefSeq, Jan 2016]

Canonical amino-acid sequenceUniProt

476 residues, UniProt reviewed canonical sequence.

>P09238|MMP10
     1  MMHLAFLVLL CLPVCSAYPL SGAAKEEDSN KDLAQQYLEK YYNLEKDVKQ FRRKDSNLIV
    61  KKIQGMQKFL GLEVTGKLDT DTLEVMRKPR CGVPDVGHFS SFPGMPKWRK THLTYRIVNY
   121  TPDLPRDAVD SAIEKALKVW EEVTPLTFSR LYEGEADIMI SFAVKEHGDF YSFDGPGHSL
   181  AHAYPPGPGL YGDIHFDDDE KWTEDASGTN LFLVAAHELG HSLGLFHSAN TEALMYPLYN
   241  SFTELAQFRL SQDDVNGIQS LYGPPPASTE EPLVPTKSVP SGSEMPAKCD PALSFDAIST
   301  LRGEYLFFKD RYFWRRSHWN PEPEFHLISA FWPSLPSYLD AAYEVNSRDT VFIFKGNEFW
   361  AIRGNEVQAG YPRGIHTLGF PPTIRKIDAA VSDKEKKKTY FFAADKYWRF DENSQSMEQG
   421  FPRLIADDFP GVEPKVDAVL QAFGFFYFFS GSSQFEFDPN ARMVTHILKS NSWLHC

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against MMP10 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)

0.29

Highest tissue expression

250 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about MMP10.

Disease | ImmuneIEDB

Conditions an epitope on MMP10 was assayed in.

• type 1 diabetes mellitus T cell

ReferencesPubMed · IEDB

Publications for MMP10 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.

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. IEDB — curated epitope assays from the Immune Epitope Database (Vita et al., Nucleic Acids Research 2019). 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)

1.41

gnomAD pLI

0

gnomAD missense Z

-1.08

DepMap mean gene effect

0.09

DepMap dependency class

none

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

• collagen catabolic process
• extracellular matrix disassembly
• extracellular matrix organization
• proteolysis

Molecular functions

• metalloendopeptidase activity
• serine-type endopeptidase activity
• zinc ion binding

Cellular components

• extracellular matrix
• extracellular region
• extracellular space

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

• Calcium
• Collagen degradation
• Disulfide bond
• Extracellular matrix
• Hydrolase
• Metal-binding
• Metalloprotease
• Protease
• Repeat
• Secreted
• Signal
• Zinc
• Zymogen

InteractionsUniProt · HPA

Protein binding partners of MMP10 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• TIMP1