MMP7

Protein identityUniProt · HPA

UniProt accession

P09237

Gene

MMP7

Ensembl

ENSG00000137673

Chromosome

11

Canonical length

267 aa

Protein class

Cancer-related genes, Enzymes, Plasma proteins, Predicted secreted proteins

Subcellular location

Nucleoplasm,Vesicles,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 proteoglycans, fibronectin, elastin and casein and differs from most MMP family members in that it lacks a conserved C-terminal hemopexin domain. The enzyme is involved in wound healing, and studies in mice suggest that it regulates the activity of defensins in intestinal mucosa. The gene is part of a cluster of MMP genes on chromosome 11. This gene exhibits elevated expression levels in multiple human cancers. [provided by RefSeq, Jan 2016]

Canonical amino-acid sequenceUniProt

267 residues, UniProt reviewed canonical sequence.

>P09237|MMP7
     1  MRLTVLCAVC LLPGSLALPL PQEAGGMSEL QWEQAQDYLK RFYLYDSETK NANSLEAKLK
    61  EMQKFFGLPI TGMLNSRVIE IMQKPRCGVP DVAEYSLFPN SPKWTSKVVT YRIVSYTRDL
   121  PHITVDRLVS KALNMWGKEI PLHFRKVVWG TADIMIGFAR GAHGDSYPFD GPGNTLAHAF
   181  APGTGLGGDA HFDEDERWTD GSSLGINFLY AATHELGHSL GMGHSSDPNA VMYPTYGNGD
   241  PQNFKLSQDD IKGIQKLYGK RSNSRKK

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against MMP7 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)

0.31

Highest tissue expression

479 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about MMP7.

Disease | ImmuneIEDB

Conditions an epitope on MMP7 was assayed in.

• bile duct adenocarcinoma T cell
• intrahepatic cholangiocarcinoma T cell
• melanoma T cell
• renal carcinoma T cell

ReferencesPubMed · IEDB

Publications for MMP7 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)

1.52

gnomAD pLI

0

gnomAD missense Z

-0.43

DepMap mean gene effect

-0.02

DepMap dependency class

none

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 4% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• antibacterial peptide biosynthetic process
• collagen catabolic process
• defense response to Gram-negative bacterium
• defense response to Gram-positive bacterium
• extracellular matrix disassembly
• extracellular matrix organization
• membrane protein ectodomain proteolysis
• membrane protein intracellular domain proteolysis
• positive regulation of cell migration
• proteolysis
• regulation of cell population proliferation
• response to xenobiotic stimulus
• antibacterial peptide secretion

Molecular functions

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

Cellular components

• extracellular exosome
• extracellular matrix
• extracellular region
• extracellular space

Protein domainsUniProt · Pfam · InterPro

• Peptidase M10, metallopeptidase
• Peptidoglycan binding-like
• Peptidase, metallopeptidase
• Peptidase M10A, cysteine switch, zinc binding site
• Peptidase M10A
• Metallopeptidase, catalytic domain superfamily
• Peptidase M10A, catalytic domain
• PGBD-like superfamily
• Matrixin
• Putative peptidoglycan binding domain

KeywordsUniProt

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