Mmp28 matrix metallopeptidase 28 (epilysin) [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Mmp28provided by MGI
Official Full Name: matrix metallopeptidase 28 (epilysin)provided by MGI
Primary source: MGI:MGI:2153062
See related: Ensembl:ENSMUSG00000020682 AllianceGenome:MGI:2153062
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: D130023P12
Summary: Predicted to enable metalloendopeptidase activity. Acts upstream of or within negative regulation of macrophage chemotaxis. Located in cytoplasm. Is expressed in several structures, including heart; hindlimb; lung; nervous system; and skin. Orthologous to human MMP28 (matrix metallopeptidase 28). [provided by Alliance of Genome Resources, Dec 2024]
Expression: Broad expression in testis adult (RPKM 14.0), subcutaneous fat pad adult (RPKM 11.4) and 24 other tissues See more
Orthologs: human all
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Genomic context

Location:: 11 C; 11 50.39 cM

Exon count:: 9

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	11	NC_000077.7 (83331594..83353890, complement)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	11	NC_000077.6 (83440768..83463040, complement)

Chromosome 11 - NC_000077.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: Mouse ENCODE transcriptome data
Description: RNA profiling data sets generated by the Mouse ENCODE project.
BioProject: PRJNA66167
Publication: PMID 25409824
Analysis date: n/a

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

this study shows that Mmp28 is regulated by TRIF- and type I IFN-dependent signaling in macrophages
Title: Matrix metalloproteinase 28 is regulated by TRIF- and type I IFN-dependent signaling in macrophages.
MMP28 is upregulated in epithelial cells from Idiopathic pulmonary fibrosis lungs.
Title: Upregulation and Nuclear Location of MMP28 in Alveolar Epithelium of Idiopathic Pulmonary Fibrosis.
results demonstrate that Ranbp2 controls nucleocytoplasmic, chemokine and metalloproteinase 28 signaling, and proteostasis of substrates that are crucial to motoneuronal homeostasis and whose impairments by loss of Ranbp2 drive ALS-like syndromes
Title: Loss of Ranbp2 in motoneurons causes disruption of nucleocytoplasmic and chemokine signaling, proteostasis of hnRNPH3 and Mmp28, and development of amyotrophic lateral sclerosis-like syndromes.
MMP28 promotes macrophage polarization toward M2 cells and augments pulmonary fibrosis.
Title: MMP28 promotes macrophage polarization toward M2 cells and augments pulmonary fibrosis.
MMP-28 deletion aggravated MI-induced LV dysfunction and rupture as a result of defective inflammatory response and scar formation by suppressing M2 macrophage activation.
Title: Matrix metalloproteinase-28 deletion exacerbates cardiac dysfunction and rupture after myocardial infarction in mice by inhibiting M2 macrophage activation.
Epilysin serves as a negative regulator of early macrophage recruitment, a novel function that may have evolved as a mechanism to restrain unnecessary and untimely inflammation.
Title: Epilysin (MMP-28) restrains early macrophage recruitment in Pseudomonas aeruginosa pneumonia.
These results suggest that MMP-28 plays an evolutionarily conserved role in neural development and is likely to modulate the axonal-glial extracellular microenvironment.
Title: Neural MMP-28 expression precedes myelination during development and peripheral nerve repair.
Epilysin is alternatively spliced and processed by a furin-like proprotein convertase.
Title: The mouse matrix metalloproteinase, epilysin (MMP-28), is alternatively spliced and processed by a furin-like proprotein convertase.

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Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Endonuclease-mediated (2)
Gene trapped (1)
Targeted (1) 1 citation

General gene information

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Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables metalloendopeptidase activity	IBA Inferred from Biological aspect of Ancestor more info
enables metalloendopeptidase activity	ISO Inferred from Sequence Orthology more info	PubMed

Process	Evidence Code	Pubs
involved_in collagen catabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in extracellular matrix organization	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within negative regulation of macrophage chemotaxis	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
is_active_in extracellular space	IBA Inferred from Biological aspect of Ancestor more info

General protein information

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Preferred Names: matrix metalloproteinase-28

Names: matrix metalloproteinase 28 (epilysin)

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_001320300.1 → NP_001307229.1 matrix metalloproteinase-28 isoform 3 precursor

Status: VALIDATED

Description

Transcript Variant: This variant (3) uses an alternate, in-frame splice site in the 3' coding region, compared to variant 1. It encodes isoform 3, which is longer than isoform 1.

Source sequence(s)

AK051258, AL663096, BC145048, BY308224

Consensus CDS

CCDS83860.1

UniProtKB/TrEMBL

Q8CGV8

Related

ENSMUSP00000103772.3, ENSMUST00000108137.9

Conserved Domains (4) summary

cd00094
Location:321 → 510

HX; Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of ...

cd04278
Location:129 → 284

ZnMc_MMP; Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate ...

pfam00413
Location:129 → 284

Peptidase_M10; Matrixin

pfam01471
Location:31 → 86

PG_binding_1; Putative peptidoglycan binding domain
NM_080453.3 → NP_536701.1 matrix metalloproteinase-28 isoform 1 precursor

See identical proteins and their annotated locations for NP_536701.1

Status: VALIDATED

Description

Transcript Variant: This variant (1) encodes the isoform 1.

Source sequence(s)

AK051258, AL663096, BC145049, BY308224

Consensus CDS

CCDS25166.1

UniProtKB/TrEMBL

Q8CGV5

Related

ENSMUSP00000021020.7, ENSMUST00000021020.13

Conserved Domains (4) summary

cd04278
Location:129 → 284

ZnMc_MMP; Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate ...

pfam00413
Location:129 → 284

Peptidase_M10; Matrixin

pfam01471
Location:31 → 86

PG_binding_1; Putative peptidoglycan binding domain

cl02471
Location:321 → 500

HX; Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of ...
NM_172797.3 → NP_766385.1 matrix metalloproteinase-28 isoform 2 precursor

See identical proteins and their annotated locations for NP_766385.1

Status: VALIDATED

Description

Transcript Variant: This variant (2) uses an alternate in-frame splice site in the 3' coding region, compared to variant 1. It encodes isoform 2, which is shorter than isoform 1.

Source sequence(s)

AK051258, AL663096

Consensus CDS

CCDS25167.1

UniProtKB/TrEMBL

Q8BG29

Related

ENSMUSP00000099498.4, ENSMUST00000103209.10

Conserved Domains (4) summary

cd04278
Location:129 → 284

ZnMc_MMP; Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate ...

pfam00413
Location:129 → 284

Peptidase_M10; Matrixin

pfam01471
Location:31 → 86

PG_binding_1; Putative peptidoglycan binding domain

cl02471
Location:321 → 486

HX; Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of ...

RefSeqs of Annotated Genomes: GCF_000001635.27-RS_2024_02

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCm39 C57BL/6J

Genomic

NC_000077.7 Reference GRCm39 C57BL/6J

Range

83331594..83353890 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_036156248.1 → XP_036012141.1 matrix metalloproteinase-28 isoform X1

UniProtKB/TrEMBL

Q5SSG2

Related

ENSMUSP00000112566.2, ENSMUST00000119346.2

Conserved Domains (3) summary

cd04278
Location:129 → 284

ZnMc_MMP; Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate ...

pfam01471
Location:31 → 86

PG_binding_1; Putative peptidoglycan binding domain

cl02471
Location:321 → 390

HX; Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of ...