Mep1b meprin 1 beta [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Mep1bprovided by MGI
Official Full Name: meprin 1 betaprovided by MGI
Primary source: MGI:MGI:96964
See related: Ensembl:ENSMUSG00000024313 AllianceGenome:MGI:96964
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: Mep-1b
Summary: Predicted to enable identical protein binding activity and metalloendopeptidase activity. Predicted to be involved in inflammatory response and proteolysis. Located in membrane. Is expressed in cortical early distal tubule; cortical early proximal tubule; intestine; intestine epithelium; and metanephros. Orthologous to human MEP1B (meprin A subunit beta). [provided by Alliance of Genome Resources, Nov 2024]
Expression: Biased expression in large intestine adult (RPKM 195.8), small intestine adult (RPKM 74.1) and 2 other tissues See more
Orthologs: human all
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Genomic context

Location:: 18 A2; 18 11.81 cM

Exon count:: 15

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	18	NC_000084.7 (21205401..21233256)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	18	NC_000084.6 (21072344..21100199)

Chromosome 18 - NC_000084.7 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?

Meprin beta knockout reduces brain Abeta levels and rescues learning and memory impairments in the APP/lon mouse model for Alzheimer's disease.
Title: Meprin β knockout reduces brain Aβ levels and rescues learning and memory impairments in the APP/lon mouse model for Alzheimer's disease.
Meprin-beta enhances ischemia reperfusion-induced kidney injury in part by modulating mediators of the PKA-Cbeta signaling pathway.
Title: Meprin-β activity modulates the β-catalytic subunit of protein kinase A in ischemia-reperfusion-induced acute kidney injury.
meprin-beta activity enhances diabetic kidney injury in part by altering the metabolite balance in kidneys, favoring high levels of uremic toxins such as indoxyl sulfate and N-methyl-pyridone-carboxamide
Title: LC-MS-based metabolomics analysis to identify meprin-β-associated changes in kidney tissue from mice with STZ-induced type 1 diabetes and diabetic kidney injury.
Results provide evidence that meprin beta is involved in collagen deposition in vivo in the lung of bleomycin treated mice and it localized in region with immature collagen. This suggests that meprin beta can favor the progression of the fibrotic process enhancing collagen processing and deposition.
Title: Meprin β contributes to collagen deposition in lung fibrosis.
This secreted cysteine protease potently converts membrane-bound meprin beta into its active form, impairing meprin beta shedding and its function as a mucus-detaching protease
Title: Mucus Detachment by Host Metalloprotease Meprin β Requires Shedding of Its Inactive Pro-form, which Is Abrogated by the Pathogenic Protease RgpB.
Meprin alphabeta knockout (alphabetaKO) mice and their wild-type (WT) counterparts to streptozotocin-induced type 1 diabetes. The 18-week survival rates were significantly lower for diabetic meprin alphabetaKO mice when compared to those for their wild type counterparts.
Title: Meprin Metalloprotease Deficiency Associated with Higher Mortality Rates and More Severe Diabetic Kidney Injury in Mice with STZ-Induced Type 1 Diabetes.
no significant dentin malformation was observed in Mep1b (-/-) or Mep1a (-/-) deficient mice.
Title: Deficiency of the DSPP-cleaving enzymes meprin α and meprin β does not result in dentin malformation in mice.
meprin alpha and meprin beta join the modulators of Reelin signalling as they cleave Reelin at a specific site and are upregulated under specific pathological conditions.
Title: Determination of cleavage site of Reelin between its sixth and seventh repeat and contribution of meprin metalloproteases to the cleavage.
These studies provide strong evidence for a pathophysiological link between meprin beta and urinary excretion of cleaved nidogen-1 during cisplatin-induced acute kidney injury.
Title: Basement membrane protein nidogen-1 is a target of meprin β in cisplatin nephrotoxicity.
While meprin A only cleaved protein kinase A (PKA) catalytic subunit beta1, meprin B cleaved all three PKA catalytic isoforms.
Title: Isoform-specific interactions between meprin metalloproteases and the catalytic subunit of protein kinase A: significance in acute and chronic kidney injury.

Submit: New GeneRIF Correction See all GeneRIFs (24)

Variation

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Alleles

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

Endonuclease-mediated (4)
Targeted (1) 1 citation

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

D18Mit173 (e-PCR), detects polymorphism
- UniSTS:128194

L15193 (e-PCR)
- UniSTS:160726

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables identical protein binding	IEA Inferred from Electronic Annotation more info
enables identical protein binding	ISO Inferred from Sequence Orthology more info
enables metalloendopeptidase activity	IBA Inferred from Biological aspect of Ancestor more info
enables metalloendopeptidase activity	IEA Inferred from Electronic Annotation more info
enables metalloendopeptidase activity	ISO Inferred from Sequence Orthology more info
enables zinc ion binding	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in inflammatory response	IEA Inferred from Electronic Annotation more info
involved_in proteolysis	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
located_in extracellular region	IEA Inferred from Electronic Annotation more info
located_in membrane	IDA Inferred from Direct Assay more info	PubMed
part_of meprin A complex	IEA Inferred from Electronic Annotation more info
located_in plasma membrane	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: meprin A subunit beta

Names: endopeptidase-2; meprin B; meprin beta

NP_032612.2

EC 3.4.24.63

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_008586.2 → NP_032612.2 meprin A subunit beta precursor

Status: VALIDATED

Source sequence(s)

AK098127

Consensus CDS

CCDS37747.1

UniProtKB/Swiss-Prot

Q059K0, Q61847

Related

ENSMUSP00000080866.5, ENSMUST00000082235.5

Conserved Domains (6) summary

cd06263
Location:266 → 428

MAM; Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members ...

cd00054
Location:609 → 647

EGF_CA; Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the ...

pfam00629
Location:266 → 430

MAM; MAM domain, meprin/A5/mu

pfam01400
Location:70 → 258

Astacin; Astacin (Peptidase family M12A)

cl00064
Location:30 → 256

ZnMc; Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major branches, the astacin-like proteases and the adamalysin/reprolysin-like proteases. Both branches have wide phylogenetic distribution, and contain sub-families, which ...

cl02446
Location:428 → 587

MATH; MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded beta-sandwich structure found in meprins, TRAFs and other proteins. Meprins comprise a class of extracellular metalloproteases which are anchored to the membrane ...