MEP1B meprin A subunit beta [Homo sapiens (human)] - Gene

Summary

Official Symbol: MEP1Bprovided by HGNC
Official Full Name: meprin A subunit betaprovided by HGNC
Primary source: HGNC:HGNC:7020
See related: Ensembl:ENSG00000141434 MIM:600389; AllianceGenome:HGNC:7020
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Summary: Meprins are multidomain zinc metalloproteases that are highly expressed in mammalian kidney and intestinal brush border membranes, and in leukocytes and certain cancer cells. They are involved in the hydrolysis of a variety of peptide and protein substrates, and have been implicated in cancer and intestinal inflammation. Mature meprins are oligomers of evolutionarily related, but separately encoded alpha and/or beta subunits. Homooligomers of alpha subunit are secreted, whereas, oligomers containing the beta subunit are plasma membrane-bound. This gene encodes the beta subunit. Targeted disruption of this gene in mice affects embryonic viability, renal gene expression profiles, and distribution of the membrane-associated alpha subunit in kidney and intestine. [provided by RefSeq, Oct 2011]
Expression: Biased expression in small intestine (RPKM 150.9) and duodenum (RPKM 98.0) See more
Orthologs: mouse all
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Genomic context

Location:: 18q12.1

Exon count:: 15

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	18	NC_000018.10 (32190039..32220404)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	18	NC_060942.1 (32380357..32410718)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	18	NC_000018.9 (29770002..29800367)

Chromosome 18 - NC_000018.10 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: HPA RNA-seq normal tissues HPA RNA-seq normal tissues
Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
BioProject: PRJEB4337
Publication: PMID 24309898
Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

The putative pleiotropic functions of meprin beta in gastric cancer.
Title: The putative pleiotropic functions of meprin β in gastric cancer.
Structure and Dynamics of Meprin beta in Complex with a Hydroxamate-Based Inhibitor.
Title: Structure and Dynamics of Meprin β in Complex with a Hydroxamate-Based Inhibitor.
The authors found that increased meprin beta G32R activity at the cell surface reduces cell proliferation, but increases cell invasion.
Title: The cancer-associated meprin β variant G32R provides an additional activation site and promotes cancer cell invasion.
As meprin beta cleavage of APP has been shown to result in formation of highly aggregation-prone, truncated Abeta2-40/42 peptides, enhanced APP processing by this enzyme could contribute to Alzheimer's disease pathology.
Title: Phosphorylation of the amyloid precursor protein (APP) at Ser-675 promotes APP processing involving meprin β.
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.
For meprin beta a reduction and for BMP-1 an increase in activity was reported under increasing calcium concentrations.
Title: Meprin β and BMP-1 are differentially regulated by CaCl(2).
In this review we report on recent findings that summarize the complex molecular regulation of meprins, particular folding, activation and shedding. Dysregulation of meprin alpha and meprin beta is often associated with pathological conditions such as neurodegeneration, inflammatory bowel disease and fibrosis
Title: Meprin metalloproteases: Molecular regulation and function in inflammation and fibrosis.
TSPAN8 might be important for the orchestration of meprin beta at the cell surface with impact on certain proteolytic processes
Title: Tetraspanin 8 is an interactor of the metalloprotease meprin β within tetraspanin-enriched microdomains.
n conclusion, we show that the concept of cleavable linkers specific for meprin beta is feasible, as the peptides are rapidly cleaved by the enzyme while retaining their biological properties
Title: Evaluation of ¹¹¹in-labelled exendin-4 derivatives containing different meprin β-specific cleavable linkers.

Submit: New GeneRIF Correction See all GeneRIFs (26)

Phenotypes

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Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

Variation

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See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

D18S1025 (e-PCR)
- UniSTS:12578

SHGC-78721 (e-PCR)
- UniSTS:95592

MARC_7239-7240:996687677:1 (e-PCR)
- UniSTS:269745

D18S47 (e-PCR)
- UniSTS:147186

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables identical protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables metalloendopeptidase activity	IBA Inferred from Biological aspect of Ancestor more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
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
part_of meprin A complex	IDA Inferred from Direct Assay more info	PubMed
located_in plasma membrane	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: meprin A subunit beta

Names: N-benzoyl-L-tyrosyl-P-amino-benzoic acid hydrolase subunit beta; N-benzoyl-L-tyrosyl-p-amino-benzoic acid hydrolase beta subunit; PABA peptide hydrolase; PPH beta; endopeptidase-2; meprin A, beta; meprin B

NP_001295100.1

EC 3.4.24.63

NP_005916.2

EC 3.4.24.63

XP_011524315.1

EC 3.4.24.63

XP_011524316.1

EC 3.4.24.63

XP_054174633.1

EC 3.4.24.63

XP_054174634.1

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_001308171.2 → NP_001295100.1 meprin A subunit beta isoform 2 precursor

See identical proteins and their annotated locations for NP_001295100.1

Status: VALIDATED

Description

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

Source sequence(s)

AC011825, AC015563, X81333

Consensus CDS

CCDS77173.1

UniProtKB/TrEMBL

J3QKX5

Related

ENSP00000463280.1, ENST00000581447.1

Conserved Domains (5) summary

cd06263
Location:265 → 427

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 ...

smart00137
Location:260 → 427

MAM; Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others)

cd04282
Location:26 → 255

ZnMc_meprin; Zinc-dependent metalloprotease, meprin_like subfamily. Meprins are membrane-bound or secreted extracellular proteases, which cleave a variety of targets, including peptides such as parathyroid hormone, gastrin, and cholecystokinin, cytokines such as ...

pfam01400
Location:69 → 257

Astacin; Astacin (Peptidase family M12A)

cl02446
Location:427 → 586

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 ...
NM_005925.3 → NP_005916.2 meprin A subunit beta isoform 1 precursor

See identical proteins and their annotated locations for NP_005916.2

Status: VALIDATED

Description

Transcript Variant: This variant (1) represents the longer transcript and encodes the longer isoform (1).

Source sequence(s)

AY695931, X81333

Consensus CDS

CCDS45846.1

UniProtKB/Swiss-Prot

B7ZM35, B9EGL6, Q16820, Q670J1

Related

ENSP00000269202.6, ENST00000269202.11

Conserved Domains (5) summary

cd06263
Location:265 → 427

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 ...

smart00137
Location:260 → 427

MAM; Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others)

cd04282
Location:26 → 255

ZnMc_meprin; Zinc-dependent metalloprotease, meprin_like subfamily. Meprins are membrane-bound or secreted extracellular proteases, which cleave a variety of targets, including peptides such as parathyroid hormone, gastrin, and cholecystokinin, cytokines such as ...

pfam01400
Location:69 → 257

Astacin; Astacin (Peptidase family M12A)

cl02446
Location:427 → 586

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 ...

RefSeqs of Annotated Genomes: GCF_000001405.40-RS_2024_08

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

Reference GRCh38.p14 Primary Assembly

Genomic

NC_000018.10 Reference GRCh38.p14 Primary Assembly

Range

32190039..32220404

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_011526013.3 → XP_011524315.1 meprin A subunit beta isoform X1

Conserved Domains (4) summary

cd06263
Location:192 → 354

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 ...

smart00137
Location:187 → 354

MAM; Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others)

cd03782
Location:354 → 513

MATH_Meprin_Beta; Meprin family, Beta subunit, MATH domain; Meprins are multidomain extracellular metalloproteases capable of cleaving growth factors, cytokines, extracellular matrix proteins, and biologically active peptides. They are composed of two related subunits, ...

cl00064
Location:26 → 188

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 ...
XM_011526014.3 → XP_011524316.1 meprin A subunit beta isoform X2

Conserved Domains (5) summary

cd06263
Location:182 → 303

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 ...

smart00235
Location:70 → 197

ZnMc; Zinc-dependent metalloprotease

cd00054
Location:482 → 520

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 ...

cd03782
Location:303 → 462

MATH_Meprin_Beta; Meprin family, Beta subunit, MATH domain; Meprins are multidomain extracellular metalloproteases capable of cleaving growth factors, cytokines, extracellular matrix proteins, and biologically active peptides. They are composed of two related subunits, ...

cl00064
Location:26 → 215

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 ...