MEP1A

Protein-coding gene in the species Homo sapiens

MEP1A

Available structures

PDB

Ortholog search: PDBe RCSB

List of PDB id codes
1IAF

Identifiers

Aliases

MEP1A, PPHA, meprin A subunit alpha

External IDs

OMIM: 600388; MGI: 96963; HomoloGene: 31323; GeneCards: MEP1A; OMA:MEP1A - orthologs

Gene location (Human)

Chr.	Chromosome 6 (human)^[1]

Band	6p12.3	Start	46,793,389 bp^[1]
Band	6p12.3	End	46,839,778 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 17 (mouse)^[2]

Band	17 B3\|17 19.73 cM	Start	43,785,215 bp^[2]
Band	17 B3\|17 19.73 cM	End	43,813,703 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

mucosa of ileum

jejunal mucosa

mucosa of colon

mucosa of sigmoid colon

rectum

mucosa of transverse colon

duodenum

testicle

appendix

amniotic fluid

Top expressed in

right kidney

ileum

proximal tubule

human kidney

intestinal villus

epithelium of small intestine

left colon

jejunum

renal pelvis

migratory enteric neural crest cell

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	zinc ion binding peptidase activity metalloendopeptidase activity protein binding hydrolase activity metallopeptidase activity metal ion binding
Cellular component	integral component of membrane meprin A complex integral component of plasma membrane extracellular exosome membrane extracellular space
Biological process	digestion proteolysis
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


4224


17287

Ensembl


ENSG00000112818


ENSMUSG00000023914

UniProt


Q16819


P28825

RefSeq (mRNA)


NM_005588


NM_008585

RefSeq (protein)


NP_005579


NP_032611

Location (UCSC)

Chr 6: 46.79 – 46.84 Mb

Chr 17: 43.79 – 43.81 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Meprin A subunit alpha also known as endopeptidase-2 or PABA peptide hydrolase is the alpha subunit of the meprin A enzyme that in humans is encoded by the MEP1A gene.^[5]^[6] The MEP1A locus is on chromosome 6p in humans and on chromosome 17 in mice.^[7]

Function

The meprin alpha subunit product of the MEP1A gene is processed in the endoplasmic reticulum during intracellular transport, and is secreted as homomeric meprin A. Meprin alpha subunits may self-associate, and once secreted, form very large multimers, with a molecular mass of over 1 million daltons. In cells concurrently expressing MEP1B, the meprin alpha and meprin beta subunits form disulfide dimers that interact to form membrane bound heterotetrameric meprin A.

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000112818 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000023914 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Bond JS, Rojas K, Overhauser J, Zoghbi HY, Jiang W (Jul 1995). "The structural genes, MEP1A and MEP1B, for the alpha and beta subunits of the metalloendopeptidase meprin map to human chromosomes 6p and 18q, respectively". Genomics. 25 (1): 300–3. doi:10.1016/0888-7543(95)80142-9. PMID 7774936.
^ "Entrez Gene: MEP1A meprin A, alpha (PABA peptide hydrolase)".
^ Banerjee S, Oneda B, Yap LM, Jewell DP, Matters GL, Fitzpatrick LR, Seibold F, Sterchi EE, Ahmad T, Lottaz D, Bond JS (May 2009). "MEP1A allele for meprin A metalloprotease is a susceptibility gene for inflammatory bowel disease". Mucosal Immunol. 2 (3): 220–31. doi:10.1038/mi.2009.3. PMC 2670347. PMID 19262505.

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Jiang W, Le B (2000). "Structure and expression of the human MEP1A gene encoding the alpha subunit of metalloendopeptidase meprin A". Arch. Biochem. Biophys. 379 (2): 183–7. doi:10.1006/abbi.2000.1873. PMID 10898933.
Kumar JM, Bond JS (2001). "Developmental expression of meprin metalloprotease subunits in ICR and C3H/He mouse kidney and intestine in the embryo, postnatally and after weaning". Biochim. Biophys. Acta. 1518 (1–2): 106–14. doi:10.1016/S0167-4781(01)00188-9. PMID 11267665.
Bertenshaw GP, Turk BE, Hubbard SJ, et al. (2001). "Marked differences between metalloproteases meprin A and B in substrate and peptide bond specificity". J. Biol. Chem. 276 (16): 13248–55. doi:10.1074/jbc.M011414200. PMID 11278902.
Ishmael FT, Norcum MT, Benkovic SJ, Bond JS (2001). "Multimeric structure of the secreted meprin A metalloproteinase and characterization of the functional protomer". J. Biol. Chem. 276 (25): 23207–11. doi:10.1074/jbc.M102654200. PMID 11301339.
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