MEP1A

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]

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] 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] 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
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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.