MEP1A

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
Gene location (Human)
Chr.	Chromosome 6 (human)
End	46,839,778 bp
Gene location (Mouse)
Chr.	Chromosome 17 (mouse)
End	43,813,703 bp
RNA expression pattern
	Top expressed in
	jejunal mucosa; ; rectum; ; duodenum; ; appendix; ; amniotic fluid; ; pancreatic ductal cell; ; smooth muscle tissue; ; body of pancreas; ; lymph node; ; right uterine tube;
	Top expressed in
	ileum; ; proximal tubule; ; kidney; ; intestinal villus; ; left colon; ; jejunum; ; renal pelvis; ; duodenum; ; renal calyx; ; crypt of lieberkuhn of small intestine;
	More reference expression data
	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
	4224
	17287
	ENSG00000112818
	ENSMUSG00000023914
	Q16819
	P28825
	NM_005588
	NM_008585
	NP_005579
	NP_032611
	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.

Dumermuth E, Sterchi EE, Jiang WP, et al. (1991). "The astacin family of metalloendopeptidases". J. Biol. Chem. 266 (32): 21381–5. doi:10.1016/S0021-9258(18)54648-2. PMID 1939172.
Kärgel HJ, Dettmer R, Etzold G, et al. (1982). "Action of rat liver cathepsin L on glucagon". Acta Biol. Med. Ger. 40 (9): 1139–43. PMID 7340337.
Kaushal GP, Walker PD, Shah SV (1994). "An old enzyme with a new function: purification and characterization of a distinct matrix-degrading metalloproteinase in rat kidney cortex and its identification as meprin". J. Cell Biol. 126 (5): 1319–27. doi:10.1083/jcb.126.5.1319. PMC 2120165. PMID 8063866.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Dumermuth E, Eldering JA, Grünberg J, et al. (1994). "Cloning of the PABA peptide hydrolase alpha subunit (PPH alpha) from human small intestine and its expression in COS-1 cells". FEBS Lett. 335 (3): 367–75. doi:10.1016/0014-5793(93)80421-P. PMID 8262185. S2CID 32599035.
Bankus JM, Bond JS (1996). "Expression and distribution of meprin protease subunits in mouse intestine". Arch. Biochem. Biophys. 331 (1): 87–94. doi:10.1006/abbi.1996.0286. PMID 8660687.
Chevallier S, Ahn J, Boileau G, Crine P (1996). "Identification of the cysteine residues implicated in the formation of alpha 2 and alpha/beta dimers of rat meprin". Biochem. J. 317 (Pt 3): 731–8. doi:10.1042/bj3170731. PMC 1217546. PMID 8760356.
Eldering JA, Grünberg J, Hahn D, et al. (1997). "Polarised expression of human intestinal N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase (human meprin) alpha and beta subunits in Madin-Darby canine kidney cells". Eur. J. Biochem. 247 (3): 920–32. doi:10.1111/j.1432-1033.1997.00920.x. PMID 9288916.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Lottaz D, Hahn D, Müller S, et al. (1999). "Secretion of human meprin from intestinal epithelial cells depends on differential expression of the alpha and beta subunits". Eur. J. Biochem. 259 (1–2): 496–504. doi:10.1046/j.1432-1327.1999.00071.x. PMID 9914532.
Richter R, Schulz-Knappe P, Schrader M, et al. (1999). "Composition of the peptide fraction in human blood plasma: database of circulating human peptides". J. Chromatogr. B. 726 (1–2): 25–35. doi:10.1016/S0378-4347(99)00012-2. PMID 10348167.
Köhler D, Kruse M, Stöcker W, Sterchi EE (2000). "Heterologously overexpressed, affinity-purified human meprin alpha is functionally active and cleaves components of the basement membrane in vitro". FEBS Lett. 465 (1): 2–7. doi:10.1016/S0014-5793(99)01712-3. PMID 10620696. S2CID 22895580.
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.
Rösmann S, Hahn D, Lottaz D, et al. (2002). "Activation of human meprin-alpha in a cell culture model of colorectal cancer is triggered by the plasminogen-activating system". J. Biol. Chem. 277 (43): 40650–8. doi:10.1074/jbc.M206203200. PMID 12189145.
Norman LP, Jiang W, Han X, et al. (2003). "Targeted Disruption of the Meprin β Gene in Mice Leads to Underrepresentation of Knockout Mice and Changes in Renal Gene Expression Profiles". Mol. Cell. Biol. 23 (4): 1221–30. doi:10.1128/MCB.23.4.1221-1230.2003. PMC 141138. PMID 12556482.
Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: Large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.

This article on a gene on human chromosome 6 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000112818 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000023914 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid7774936-5] 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-6] "Entrez Gene: MEP1A meprin A, alpha (PABA peptide hydrolase)".

[pmid19262505-7] 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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MEP1A

Function

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MEP1A

Function

References

Further reading

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