MEP1A: Difference between revisions

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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''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]].<ref name="pmid7774936">{{cite journal |vauthors=Bond JS, Rojas K, Overhauser J, Zoghbi HY, Jiang W | title = The structural genes, MEP1A and MEP1B, for the alpha and beta subunits of the metalloendopeptidase meprin map to human chromosomes 6p and 18q, respectively | journal = Genomics | volume = 25 | issue = 1 | pages = 300–3 |date=Jul 1995 | pmid = 7774936 | pmc = | doi =10.1016/0888-7543(95)80142-9 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: MEP1A meprin A, alpha (PABA peptide hydrolase)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4224| accessdate = }}</ref> The MEP1A locus is on chromosome 6p in humans and on chromosome 17 in mice.<ref name="pmid19262505">{{cite journal |vauthors=Banerjee S, Oneda B, Yap LM, Jewell DP, Matters GL, Fitzpatrick LR, Seibold F, Sterchi EE, Ahmad T, Lottaz D, Bond JS | title = MEP1A allele for meprin A metalloprotease is a susceptibility gene for inflammatory bowel disease | journal = Mucosal Immunol | volume = 2 | issue = 3 | pages = 220–31 |date=May 2009 | pmid = 19262505 | pmc = 2670347 | doi = 10.1038/mi.2009.3 | url = }}</ref>
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| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Meprin A, alpha (PABA peptide hydrolase)
| HGNCid = 7015
| Symbol = MEP1A
| AltSymbols =; PPHA
| OMIM = 600388
| ECnumber = 
| Homologene = 31323
| MGIid = 96963
| GeneAtlas_image1 = PBB_GE_MEP1A_206000_at_tn.png
| Function = {{GNF_GO|id=GO:0004238 |text = meprin A activity}} {{GNF_GO|id=GO:0008237 |text = metallopeptidase activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0008533 |text = astacin activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0005625 |text = soluble fraction}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0005902 |text = microvillus}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0007586 |text = digestion}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 4224
    | Hs_Ensembl = ENSG00000112818
    | Hs_RefseqProtein = NP_005579
    | Hs_RefseqmRNA = NM_005588
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 6
    | Hs_GenLoc_start = 46869085
    | Hs_GenLoc_end = 46915478
    | Hs_Uniprot = Q16819
    | Mm_EntrezGene = 17287
    | Mm_Ensembl = ENSMUSG00000023914
    | Mm_RefseqmRNA = NM_008585
    | Mm_RefseqProtein = NP_032611
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 17
    | Mm_GenLoc_start = 42938373
    | Mm_GenLoc_end = 42967156
    | Mm_Uniprot = Q3TP44
  }}
}}
'''Meprin A, alpha (PABA peptide hydrolase)''', also known as '''MEP1A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MEP1A meprin A, alpha (PABA peptide hydrolase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4224| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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]].
{{PBB_Summary
| section_title =
| summary_text =
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
*{{cite journal   |vauthors=Dumermuth E, Sterchi EE, Jiang WP, etal |title=The astacin family of metalloendopeptidases |journal=J. Biol. Chem. |volume=266 |issue= 32 |pages= 21381–5 |year= 1991 |pmid= 1939172 |doi=  }}
| citations =
*{{cite journal   |vauthors=Kärgel HJ, Dettmer R, Etzold G, etal |title=Action of rat liver cathepsin L on glucagon |journal=Acta Biol. Med. Ger. |volume=40 |issue= 9 |pages= 1139–43 |year= 1982 |pmid= 7340337 |doi=  }}
*{{cite journal | author=Dumermuth E, Sterchi EE, Jiang WP, ''et al.'' |title=The astacin family of metalloendopeptidases. |journal=J. Biol. Chem. |volume=266 |issue= 32 |pages= 21381-5 |year= 1991 |pmid= 1939172 |doi=  }}
*{{cite journal  |vauthors=Kaushal GP, Walker PD, Shah SV |title=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 |journal=J. Cell Biol. |volume=126 |issue= 5 |pages= 1319–27 |year= 1994 |pmid= 8063866 |doi=10.1083/jcb.126.5.1319  | pmc=2120165 }}
*{{cite journal | author=Kärgel HJ, Dettmer R, Etzold G, ''et al.'' |title=Action of rat liver cathepsin L on glucagon. |journal=Acta Biol. Med. Ger. |volume=40 |issue= 9 |pages= 1139-43 |year= 1982 |pmid= 7340337 |doi=  }}
*{{cite journal  |vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8 }}
*{{cite journal  | author=Bond JS, Rojas K, Overhauser J, ''et al.'' |title=The structural genes, MEP1A and MEP1B, for the alpha and beta subunits of the metalloendopeptidase meprin map to human chromosomes 6p and 18q, respectively. |journal=Genomics |volume=25 |issue= 1 |pages= 300-3 |year= 1995 |pmid= 7774936 |doi=  }}
*{{cite journal   |vauthors=Dumermuth E, Eldering JA, Grünberg J, etal |title=Cloning of the PABA peptide hydrolase alpha subunit (PPH alpha) from human small intestine and its expression in COS-1 cells |journal=FEBS Lett. |volume=335 |issue= 3 |pages= 367–75 |year= 1994 |pmid= 8262185 |doi=10.1016/0014-5793(93)80421-P }}
*{{cite journal  | author=Kaushal GP, Walker PD, Shah SV |title=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. |journal=J. Cell Biol. |volume=126 |issue= 5 |pages= 1319-27 |year= 1994 |pmid= 8063866 |doi=  }}
*{{cite journal  |vauthors=Bankus JM, Bond JS |title=Expression and distribution of meprin protease subunits in mouse intestine |journal=Arch. Biochem. Biophys. |volume=331 |issue= 1 |pages= 87–94 |year= 1996 |pmid= 8660687 |doi= 10.1006/abbi.1996.0286 }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi=  }}
*{{cite journal  |vauthors=Chevallier S, Ahn J, Boileau G, Crine P |title=Identification of the cysteine residues implicated in the formation of alpha 2 and alpha/beta dimers of rat meprin |journal=Biochem. J. |volume=317 |issue= Pt 3|pages= 731–8 |year= 1996 |pmid= 8760356 |doi= | pmc=1217546  }}
*{{cite journal  | author=Dumermuth E, Eldering JA, Grünberg J, ''et al.'' |title=Cloning of the PABA peptide hydrolase alpha subunit (PPH alpha) from human small intestine and its expression in COS-1 cells. |journal=FEBS Lett. |volume=335 |issue= 3 |pages= 367-75 |year= 1994 |pmid= 8262185 |doi= }}
*{{cite journal   |vauthors=Eldering JA, Grünberg J, Hahn D, etal |title=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 |journal=Eur. J. Biochem. |volume=247 |issue= 3 |pages= 920–32 |year= 1997 |pmid= 9288916 |doi=10.1111/j.1432-1033.1997.00920.x }}
*{{cite journal  | author=Bankus JM, Bond JS |title=Expression and distribution of meprin protease subunits in mouse intestine. |journal=Arch. Biochem. Biophys. |volume=331 |issue= 1 |pages= 87-94 |year= 1996 |pmid= 8660687 |doi= 10.1006/abbi.1996.0286 }}
*{{cite journal   |vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, etal |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library |journal=Gene |volume=200 |issue= 1–2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3 }}
*{{cite journal | author=Chevallier S, Ahn J, Boileau G, Crine P |title=Identification of the cysteine residues implicated in the formation of alpha 2 and alpha/beta dimers of rat meprin. |journal=Biochem. J. |volume=317 ( Pt 3) |issue= |pages= 731-8 |year= 1996 |pmid= 8760356 |doi=  }}
*{{cite journal   |vauthors=Lottaz D, Hahn D, Müller S, etal |title=Secretion of human meprin from intestinal epithelial cells depends on differential expression of the alpha and beta subunits |journal=Eur. J. Biochem. |volume=259 |issue= 1–2 |pages= 496–504 |year= 1999 |pmid= 9914532 |doi=10.1046/j.1432-1327.1999.00071.x }}
*{{cite journal | author=Eldering JA, Grünberg J, Hahn D, ''et al.'' |title=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. |journal=Eur. J. Biochem. |volume=247 |issue= 3 |pages= 920-32 |year= 1997 |pmid= 9288916 |doi=  }}
*{{cite journal   |vauthors=Richter R, Schulz-Knappe P, Schrader M, etal |title=Composition of the peptide fraction in human blood plasma: database of circulating human peptides |journal=J. Chromatogr. B |volume=726 |issue= 1–2 |pages= 25–35 |year= 1999 |pmid= 10348167 |doi=10.1016/S0378-4347(99)00012-2 }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi=  }}
*{{cite journal  |vauthors=Köhler D, Kruse M, Stöcker W, Sterchi EE |title=Heterologously overexpressed, affinity-purified human meprin alpha is functionally active and cleaves components of the basement membrane in vitro |journal=FEBS Lett. |volume=465 |issue= 1 |pages= 2–7 |year= 2000 |pmid= 10620696 |doi=10.1016/S0014-5793(99)01712-3 }}
*{{cite journal | author=Lottaz D, Hahn D, Müller S, ''et al.'' |title=Secretion of human meprin from intestinal epithelial cells depends on differential expression of the alpha and beta subunits. |journal=Eur. J. Biochem. |volume=259 |issue= 1-2 |pages= 496-504 |year= 1999 |pmid= 9914532 |doi=  }}
*{{cite journal  |vauthors=Jiang W, Le B |title=Structure and expression of the human MEP1A gene encoding the alpha subunit of metalloendopeptidase meprin A |journal=Arch. Biochem. Biophys. |volume=379 |issue= 2 |pages= 183–7 |year= 2000 |pmid= 10898933 |doi= 10.1006/abbi.2000.1873 }}
*{{cite journal  | author=Richter R, Schulz-Knappe P, Schrader M, ''et al.'' |title=Composition of the peptide fraction in human blood plasma: database of circulating human peptides. |journal=J. Chromatogr. B Biomed. Sci. Appl. |volume=726 |issue= 1-2 |pages= 25-35 |year= 1999 |pmid= 10348167 |doi=  }}
*{{cite journal  |vauthors=Kumar JM, Bond JS |title=Developmental expression of meprin metalloprotease subunits in ICR and C3H/He mouse kidney and intestine in the embryo, postnatally and after weaning |journal=Biochim. Biophys. Acta |volume=1518 |issue= 1–2 |pages= 106–14 |year= 2001 |pmid= 11267665 |doi= 10.1016/S0167-4781(01)00188-9}}
*{{cite journal  | author=Köhler D, Kruse M, Stöcker W, Sterchi EE |title=Heterologously overexpressed, affinity-purified human meprin alpha is functionally active and cleaves components of the basement membrane in vitro. |journal=FEBS Lett. |volume=465 |issue= 1 |pages= 2-7 |year= 2000 |pmid= 10620696 |doi= }}
*{{cite journal   |vauthors=Bertenshaw GP, Turk BE, Hubbard SJ, etal |title=Marked differences between metalloproteases meprin A and B in substrate and peptide bond specificity |journal=J. Biol. Chem. |volume=276 |issue= 16 |pages= 13248–55 |year= 2001 |pmid= 11278902 |doi= 10.1074/jbc.M011414200 }}
*{{cite journal  | author=Jiang W, Le B |title=Structure and expression of the human MEP1A gene encoding the alpha subunit of metalloendopeptidase meprin A. |journal=Arch. Biochem. Biophys. |volume=379 |issue= 2 |pages= 183-7 |year= 2000 |pmid= 10898933 |doi= 10.1006/abbi.2000.1873 }}
*{{cite journal  |vauthors=Ishmael FT, Norcum MT, Benkovic SJ, Bond JS |title=Multimeric structure of the secreted meprin A metalloproteinase and characterization of the functional protomer |journal=J. Biol. Chem. |volume=276 |issue= 25 |pages= 23207–11 |year= 2001 |pmid= 11301339 |doi= 10.1074/jbc.M102654200 }}
*{{cite journal | author=Kumar JM, Bond JS |title=Developmental expression of meprin metalloprotease subunits in ICR and C3H/He mouse kidney and intestine in the embryo, postnatally and after weaning. |journal=Biochim. Biophys. Acta |volume=1518 |issue= 1-2 |pages= 106-14 |year= 2001 |pmid= 11267665 |doi= }}
*{{cite journal   |vauthors=Rösmann S, Hahn D, Lottaz D, etal |title=Activation of human meprin-alpha in a cell culture model of colorectal cancer is triggered by the plasminogen-activating system |journal=J. Biol. Chem. |volume=277 |issue= 43 |pages= 40650–8 |year= 2002 |pmid= 12189145 |doi= 10.1074/jbc.M206203200 }}
*{{cite journal  | author=Bertenshaw GP, Turk BE, Hubbard SJ, ''et al.'' |title=Marked differences between metalloproteases meprin A and B in substrate and peptide bond specificity. |journal=J. Biol. Chem. |volume=276 |issue= 16 |pages= 13248-55 |year= 2001 |pmid= 11278902 |doi= 10.1074/jbc.M011414200 }}
*{{cite journal   |vauthors=Norman LP, Jiang W, Han X, etal |title=Targeted Disruption of the Meprin β Gene in Mice Leads to Underrepresentation of Knockout Mice and Changes in Renal Gene Expression Profiles |journal=Mol. Cell. Biol. |volume=23 |issue= 4 |pages= 1221–30 |year= 2003 |pmid= 12556482 |doi=10.1128/MCB.23.4.1221-1230.2003  | pmc=141138  }}
*{{cite journal | author=Ishmael FT, Norcum MT, Benkovic SJ, Bond JS |title=Multimeric structure of the secreted meprin A metalloproteinase and characterization of the functional protomer. |journal=J. Biol. Chem. |volume=276 |issue= 25 |pages= 23207-11 |year= 2001 |pmid= 11301339 |doi= 10.1074/jbc.M102654200 }}
*{{cite journal   |vauthors=Kimura K, Wakamatsu A, Suzuki Y, etal |title=Diversification of transcriptional modulation: Large-scale identification and characterization of putative alternative promoters of human genes |journal=Genome Res. |volume=16 |issue= 1 |pages= 55–65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406 | pmc=1356129 }}
*{{cite journal | author=Rösmann S, Hahn D, Lottaz D, ''et al.'' |title=Activation of human meprin-alpha in a cell culture model of colorectal cancer is triggered by the plasminogen-activating system. |journal=J. Biol. Chem. |volume=277 |issue= 43 |pages= 40650-8 |year= 2002 |pmid= 12189145 |doi= 10.1074/jbc.M206203200 }}
*{{cite journal | author=Norman LP, Jiang W, Han X, ''et al.'' |title=Targeted disruption of the meprin beta gene in mice leads to underrepresentation of knockout mice and changes in renal gene expression profiles. |journal=Mol. Cell. Biol. |volume=23 |issue= 4 |pages= 1221-30 |year= 2003 |pmid= 12556482 |doi= }}
*{{cite journal  | author=Kimura K, Wakamatsu A, Suzuki Y, ''et al.'' |title=Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes. |journal=Genome Res. |volume=16 |issue= 1 |pages= 55-65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406 }}
}}
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Latest revision as of 08:57, 23 July 2018

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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.[1][2] The MEP1A locus is on chromosome 6p in humans and on chromosome 17 in mice.[3]

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

  1. ↑ 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.
  2. ↑ "Entrez Gene: MEP1A meprin A, alpha (PABA peptide hydrolase)".
  3. ↑ 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.

Further reading


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