MEP1B

MEP1B
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4GWM, 4GWN
Identifiers
Aliases	MEP1B , meprin A subunit beta
External IDs	OMIM: 600389 MGI: 96964 HomoloGene: 48382 GeneCards: MEP1B
Gene location (Human) Chr. Chromosome 18 (human) [1] Band 18q12.1 Start 32,185,069 bp [1] End 32,220,404 bp [1]
Gene location (Mouse) Chr. Chromosome 18 (mouse) [2] Band 18 A2|18 11.81 cM Start 21,194,980 bp [2] End 21,233,256 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in jejunal mucosa duodenum rectum gastric mucosa islet of Langerhans smooth muscle tissue left uterine tube sural nerve cerebellar hemisphere right lobe of liver Top expressed in ileum jejunum duodenum Intestinal epithelium kidney large intestine colon proximal tubule Paneth cell left colon More reference expression data BioGPS More reference expression data
Gene ontology Molecular function peptidase activity metalloendopeptidase activity protein binding metallopeptidase activity hydrolase activity metal ion binding identical protein binding zinc ion binding Cellular component integral component of membrane extracellular region membrane plasma membrane integral component of plasma membrane meprin A complex Biological process inflammatory response toxin transport proteolysis Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 4225 17288 Ensembl ENSG00000141434 ENSMUSG00000024313 UniProt Q16820 Q61847 RefSeq (mRNA) NM_001308171 NM_005925 NM_008586 RefSeq (protein) NP_001295100 NP_005916 NP_032612 Location (UCSC) Chr 18: 32.19 – 32.22 Mb Chr 18: 21.19 – 21.23 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Meprin A subunit beta is a protein that in humans is encoded by the MEP1B gene. ^{[5] [6]}

Meprins are multidomain zinc metalloproteases that are highly expressed in mammalian kidney and intestinal brush border membranes and in leukocytes and certain cancer cells. Mature meprins are oligomers of evolutionarily related, separately encoded alpha and/or beta subunits. Homooligomers of meprin-alpha (MEP1A; MIM 600388) are secreted; oligomers containing meprin-beta are associated with the plasma membrane. Substrates include bioactive peptides and extracellular matrix proteins. See MIM 600388 for further information on meprins.[supplied by OMIM] ^[6]

References

1. GRCh38: Ensembl release 89: ENSG00000141434 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000024313 - 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.
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.
6. "Entrez Gene: MEP1B meprin A, beta".

Further reading

• Yamaguchi T, Fukase M, Sugimoto T, et al. (1995). "Purification of meprin from human kidney and its role in parathyroid hormone degradation". Biol. Chem. Hoppe-Seyler. 375 (12): 821–4. PMID   7710697.
• 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.
• 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 (3): 731–8. doi:10.1042/bj3170731. PMC   1217546 . PMID   8760356.
• Chestukhin A, Muradov K, Litovchick L, Shaltiel S (1997). "The cleavage of protein kinase A by the kinase-splitting membranal proteinase is reproduced by meprin beta". J. Biol. Chem. 271 (47): 30272–80. doi: 10.1074/jbc.271.47.30272 . PMID   8939981.
• 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.
• 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.
• 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.
• Litovchick L, Friedmann E, Shaltiel S (2002). "A selective interaction between OS-9 and the carboxyl-terminal tail of meprin beta". J. Biol. Chem. 277 (37): 34413–23. doi: 10.1074/jbc.M203986200 . PMID   12093806.
• Leuenberger B, Hahn D, Pischitzis A, et al. (2003). "Human meprin beta: O-linked glycans in the intervening region of the type I membrane protein protect the C-terminal region from proteolytic cleavage and diminish its secretion". Biochem. J. 369 (Pt 3): 659–65. doi:10.1042/BJ20021398. PMC   1223113 . PMID   12387727.
• Bertenshaw GP, Norcum MT, Bond JS (2003). "Structure of homo- and hetero-oligomeric meprin metalloproteases. Dimers, tetramers, and high molecular mass multimers". J. Biol. Chem. 278 (4): 2522–32. doi: 10.1074/jbc.M208808200 . PMID   12399461.
• Norman LP, Jiang W, Han X, et al. (2003). "Targeted disruption of the meprin beta 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.
• Hahn D, Pischitzis A, Roesmann S, et al. (2003). "Phorbol 12-myristate 13-acetate-induced ectodomain shedding and phosphorylation of the human meprinbeta metalloprotease". J. Biol. Chem. 278 (44): 42829–39. doi: 10.1074/jbc.M211169200 . PMID   12941954.
• Herzog C, Kaushal GP, Haun RS (2005). "Generation of biologically active interleukin-1beta by meprin B.". Cytokine. 31 (5): 394–403. doi:10.1016/j.cyto.2005.06.012. PMID   16095909.
• Becker-Pauly C, Höwel M, Walker T, et al. (2007). "The alpha and beta subunits of the metalloprotease meprin are expressed in separate layers of human epidermis, revealing different functions in keratinocyte proliferation and differentiation". J. Invest. Dermatol. 127 (5): 1115–25. doi: 10.1038/sj.jid.5700675 . PMID   17195012.