XPNPEP2

XPNPEP2
Identifiers
Aliases	XPNPEP2 , AEACEI, APP2, X-prolyl aminopeptidase (aminopeptidase P) 2, membrane-bound, X-prolyl aminopeptidase 2
External IDs	OMIM: 300145 MGI: 2180001 HomoloGene: 37766 GeneCards: XPNPEP2
Gene location (Human) Chr. X chromosome (human) [1] Band Xq26.1 Start 129,738,949 bp [1] End 129,769,536 bp [1]
Gene location (Mouse) Chr. X chromosome (mouse) [2] Band X|X A4 Start 47,197,602 bp [2] End 47,225,858 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in jejunal mucosa kidney tubule glomerulus kidney duodenum metanephric glomerulus gastric mucosa right coronary artery left coronary artery right lobe of liver Top expressed in intestinal villus jejunum ileum proximal tubule esophagus duodenum skeletal muscle tissue lip quadriceps femoris muscle extraocular muscle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function peptidase activity aminopeptidase activity hydrolase activity metallopeptidase activity metal ion binding metalloaminopeptidase activity Cellular component anchored component of membrane extracellular exosome membrane extracellular region plasma membrane cytoplasm Biological process proteolysis C-terminal protein lipidation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 7512 170745 Ensembl ENSG00000122121 ENSMUSG00000037005 UniProt O43895 B1AVD1 RefSeq (mRNA) NM_003399 NM_001289729 NM_133213 RefSeq (protein) NP_003390 NP_001276658 NP_573476 Location (UCSC) Chr X: 129.74 – 129.77 Mb Chr X: 47.2 – 47.23 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Xaa-Pro aminopeptidase 2 is an enzyme that in humans is encoded by the XPNPEP2 gene. ^{[5] [6] [7]}

Aminopeptidase P is a hydrolase specific for N-terminal imido bonds, which are common to several collagen degradation products, neuropeptides, vasoactive peptides, and cytokines. Structurally, the enzyme is a member of the 'pita bread fold' family and occurs in mammalian tissues in both soluble and GPI-anchored membrane-bound forms. A membrane-bound and soluble form of this enzyme have been identified as products of two separate genes. ^[7]

References

1. GRCh38: Ensembl release 89: ENSG00000122121 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000037005 - 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. Venema RC, Ju H, Zou R, Venema VJ, Ryan JW (Dec 1997). "Cloning and tissue distribution of human membrane-bound aminopeptidase P". Biochim Biophys Acta. 1354 (1): 45–8. doi:10.1016/s0167-4781(97)00126-7. PMID   9375790.
6. Sprinkle TJ, Stone AA, Venema RC, Denslow ND, Caldwell C, Ryan JW (Apr 1999). "Assignment of the membrane-bound human aminopeptidase P gene (XPNPEP2) to chromosome Xq25". Genomics. 50 (1): 114–6. doi:10.1006/geno.1998.5302. PMID   9628831.
7. "Entrez Gene: XPNPEP2 X-prolyl aminopeptidase (aminopeptidase P) 2, membrane-bound".

Further reading

• Vanhoof G, De Meester I, Goossens F, et al. (1992). "Kininase activity in human platelets: cleavage of the Arg1-Pro2 bond of bradykinin by aminopeptidase P". Biochem. Pharmacol. 44 (3): 479–87. doi:10.1016/0006-2952(92)90439-P. PMID   1510698.
• Cottrell GS, Hyde RJ, Hooper NM, Turner AJ (1998). "The cloning and functional expression of human pancreatic aminopeptidase P". Biochem. Soc. Trans. 26 (3): S248. doi:10.1042/bst026s248. PMID   9765967.
• Dias Neto E, Correa RG, Verjovski-Almeida S, et al. (2000). "Shotgun sequencing of the human transcriptome with ORF expressed sequence tags". Proc. Natl. Acad. Sci. U.S.A. 97 (7): 3491–6. Bibcode:2000PNAS...97.3491D. doi: 10.1073/pnas.97.7.3491 . PMC   16267 . PMID   10737800.
• Prueitt RL, Ross JL, Zinn AR (2000). "Physical mapping of nine Xq translocation breakpoints and identification of XPNPEP2 as a premature ovarian failure candidate gene". Cytogenet. Cell Genet. 89 (1–2): 44–50. doi:10.1159/000015560. PMID   10894934. S2CID   46232057.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC   139241 . PMID   12477932.
• Fu GK, Wang JT, Yang J, et al. (2005). "Circular rapid amplification of cDNA ends for high-throughput extension cloning of partial genes". Genomics. 84 (1): 205–10. doi:10.1016/j.ygeno.2004.01.011. PMID   15203218.
• Suzuki Y, Yamashita R, Shirota M, et al. (2004). "Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions". Genome Res. 14 (9): 1711–8. doi:10.1101/gr.2435604. PMC   515316 . PMID   15342556.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC   528928 . PMID   15489334.
• Ross MT, Grafham DV, Coffey AJ, et al. (2005). "The DNA sequence of the human X chromosome". Nature. 434 (7031): 325–37. Bibcode:2005Natur.434..325R. doi:10.1038/nature03440. PMC   2665286 . PMID   15772651.
• Molinaro G, Duan QL, Chagnon M, et al. (2007). "Kinin-dependent hypersensitivity reactions in hemodialysis: metabolic and genetic factors". Kidney Int. 70 (10): 1823–31. doi: 10.1038/sj.ki.5001873 . PMID   17003818.