XPNPEP2

From Wikipedia, the free encyclopedia

X-prolyl aminopeptidase (aminopeptidase P) 2, membrane-bound

Identifiers

External IDs

OMIM: 300145 MGI: 2180001 HomoloGene: 37766

Gene ontology
Molecular Function:	• metalloexopeptidase activity • X-Pro aminopeptidase activity • manganese ion binding • metal ion binding • GPI anchor binding
Cellular Component:	• membrane
Biological Process:	• proteolysis

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

Refseq

NM_003399 (mRNA)
NP_003390 (protein)

NM_133213 (mRNA)
NP_573476 (protein)

Location

Chr X: 128.7 - 128.73 Mb

Chr X: 44.35 - 44.38 Mb

Pubmed search

[1]

[2]

X-prolyl aminopeptidase (aminopeptidase P) 2, membrane-bound, also known as XPNPEP2, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: XPNPEP2 X-prolyl aminopeptidase (aminopeptidase P) 2, membrane-bound.

[edit] 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. PMID 1510698.
Venema RC, Ju H, Zou R, et al. (1997). "Cloning and tissue distribution of human membrane-bound aminopeptidase P.". Biochim. Biophys. Acta 1354 (1): 45–8. PMID 9375790.
Sprinkle TJ, Stone AA, Venema RC, et al. (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.
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. 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. 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. PMID 10894934.
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. doi:10.1073/pnas.242603899. 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. 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. PMID 15489334.
Ross MT, Grafham DV, Coffey AJ, et al. (2005). "The DNA sequence of the human X chromosome.". Nature 434 (7031): 325–37. doi:10.1038/nature03440. 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.