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{{Infobox_gene}}
{{PBB_Controls
'''Xaa-Pro aminopeptidase 2''' is an [[enzyme]] that in humans is encoded by the ''XPNPEP2'' [[gene]].<ref name="pmid9375790">{{cite journal | vauthors = Venema RC, Ju H, Zou R, Venema VJ, Ryan JW | title = Cloning and tissue distribution of human membrane-bound aminopeptidase P | journal = Biochim Biophys Acta | volume = 1354 | issue = 1 | pages = 45–8 |date=Dec 1997 | pmid = 9375790 | pmc =  | doi =  10.1016/s0167-4781(97)00126-7}}</ref><ref name="pmid9628831">{{cite journal | vauthors = Sprinkle TJ, Stone AA, Venema RC, Denslow ND, Caldwell C, Ryan JW | title = Assignment of the membrane-bound human aminopeptidase P gene (XPNPEP2) to chromosome Xq25 | journal = Genomics | volume = 50 | issue = 1 | pages = 114–6 |date=Apr 1999 | pmid = 9628831 | pmc = | doi = 10.1006/geno.1998.5302 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: XPNPEP2 X-prolyl aminopeptidase (aminopeptidase P) 2, membrane-bound| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7512| accessdate = }}</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
[[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 [[Glycosylphosphatidylinositol|GPI-anchored]] membrane-bound forms. A membrane-bound and soluble form of this enzyme have been identified as products of two separate genes.<ref name="entrez" />
{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = X-prolyl aminopeptidase (aminopeptidase P) 2, membrane-bound
| HGNCid = 12823
| Symbol = XPNPEP2
| AltSymbols =;
| OMIM = 300145
| ECnumber = 
| Homologene = 37766
| MGIid = 2180001
| GeneAtlas_image1 = PBB_GE_XPNPEP2_216910_at_tn.png
| GeneAtlas_image2 = PBB_GE_XPNPEP2_206484_s_at_tn.png
| Function = {{GNF_GO|id=GO:0008235 |text = metalloexopeptidase activity}} {{GNF_GO|id=GO:0008451 |text = X-Pro aminopeptidase activity}} {{GNF_GO|id=GO:0030145 |text = manganese ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0048503 |text = GPI anchor binding}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 7512
    | Hs_Ensembl = ENSG00000122121
    | Hs_RefseqProtein = NP_003390
    | Hs_RefseqmRNA = NM_003399
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = X
    | Hs_GenLoc_start = 128700631
    | Hs_GenLoc_end = 128731206
    | Hs_Uniprot = O43895
    | Mm_EntrezGene = 170745
    | Mm_Ensembl = ENSMUSG00000037005
    | Mm_RefseqmRNA = NM_133213
    | Mm_RefseqProtein = NP_573476
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = X
    | Mm_GenLoc_start = 44353502
    | Mm_GenLoc_end = 44381608
    | Mm_Uniprot = 
  }}
}}
'''X-prolyl aminopeptidase (aminopeptidase P) 2, membrane-bound''', also known as '''XPNPEP2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: XPNPEP2 X-prolyl aminopeptidase (aminopeptidase P) 2, membrane-bound| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7512| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: XPNPEP2 X-prolyl aminopeptidase (aminopeptidase P) 2, membrane-bound| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7512| accessdate = }}</ref>
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
*{{cite journal   |vauthors=Vanhoof G, De Meester I, Goossens F, etal |title=Kininase activity in human platelets: cleavage of the Arg1-Pro2 bond of bradykinin by aminopeptidase P |journal=Biochem. Pharmacol. |volume=44 |issue= 3 |pages= 479–87 |year= 1992 |pmid= 1510698 |doi=10.1016/0006-2952(92)90439-P  }}
| citations =
*{{cite journal  | vauthors=Cottrell GS, Hyde RJ, Hooper NM, Turner AJ |title=The cloning and functional expression of human pancreatic aminopeptidase P |journal=Biochem. Soc. Trans. |volume=26 |issue= 3 |pages= S248 |year= 1998 |pmid= 9765967 |doi=  }}
*{{cite journal | author=Vanhoof G, De Meester I, Goossens F, ''et al.'' |title=Kininase activity in human platelets: cleavage of the Arg1-Pro2 bond of bradykinin by aminopeptidase P. |journal=Biochem. Pharmacol. |volume=44 |issue= 3 |pages= 479-87 |year= 1992 |pmid= 1510698 |doi= }}
*{{cite journal   |vauthors=Dias Neto E, Correa RG, Verjovski-Almeida S, etal |title=Shotgun sequencing of the human transcriptome with ORF expressed sequence tags |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 7 |pages= 3491–6 |year= 2000 |pmid= 10737800 |doi=10.1073/pnas.97.7.3491  | pmc=16267 }}
*{{cite journal  | author=Venema RC, Ju H, Zou R, ''et al.'' |title=Cloning and tissue distribution of human membrane-bound aminopeptidase P. |journal=Biochim. Biophys. Acta |volume=1354 |issue= 1 |pages= 45-8 |year= 1997 |pmid= 9375790 |doi=  }}
*{{cite journal  | vauthors=Prueitt RL, Ross JL, Zinn AR |title=Physical mapping of nine Xq translocation breakpoints and identification of XPNPEP2 as a premature ovarian failure candidate gene |journal=Cytogenet. Cell Genet. |volume=89 |issue= 1–2 |pages= 44–50 |year= 2000 |pmid= 10894934 |doi=10.1159/000015560 }}
*{{cite journal  | author=Sprinkle TJ, Stone AA, Venema RC, ''et al.'' |title=Assignment of the membrane-bound human aminopeptidase P gene (XPNPEP2) to chromosome Xq25. |journal=Genomics |volume=50 |issue= 1 |pages= 114-6 |year= 1999 |pmid= 9628831 |doi= 10.1006/geno.1998.5302 }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }}
*{{cite journal  | author=Cottrell GS, Hyde RJ, Hooper NM, Turner AJ |title=The cloning and functional expression of human pancreatic aminopeptidase P. |journal=Biochem. Soc. Trans. |volume=26 |issue= 3 |pages= S248 |year= 1998 |pmid= 9765967 |doi=  }}
*{{cite journal   |vauthors=Fu GK, Wang JT, Yang J, etal |title=Circular rapid amplification of cDNA ends for high-throughput extension cloning of partial genes |journal=Genomics |volume=84 |issue= 1 |pages= 205–10 |year= 2005 |pmid= 15203218 |doi= 10.1016/j.ygeno.2004.01.011 }}
*{{cite journal | author=Dias Neto E, Correa RG, Verjovski-Almeida S, ''et al.'' |title=Shotgun sequencing of the human transcriptome with ORF expressed sequence tags. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 7 |pages= 3491-6 |year= 2000 |pmid= 10737800 |doi=  }}
*{{cite journal   |vauthors=Suzuki Y, Yamashita R, Shirota M, etal |title=Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions |journal=Genome Res. |volume=14 |issue= 9 |pages= 1711–8 |year= 2004 |pmid= 15342556 |doi= 10.1101/gr.2435604 | pmc=515316 }}
*{{cite journal  | author=Prueitt RL, Ross JL, Zinn AR |title=Physical mapping of nine Xq translocation breakpoints and identification of XPNPEP2 as a premature ovarian failure candidate gene. |journal=Cytogenet. Cell Genet. |volume=89 |issue= 1-2 |pages= 44-50 |year= 2000 |pmid= 10894934 |doi=  }}
*{{cite journal   |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal   |vauthors=Ross MT, Grafham DV, Coffey AJ, etal |title=The DNA sequence of the human X chromosome |journal=Nature |volume=434 |issue= 7031 |pages= 325–37 |year= 2005 |pmid= 15772651 |doi= 10.1038/nature03440 | pmc=2665286 }}
*{{cite journal | author=Fu GK, Wang JT, Yang J, ''et al.'' |title=Circular rapid amplification of cDNA ends for high-throughput extension cloning of partial genes. |journal=Genomics |volume=84 |issue= 1 |pages= 205-10 |year= 2005 |pmid= 15203218 |doi= 10.1016/j.ygeno.2004.01.011 }}
*{{cite journal   |vauthors=Molinaro G, Duan QL, Chagnon M, etal |title=Kinin-dependent hypersensitivity reactions in hemodialysis: metabolic and genetic factors |journal=Kidney Int. |volume=70 |issue= 10 |pages= 1823–31 |year= 2007 |pmid= 17003818 |doi= 10.1038/sj.ki.5001873 }}
*{{cite journal | author=Suzuki Y, Yamashita R, Shirota M, ''et al.'' |title=Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions. |journal=Genome Res. |volume=14 |issue= 9 |pages= 1711-8 |year= 2004 |pmid= 15342556 |doi= 10.1101/gr.2435604 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal | author=Ross MT, Grafham DV, Coffey AJ, ''et al.'' |title=The DNA sequence of the human X chromosome. |journal=Nature |volume=434 |issue= 7031 |pages= 325-37 |year= 2005 |pmid= 15772651 |doi= 10.1038/nature03440 }}
*{{cite journal | author=Molinaro G, Duan QL, Chagnon M, ''et al.'' |title=Kinin-dependent hypersensitivity reactions in hemodialysis: metabolic and genetic factors. |journal=Kidney Int. |volume=70 |issue= 10 |pages= 1823-31 |year= 2007 |pmid= 17003818 |doi= 10.1038/sj.ki.5001873 }}
}}
{{refend}}
{{refend}}


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Latest revision as of 21:42, 18 September 2017

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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

Xaa-Pro aminopeptidase 2 is an enzyme that in humans is encoded by the XPNPEP2 gene.[1][2][3]

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.[3]


References

  1. ↑ 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.
  2. ↑ 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.
  3. ↑ 3.0 3.1 "Entrez Gene: XPNPEP2 X-prolyl aminopeptidase (aminopeptidase P) 2, membrane-bound".

Further reading


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