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{{Infobox_gene}}
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'''Dipeptidyl-peptidase 2''' is an [[enzyme]] that in humans is encoded by the ''DPP7'' [[gene]].<ref name="pmid10477574">{{cite journal | vauthors = Chiravuri M, Schmitz T, Yardley K, Underwood R, Dayal Y, Huber BT | title = A novel apoptotic pathway in quiescent lymphocytes identified by inhibition of a post-proline cleaving aminodipeptidase: a candidate target protease, quiescent cell proline dipeptidase | journal = J Immunol | volume = 163 | issue = 6 | pages = 3092–9 |date=Oct 1999 | pmid = 10477574 | pmc =  | doi =  }}</ref><ref name="pmid11139392">{{cite journal | vauthors = Fukasawa KM, Fukasawa K, Higaki K, Shiina N, Ohno M, Ito S, Otogoto J, Ota N | title = Cloning and functional expression of rat kidney dipeptidyl peptidase II | journal = Biochem J | volume = 353 | issue = Pt 2 | pages = 283–90 |date=Jan 2001 | pmid = 11139392 | pmc = 1221570 | doi =10.1042/0264-6021:3530283 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: DPP7 dipeptidyl-peptidase 7| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=29952| accessdate = }}</ref>
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{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Dipeptidyl-peptidase 7
| HGNCid = 14892
| Symbol = DPP7
| AltSymbols =; DPP2; DPPII; QPP
| OMIM = 610537
| ECnumber = 
| Homologene = 22748
| MGIid = 1933213
| Function = {{GNF_GO|id=GO:0004177 |text = aminopeptidase activity}} {{GNF_GO|id=GO:0004252 |text = serine-type endopeptidase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008236 |text = serine-type peptidase activity}}
  | Component = {{GNF_GO|id=GO:0005764 |text = lysosome}}
  | Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}}  
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 29952
    | Hs_Ensembl = ENSG00000176978
    | Hs_RefseqProtein = XP_001130451
    | Hs_RefseqmRNA = XM_001130451
    | Hs_GenLoc_db =
    | Hs_GenLoc_chr = 9
    | Hs_GenLoc_start = 139124814
    | Hs_GenLoc_end = 139129016
    | Hs_Uniprot = Q9UHL4
    | Mm_EntrezGene = 83768
    | Mm_Ensembl = ENSMUSG00000026958
    | Mm_RefseqmRNA = NM_031843
    | Mm_RefseqProtein = NP_114031
    | Mm_GenLoc_db =   
    | Mm_GenLoc_chr = 2
    | Mm_GenLoc_start = 25174296
    | Mm_GenLoc_end = 25178340
    | Mm_Uniprot = Q8R082
  }}
}}
'''Dipeptidyl-peptidase 7''', also known as '''DPP7''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DPP7 dipeptidyl-peptidase 7| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=29952| accessdate = }}</ref>


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| section_title =  
| section_title =  
| summary_text = The protein encoded by this gene is a post-proline cleaving aminopeptidase expressed in quiescent lymphocytes. The resting lymphocytes are maintained through suppression of apoptosis, a state which is disrupted by inhibition of this novel serine protease. The enzyme has strong sequence homology with prolylcarboxypeptidase and is active at both acidic and neutral pH.<ref name="entrez">{{cite web | title = Entrez Gene: DPP7 dipeptidyl-peptidase 7| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=29952| accessdate = }}</ref>
| summary_text = The protein encoded by this gene is a post-proline cleaving aminopeptidase expressed in quiescent lymphocytes. The resting lymphocytes are maintained through suppression of apoptosis, a state which is disrupted by inhibition of this novel serine protease. The enzyme has strong sequence homology with prolylcarboxypeptidase and is active at both acidic and neutral pH.<ref name="entrez" />
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Fornas E, Mayordomo F, Renau-Piqueras J, Alborch E |title=Effect of cholesterol and its autooxidation derivatives on endocytosis and dipeptidyl peptidases of aortic endothelial cells. |journal=Histol. Histopathol. |volume=7 |issue= 2 |pages= 163-8 |year= 1992 |pmid= 1515698 |doi=  }}
*{{cite journal  | vauthors=Fornas E, Mayordomo F, Renau-Piqueras J, Alborch E |title=Effect of cholesterol and its autooxidation derivatives on endocytosis and dipeptidyl peptidases of aortic endothelial cells |journal=Histol. Histopathol. |volume=7 |issue= 2 |pages= 163–8 |year= 1992 |pmid= 1515698 |doi=  }}
*{{cite journal  | author=Roberts VJ, Gorenstein C |title=The effect of antimitotic agents on the intraneuronal distribution of lysosomes. |journal=Brain Res. |volume=521 |issue= 1-2 |pages= 62-72 |year= 1990 |pmid= 2207678 |doi=  }}
*{{cite journal  | vauthors=Roberts VJ, Gorenstein C |title=The effect of antimitotic agents on the intraneuronal distribution of lysosomes |journal=Brain Res. |volume=521 |issue= 1–2 |pages= 62–72 |year= 1990 |pmid= 2207678 |doi=10.1016/0006-8993(90)91525-L }}
*{{cite journal  | author=Andersen KJ, McDonald JK |title=Lysosomal heterogeneity of dipeptidyl peptidase II active on collagen-related peptides. |journal=Ren. Physiol. Biochem. |volume=12 |issue= 1 |pages= 32-40 |year= 1989 |pmid= 2727382 |doi=  }}
*{{cite journal  | vauthors=Andersen KJ, McDonald JK |title=Lysosomal heterogeneity of dipeptidyl peptidase II active on collagen-related peptides |journal=Ren. Physiol. Biochem. |volume=12 |issue= 1 |pages= 32–40 |year= 1989 |pmid= 2727382 |doi=  10.1159/000173177}}
*{{cite journal  | author=Demuth HU, Schlenzig D, Schierhorn A, ''et al.'' |title=Design of (omega-N-(O-acyl)hydroxy amid) aminodicarboxylic acid pyrrolidides as potent inhibitors of proline-specific peptidases. |journal=FEBS Lett. |volume=320 |issue= 1 |pages= 23-7 |year= 1993 |pmid= 8096464 |doi=  }}
*{{cite journal  | author=Demuth HU |title=Design of (omega-N-(O-acyl)hydroxy amid) aminodicarboxylic acid pyrrolidides as potent inhibitors of proline-specific peptidases |journal=FEBS Lett. |volume=320 |issue= 1 |pages= 23–7 |year= 1993 |pmid= 8096464 |doi=10.1016/0014-5793(93)81649-K |name-list-format=vanc| author2=Schlenzig D  | author3=Schierhorn A | display-authors=3  | last4=Grosche  | first4=G  | last5=Chapotchartier  | first5=M  | last6=Gripon  | first6=J }}
*{{cite journal  | author=Chiravuri M, Schmitz T, Yardley K, ''et al.'' |title=A novel apoptotic pathway in quiescent lymphocytes identified by inhibition of a post-proline cleaving aminodipeptidase: a candidate target protease, quiescent cell proline dipeptidase. |journal=J. Immunol. |volume=163 |issue= 6 |pages= 3092-9 |year= 1999 |pmid= 10477574 |doi=  }}
*{{cite journal  | author=Underwood R |title=Sequence, purification, and cloning of an intracellular serine protease, quiescent cell proline dipeptidase |journal=J. Biol. Chem. |volume=274 |issue= 48 |pages= 34053–8 |year= 1999 |pmid= 10567372 |doi=10.1074/jbc.274.48.34053  |name-list-format=vanc| author2=Chiravuri M  | author3=Lee H  | display-authors=3  | last4=Schmitz  | first4=T  | last5=Kabcenell  | first5=AK  | last6=Yardley  | first6=K  | last7=Huber  | first7=BT }}
*{{cite journal  | author=Underwood R, Chiravuri M, Lee H, ''et al.'' |title=Sequence, purification, and cloning of an intracellular serine protease, quiescent cell proline dipeptidase. |journal=J. Biol. Chem. |volume=274 |issue= 48 |pages= 34053-8 |year= 1999 |pmid= 10567372 |doi=  }}
*{{cite journal  | author=Chiravuri M |title=Vesicular localization and characterization of a novel post-proline-cleaving aminodipeptidase, quiescent cell proline dipeptidase |journal=J. Immunol. |volume=165 |issue= 10 |pages= 5695–702 |year= 2000 |pmid= 11067927 |doi=  10.4049/jimmunol.165.10.5695|name-list-format=vanc| author2=Agarraberes F  | author3=Mathieu SL  | display-authors=3  | last4=Lee  | first4=H  | last5=Huber  | first5=BT }}
*{{cite journal  | author=Chiravuri M, Agarraberes F, Mathieu SL, ''et al.'' |title=Vesicular localization and characterization of a novel post-proline-cleaving aminodipeptidase, quiescent cell proline dipeptidase. |journal=J. Immunol. |volume=165 |issue= 10 |pages= 5695-702 |year= 2000 |pmid= 11067927 |doi=  }}
*{{cite journal  | author=Araki H |title=Purification, molecular cloning, and immunohistochemical localization of dipeptidyl peptidase II from the rat kidney and its identity with quiescent cell proline dipeptidase |journal=J. Biochem. |volume=129 |issue= 2 |pages= 279–88 |year= 2001 |pmid= 11173530 |doi= 10.1093/oxfordjournals.jbchem.a002855|name-list-format=vanc| author2=Li Y  | author3=Yamamoto Y  | display-authors=3  | last4=Haneda  | first4=M  | last5=Nishi  | first5=K  | last6=Kikkawa  | first6=R  | last7=Ohkubo  | first7=I }}
*{{cite journal  | author=Fukasawa KM, Fukasawa K, Higaki K, ''et al.'' |title=Cloning and functional expression of rat kidney dipeptidyl peptidase II. |journal=Biochem. J. |volume=353 |issue= Pt 2 |pages= 283-90 |year= 2001 |pmid= 11139392 |doi=  }}
*{{cite journal  | author=Zhan H |title=Peptidases play an important role in cataractogenesis: an immunohistochemical study on lenses derived from Shumiya cataract rats |journal=Histochem. J. |volume=33 |issue= 9–10 |pages= 511–21 |year= 2002 |pmid= 12005022 |doi=10.1023/A:1014943522613  |name-list-format=vanc| author2=Yamamoto Y  | author3=Shumiya S  | display-authors=3  | last4=Kunimatsu  | first4=Mitoshi  | last5=Nishi  | first5=Katsuji  | last6=Ohkubo  | first6=Iwao  | last7=Kani  | first7=Kazutaka }}
*{{cite journal  | author=Araki H, Li Y, Yamamoto Y, ''et al.'' |title=Purification, molecular cloning, and immunohistochemical localization of dipeptidyl peptidase II from the rat kidney and its identity with quiescent cell proline dipeptidase. |journal=J. Biochem. |volume=129 |issue= 2 |pages= 279-88 |year= 2001 |pmid= 11173530 |doi=  }}
*{{cite journal  | author=Strausberg RL |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  |name-list-format=vanc| author2=Feingold EA  | author3=Grouse LH  | display-authors=3  | last4=Derge  | first4=JG  | last5=Klausner  | first5=RD  | last6=Collins  | first6=FS  | last7=Wagner  | first7=L  | last8=Shenmen  | first8=CM  | last9=Schuler  | first9=GD }}
*{{cite journal  | author=Zhan H, Yamamoto Y, Shumiya S, ''et al.'' |title=Peptidases play an important role in cataractogenesis: an immunohistochemical study on lenses derived from Shumiya cataract rats. |journal=Histochem. J. |volume=33 |issue= 9-10 |pages= 511-21 |year= 2002 |pmid= 12005022 |doi=  }}
*{{cite journal  | author=Leiting B |title=Catalytic properties and inhibition of proline-specific dipeptidyl peptidases II, IV and VII |journal=Biochem. J. |volume=371 |issue= Pt 2 |pages= 525–32 |year= 2003 |pmid= 12529175 |doi= 10.1042/BJ20021643 | pmc=1223300  |name-list-format=vanc| author2=Pryor KD  | author3=Wu JK  | display-authors=3  | last4=Marsilio  | first4=Frank  | last5=Patel  | first5=Reshma A.  | last6=Craik  | first6=Charles S.  | last7=Ellman  | first7=Jonathan A.  | last8=Cummings  | first8=Richard T.  | last9=Thornberry  | first9=Nancy A. }}
*{{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=Lehner B, Sanderson CM |title=A Protein Interaction Framework for Human mRNA Degradation |journal=Genome Res. |volume=14 |issue= 7 |pages= 1315–23 |year= 2004 |pmid= 15231747 |doi= 10.1101/gr.2122004 | pmc=442147 }}
*{{cite journal  | author=Leiting B, Pryor KD, Wu JK, ''et al.'' |title=Catalytic properties and inhibition of proline-specific dipeptidyl peptidases II, IV and VII. |journal=Biochem. J. |volume=371 |issue= Pt 2 |pages= 525-32 |year= 2003 |pmid= 12529175 |doi= 10.1042/BJ20021643 }}
*{{cite journal  | author=Gerhard DS |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  |name-list-format=vanc| author2=Wagner L  | author3=Feingold EA  | display-authors=3  | last4=Shenmen  | first4=CM  | last5=Grouse  | first5=LH  | last6=Schuler  | first6=G  | last7=Klein  | first7=SL  | last8=Old  | first8=S  | last9=Rasooly  | first9=R }}
*{{cite journal  | author=Lehner B, Sanderson CM |title=A protein interaction framework for human mRNA degradation. |journal=Genome Res. |volume=14 |issue= 7 |pages= 1315-23 |year= 2004 |pmid= 15231747 |doi= 10.1101/gr.2122004 }}
*{{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 }}
}}
}}
{{refend}}
{{refend}}


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Latest revision as of 18:42, 30 August 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

Dipeptidyl-peptidase 2 is an enzyme that in humans is encoded by the DPP7 gene.[1][2][3]

The protein encoded by this gene is a post-proline cleaving aminopeptidase expressed in quiescent lymphocytes. The resting lymphocytes are maintained through suppression of apoptosis, a state which is disrupted by inhibition of this novel serine protease. The enzyme has strong sequence homology with prolylcarboxypeptidase and is active at both acidic and neutral pH.[3]

References

  1. ↑ Chiravuri M, Schmitz T, Yardley K, Underwood R, Dayal Y, Huber BT (Oct 1999). "A novel apoptotic pathway in quiescent lymphocytes identified by inhibition of a post-proline cleaving aminodipeptidase: a candidate target protease, quiescent cell proline dipeptidase". J Immunol. 163 (6): 3092–9. PMID 10477574.
  2. ↑ Fukasawa KM, Fukasawa K, Higaki K, Shiina N, Ohno M, Ito S, Otogoto J, Ota N (Jan 2001). "Cloning and functional expression of rat kidney dipeptidyl peptidase II". Biochem J. 353 (Pt 2): 283–90. doi:10.1042/0264-6021:3530283. PMC 1221570. PMID 11139392.
  3. ↑ 3.0 3.1 "Entrez Gene: DPP7 dipeptidyl-peptidase 7".

Further reading



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