DPP3: Difference between revisions

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{{Infobox_gene}}
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'''Dipeptidyl-peptidase 3''' is an [[enzyme]] that in humans is encoded by the ''DPP3'' [[gene]].<ref name="pmid10773679">{{cite journal | vauthors = Fukasawa KM, Fukasawa K, Harada M | title = Assignment of the dipeptidyl peptidase III gene (DPP3) to human chromosome 11 band q12→q13.1 by in situ hybridization | journal = Cytogenet Cell Genet | volume = 88 | issue = 1–2 | pages = 99–100 |date=Jun 2000 | pmid = 10773679 | pmc =  | doi =10.1159/000015498 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: DPP3 dipeptidyl-peptidase 3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10072| accessdate = }}</ref>
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{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = Dipeptidyl-peptidase 3
| HGNCid = 3008
| Symbol = DPP3
| AltSymbols =; DPPIII; FLJ11387; FLJ22331
| OMIM = 606818
| ECnumber = 
| Homologene = 40210
| MGIid = 1922471
| Function = {{GNF_GO|id=GO:0004177 |text = aminopeptidase activity}} {{GNF_GO|id=GO:0008237 |text = metallopeptidase activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0017039 |text = dipeptidyl-peptidase III activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 10072
    | Hs_Ensembl =   
    | Hs_RefseqProtein = NP_005691
    | Hs_RefseqmRNA = NM_005700
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 
    | Hs_GenLoc_start = 
    | Hs_GenLoc_end =   
    | Hs_Uniprot = 
    | Mm_EntrezGene = 75221
    | Mm_Ensembl = ENSMUSG00000063904
    | Mm_RefseqmRNA = NM_133803
    | Mm_RefseqProtein = NP_598564
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 19
    | Mm_GenLoc_start = 4907232
    | Mm_GenLoc_end = 4928252
    | Mm_Uniprot = Q3THP1
  }}
}}
'''Dipeptidyl-peptidase 3''', also known as '''DPP3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DPP3 dipeptidyl-peptidase 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10072| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = This gene encodes a protein that is a member of the S9B family in clan SC of the serine proteases. This cytoplasmic protein binds a single zinc ion with its zinc-binding motif (HELLGH) and has post-proline dipeptidyl aminopeptidase activity, cleaving Xaa-Pro dipeptides from the N-termini of proteins. Increased activity of this protein is associated with endometrial and ovarian cancers. Alternate transcriptional splice variants have been characterized.<ref name="entrez">{{cite web | title = Entrez Gene: DPP3 dipeptidyl-peptidase 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10072| accessdate = }}</ref>
| summary_text = This gene encodes a protein that is a member of the S9B family in clan SC of the serine proteases. This cytoplasmic protein binds a single zinc ion with its zinc-binding motif (HELLGH) and has post-proline dipeptidyl aminopeptidase activity, cleaving Xaa-Pro dipeptides from the N-termini of proteins. Increased activity of this protein is associated with endometrial and ovarian cancers. Alternate transcriptional splice variants have been characterized.<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=Kar NC, Pearson CM |title=Dipeptidyl peptidases in human muscle disease. |journal=Clin. Chim. Acta |volume=82 |issue= 1-2 |pages= 185-92 |year= 1978 |pmid= 618680 |doi=  }}
*{{cite journal  | vauthors=Kar NC, Pearson CM |title=Dipeptidyl peptidases in human muscle disease |journal=Clin. Chim. Acta |volume=82 |issue= 1–2 |pages= 185–92 |year= 1978 |pmid= 618680 |doi=10.1016/0009-8981(78)90042-6 }}
*{{cite journal  | author=Grdisa M, Vitale L |title=Types and localization of aminopeptidases in different human blood cells. |journal=Int. J. Biochem. |volume=23 |issue= 3 |pages= 339-45 |year= 1991 |pmid= 2044841 |doi=  }}
*{{cite journal  | vauthors=Grdisa M, Vitale L |title=Types and localization of aminopeptidases in different human blood cells |journal=Int. J. Biochem. |volume=23 |issue= 3 |pages= 339–45 |year= 1991 |pmid= 2044841 |doi=10.1016/0020-711X(91)90116-5 }}
*{{cite journal  | author=Swanson AA, Davis RM, Meinhardt NC |title=Proteases in human lenses and their possible significance. |journal=Curr. Eye Res. |volume=4 |issue= 1 |pages= 43-8 |year= 1985 |pmid= 2858361 |doi=  }}
*{{cite journal  | vauthors=Swanson AA, Davis RM, Meinhardt NC |title=Proteases in human lenses and their possible significance |journal=Curr. Eye Res. |volume=4 |issue= 1 |pages= 43–8 |year= 1985 |pmid= 2858361 |doi=10.3109/02713688508999965 }}
*{{cite journal  | author=Vanha-Perttula T |title=Dipeptidyl peptidase III and alanyl aminopeptidase in the human seminal plasma: origin and biochemical properties. |journal=Clin. Chim. Acta |volume=177 |issue= 2 |pages= 179-95 |year= 1989 |pmid= 2906822 |doi=  }}
*{{cite journal  | author=Vanha-Perttula T |title=Dipeptidyl peptidase III and alanyl aminopeptidase in the human seminal plasma: origin and biochemical properties |journal=Clin. Chim. Acta |volume=177 |issue= 2 |pages= 179–95 |year= 1989 |pmid= 2906822 |doi=10.1016/0009-8981(88)90140-4 }}
*{{cite journal  | author=Shimamori Y, Watanabe Y, Fujimoto Y |title=Human placental dipeptidyl aminopeptidase III: hydrolysis of enkephalins and its stimulation by cobaltous ion. |journal=Biochem. Med. Metab. Biol. |volume=40 |issue= 3 |pages= 305-10 |year= 1989 |pmid= 3233187 |doi= }}
*{{cite journal  | vauthors=Shimamori Y, Watanabe Y, Fujimoto Y |title=Human placental dipeptidyl aminopeptidase III: hydrolysis of enkephalins and its stimulation by cobaltous ion |journal=Biochem. Med. Metab. Biol. |volume=40 |issue= 3 |pages= 305–10 |year= 1989 |pmid= 3233187 |doi=10.1016/0885-4505(88)90133-8  }}
*{{cite journal  | author=Abramić M, Zubanović M, Vitale L |title=Dipeptidyl peptidase III from human erythrocytes. |journal=Biol. Chem. Hoppe-Seyler |volume=369 |issue= 1 |pages= 29-38 |year= 1988 |pmid= 3348886 |doi=  }}
*{{cite journal  | vauthors=Abramić M, Zubanović M, Vitale L |title=Dipeptidyl peptidase III from human erythrocytes |journal=Biol. Chem. Hoppe-Seyler |volume=369 |issue= 1 |pages= 29–38 |year= 1988 |pmid= 3348886 |doi=10.1515/bchm3.1988.369.1.29 }}
*{{cite journal  | author=Shimamori Y, Watanabe Y, Fujimoto Y |title=Purification and characterization of dipeptidyl aminopeptidase III from human placenta. |journal=Chem. Pharm. Bull. |volume=34 |issue= 8 |pages= 3333-40 |year= 1987 |pmid= 3791505 |doi=  }}
*{{cite journal  | vauthors=Shimamori Y, Watanabe Y, Fujimoto Y |title=Purification and characterization of dipeptidyl aminopeptidase III from human placenta |journal=Chem. Pharm. Bull. |volume=34 |issue= 8 |pages= 3333–40 |year= 1987 |pmid= 3791505 |doi=  10.1248/cpb.34.3333}}
*{{cite journal  | author=Swanson AA, Davis RM, McDonald JK |title=Dipeptidyl peptidase III of human cataractous lenses. Partial purification. |journal=Curr. Eye Res. |volume=3 |issue= 2 |pages= 287-91 |year= 1984 |pmid= 6368131 |doi=  }}
*{{cite journal  | vauthors=Swanson AA, Davis RM, McDonald JK |title=Dipeptidyl peptidase III of human cataractous lenses. Partial purification |journal=Curr. Eye Res. |volume=3 |issue= 2 |pages= 287–91 |year= 1984 |pmid= 6368131 |doi=10.3109/02713688408997211 }}
*{{cite journal  | author=Jones TH, Kapralou A |title=A rapid assay for dipeptidyl aminopeptidase III in human erythrocytes. |journal=Anal. Biochem. |volume=119 |issue= 2 |pages= 418-23 |year= 1982 |pmid= 7041700 |doi= }}
*{{cite journal  | vauthors=Jones TH, Kapralou A |title=A rapid assay for dipeptidyl aminopeptidase III in human erythrocytes |journal=Anal. Biochem. |volume=119 |issue= 2 |pages= 418–23 |year= 1982 |pmid= 7041700 |doi=10.1016/0003-2697(82)90607-8  }}
*{{cite journal  | author=Vitale L, Zubanović M, Abramić M |title=Properties and distribution of aminopeptidase and dipeptidyl aminopeptidase III of human erythrocytes. |journal=Acta Biol. Med. Ger. |volume=40 |issue= 10-11 |pages= 1489-95 |year= 1982 |pmid= 7044004 |doi=  }}
*{{cite journal  | vauthors=Vitale L, Zubanović M, Abramić M |title=Properties and distribution of aminopeptidase and dipeptidyl aminopeptidase III of human erythrocytes |journal=Acta Biol. Med. Ger. |volume=40 |issue= 10–11 |pages= 1489–95 |year= 1982 |pmid= 7044004 |doi=  }}
*{{cite journal  | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
*{{cite journal  | vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8  }}
*{{cite journal  | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
*{{cite journal  | vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library |journal=Gene |volume=200 |issue= 1–2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3  |display-authors=etal}}
*{{cite journal  | author=Fukasawa K, Fukasawa KM, Kanai M, ''et al.'' |title=Dipeptidyl peptidase III is a zinc metallo-exopeptidase. Molecular cloning and expression. |journal=Biochem. J. |volume=329 ( Pt 2) |issue=  |pages= 275-82 |year= 1998 |pmid= 9425109 |doi=  }}
*{{cite journal  | vauthors=Fukasawa K, Fukasawa KM, Kanai M |title=Dipeptidyl peptidase III is a zinc metallo-exopeptidase. Molecular cloning and expression |journal=Biochem. J. |volume=329 ( Pt 2) |issue=  Pt 2|pages= 275–82 |year= 1998 |pmid= 9425109 |doi=  | pmc=1219041  |display-authors=etal}}
*{{cite journal  | author=Simaga S, Babić D, Osmak M, ''et al.'' |title=Dipeptidyl peptidase III in malignant and non-malignant gynaecological tissue. |journal=Eur. J. Cancer |volume=34 |issue= 3 |pages= 399-405 |year= 1998 |pmid= 9640230 |doi=  }}
*{{cite journal  | vauthors=Simaga S, Babić D, Osmak M |title=Dipeptidyl peptidase III in malignant and non-malignant gynaecological tissue |journal=Eur. J. Cancer |volume=34 |issue= 3 |pages= 399–405 |year= 1998 |pmid= 9640230 |doi=10.1016/S0959-8049(97)00401-2 |display-authors=etal}}
*{{cite journal  | author=Akiyama T, Harada S, Kojima F, ''et al.'' |title=Fluostatins A and B, new inhibitors of dipeptidyl peptidase III, produced by Streptomyces sp. TA-3391. I. Taxonomy of producing strain, production, isolation, physico-chemical properties and biological properties. |journal=J. Antibiot. |volume=51 |issue= 6 |pages= 553-9 |year= 1998 |pmid= 9711218 |doi=  }}
*{{cite journal  | vauthors=Akiyama T, Harada S, Kojima F |title=Fluostatins A and B, new inhibitors of dipeptidyl peptidase III, produced by ''Streptomyces'' sp. TA-3391. I. Taxonomy of producing strain, production, isolation, physico-chemical properties and biological properties |journal=J. Antibiot. |volume=51 |issue= 6 |pages= 553–9 |year= 1998 |pmid= 9711218 |doi=  10.7164/antibiotics.51.553|display-authors=etal}}
*{{cite journal  | author=Fukasawa K, Fukasawa KM, Iwamoto H, ''et al.'' |title=The HELLGH motif of rat liver dipeptidyl peptidase III is involved in zinc coordination and the catalytic activity of the enzyme. |journal=Biochemistry |volume=38 |issue= 26 |pages= 8299-303 |year= 1999 |pmid= 10387075 |doi= 10.1021/bi9904959 }}
*{{cite journal  | vauthors=Fukasawa K, Fukasawa KM, Iwamoto H |title=The HELLGH motif of rat liver dipeptidyl peptidase III is involved in zinc coordination and the catalytic activity of the enzyme |journal=Biochemistry |volume=38 |issue= 26 |pages= 8299–303 |year= 1999 |pmid= 10387075 |doi= 10.1021/bi9904959 |display-authors=etal}}
*{{cite journal  | author=Fukasawa KM, Fukasawa K, Harada M |title=Assignment of the dipeptidyl peptidase III gene (DPP3) to human chromosome 11 band q12-->q13.1 by in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=88 |issue= 1-2 |pages= 99-100 |year= 2000 |pmid= 10773679 |doi= }}
*{{cite journal  | vauthors=Hashimoto J, Yamamoto Y, Kurosawa H |title=Identification of dipeptidyl peptidase III in human neutrophils |journal=Biochem. Biophys. Res. Commun. |volume=273 |issue= 2 |pages= 393–7 |year= 2000 |pmid= 10873616 |doi= 10.1006/bbrc.2000.2827 |display-authors=etal}}
*{{cite journal  | author=Hashimoto J, Yamamoto Y, Kurosawa H, ''et al.'' |title=Identification of dipeptidyl peptidase III in human neutrophils. |journal=Biochem. Biophys. Res. Commun. |volume=273 |issue= 2 |pages= 393-7 |year= 2000 |pmid= 10873616 |doi= 10.1006/bbrc.2000.2827 }}
*{{cite journal  | vauthors=Abramić M, Schleuder D, Dolovcak L |title=Human and rat dipeptidyl peptidase III: biochemical and mass spectrometric arguments for similarities and differences |journal=Biol. Chem. |volume=381 |issue= 12 |pages= 1233–43 |year= 2001 |pmid= 11209758 |doi=10.1515/BC.2000.151  |display-authors=etal}}
*{{cite journal  | author=Abramić M, Schleuder D, Dolovcak L, ''et al.'' |title=Human and rat dipeptidyl peptidase III: biochemical and mass spectrometric arguments for similarities and differences. |journal=Biol. Chem. |volume=381 |issue= 12 |pages= 1233-43 |year= 2001 |pmid= 11209758 |doi=  }}
*{{cite journal  | vauthors=Strausberg RL, Feingold EA, Grouse LH |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 |display-authors=etal}}
*{{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 }}
}}
}}
{{refend}}
{{refend}}
==External links==
* {{UCSC genome browser|DPP3}}
* {{UCSC gene details|DPP3}}
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Revision as of 18:41, 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 3 is an enzyme that in humans is encoded by the DPP3 gene.[1][2]

This gene encodes a protein that is a member of the S9B family in clan SC of the serine proteases. This cytoplasmic protein binds a single zinc ion with its zinc-binding motif (HELLGH) and has post-proline dipeptidyl aminopeptidase activity, cleaving Xaa-Pro dipeptides from the N-termini of proteins. Increased activity of this protein is associated with endometrial and ovarian cancers. Alternate transcriptional splice variants have been characterized.[2]

References

  1. ↑ Fukasawa KM, Fukasawa K, Harada M (Jun 2000). "Assignment of the dipeptidyl peptidase III gene (DPP3) to human chromosome 11 band q12→q13.1 by in situ hybridization". Cytogenet Cell Genet. 88 (1–2): 99–100. doi:10.1159/000015498. PMID 10773679.
  2. ↑ 2.0 2.1 "Entrez Gene: DPP3 dipeptidyl-peptidase 3".

Further reading

External links



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