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DPP3

From Wikipedia, the free encyclopedia
Protein-coding gene in the species Homo sapiens
DPP3
Available structures
PDBOrtholog search:PDBeRCSB
List of PDB id codes

3FVY,3T6B,3T6J,5E2Q,5EHH,5E33,5E3C,5E3A,5EGY

Identifiers
AliasesDPP3, DPPIII, dipeptidyl peptidase 3
External IDsOMIM:606818;MGI:1922471;HomoloGene:40210;GeneCards:DPP3;OMA:DPP3 - orthologs
Gene location (Human)
Chromosome 11 (human)
Chr.Chromosome 11 (human)[1]
Chromosome 11 (human)
Genomic location for DPP3
Genomic location for DPP3
Band11q13.2Start66,480,013bp[1]
End66,509,657bp[1]
Gene location (Mouse)
Chromosome 19 (mouse)
Chr.Chromosome 19 (mouse)[2]
Chromosome 19 (mouse)
Genomic location for DPP3
Genomic location for DPP3
Band19|19 AStart4,957,257bp[2]
End4,978,315bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • mucosa of transverse colon

  • oocyte

  • rectum

  • islet of Langerhans

  • secondary oocyte

  • granulocyte

  • mucosa of pharynx

  • mucosa of esophagus

  • stromal cell of endometrium

  • right adrenal gland
Top expressed in
  • yolk sac

  • lip

  • primitive streak

  • epiblast

  • esophagus

  • neural tube

  • lacrimal gland

  • right kidney

  • embryo

  • ventricular zone
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo /QuickGO
Orthologs
SpeciesHumanMouse
Entrez

10072

75221

Ensembl

ENSG00000254986

ENSMUSG00000063904

UniProt

Q9NY33

Q99KK7

RefSeq (mRNA)

NM_130443
NM_001256670
NM_005700

NM_133803
NM_001360711

RefSeq (protein)

NP_001243599
NP_005691
NP_569710

NP_598564
NP_001347640

Location (UCSC)Chr 11: 66.48 – 66.51 MbChr 19: 4.96 – 4.98 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Dipeptidyl-peptidase 3 is anenzyme that in humans is encoded by theDPP3gene.[5][6]

This gene encodes a protein that is a member of the S9B family in clan SC of theserine proteases. Thiscytoplasmic protein binds a single zinc ion with its zinc-binding motif (HELLGH) and has post-prolinedipeptidyl aminopeptidase activity, cleaving Xaa-Pro dipeptides from theN-termini of proteins. Increased activity of this protein is associated withendometrial andovarian cancers. Alternate transcriptional splice variants have been characterized.[7]

Dipeptidyl-peptidase 3 has been found to act as a myocardial depressant factor.Procizumab, a specific antibody for dipeptidyl-peptidase 3, was found to improve cardiac and renal function in a mouse model ofheart failure.[8] In human studies, higher levels of circulating DPP3 protein incardiogenic shock patients indicated a more severe disease course, with a higher risk ofrefractory cardiogenic shock and death.[9][10]

References

[edit]
  1. ^abcGRCh38: Ensembl release 89: ENSG00000254986Ensembl, May 2017
  2. ^abcGRCm38: Ensembl release 89: ENSMUSG00000063904Ensembl, 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. ^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.S2CID 202603.
  6. ^"DPP3 dipeptidyl peptidase 3 [Homo sapiens (human)] - Gene - NCBI".www.ncbi.nlm.nih.gov. Retrieved2019-05-16.
  7. ^"DPP3 dipeptidyl peptidase 3 [Homo sapiens (human)] - Gene - NCBI".www.ncbi.nlm.nih.gov. Retrieved2019-05-16.
  8. ^Deniau, Benjamin; Rehfeld, Linda; Santos, Karine; Dienelt, Anke; Azibani, Feriel; Sadoune, Malha; Kounde, Paul R.; Samuel, Jane L.; Tolpannen, Heli; Lassus, Johan; Harjola, Veli-Pekka; Vodovar, Nicolas; Bergmann, Andreas; Hartmann, Oliver; Mebazaa, Alexandre (February 2020)."Circulating dipeptidyl peptidase 3 is a myocardial depressant factor: dipeptidyl peptidase 3 inhibition rapidly and sustainably improves haemodynamics".European Journal of Heart Failure.22 (2):290–299.doi:10.1002/ejhf.1601.ISSN 1388-9842.PMID 31472040.
  9. ^Harjola, Veli-Pekka; Lassus, Johan; Sionis, Alessandro; Køber, Lars; Tarvasmäki, Tuukka; Spinar, Jindrich; Parissis, John; Banaszewski, Marek; Silva-Cardoso, Jose; Carubelli, Valentina; Di Somma, Salvatore; Tolppanen, Heli; Zeymer, Uwe; Thiele, Holger; Nieminen, Markku S (May 2015)."Clinical picture and risk prediction of short-term mortality in cardiogenic shock".European Journal of Heart Failure.17 (5):501–509.doi:10.1002/ejhf.260.hdl:11573/910722.ISSN 1388-9842.PMID 25820680.
  10. ^Takagi, Koji; Blet, Alice; Levy, Bruno; Deniau, Benjamin; Azibani, Feriel; Feliot, Elodie; Bergmann, Andreas; Santos, Karine; Hartmann, Oliver; Gayat, Etienne; Mebazaa, Alexandre; Kimmoun, Antoine (February 2020)."Circulating dipeptidyl peptidase 3 and alteration in haemodynamics in cardiogenic shock: results from the OptimaCC trial".European Journal of Heart Failure.22 (2):279–286.doi:10.1002/ejhf.1600.ISSN 1388-9842.PMID 31472039.

Further reading

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External links

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