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Protein

Probable dipeptidyl peptidase 4

Gene

dpp4

Organism
Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Extracellular dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. Contributes to pathogenicity.1 Publication

Catalytic activityi

Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline.

Kineticsi

  1. KM=0.38 mM for Gly-Pro pNA and Ala-Pro pNA1 Publication
  2. KM=0.15 mM for Arg-Pro pNA1 Publication

pH dependencei

Optimum pH is 6.7 to 7.0.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei613 – 6131Charge relay systemBy similarity
Active sitei690 – 6901Charge relay systemBy similarity
Active sitei725 – 7251Charge relay systemBy similarity

GO - Molecular functioni

  1. aminopeptidase activity Source: UniProtKB-KW
  2. serine-type peptidase activity Source: UniProtKB-KW

GO - Biological processi

  1. pathogenesis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease, Serine protease

Keywords - Biological processi

Virulence

Names & Taxonomyi

Protein namesi
Recommended name:
Probable dipeptidyl peptidase 4 (EC:3.4.14.5)
Alternative name(s):
Dipeptidyl peptidase IV
Short name:
DPP IV
Short name:
DppIV
Gene namesi
Name:dpp4
ORF Names:AFUB_066450
OrganismiNeosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
Taxonomic identifieri451804 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000001699 Componenti: Unassembled WGS sequence

Subcellular locationi

  1. Secreted 1 Publication

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
  2. membrane Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1414Sequence AnalysisAdd
BLAST
Chaini15 – 765751Probable dipeptidyl peptidase 4PRO_0000397810Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi35 – 351N-linked (GlcNAc...)Sequence Analysis
Glycosylationi78 – 781N-linked (GlcNAc...)Sequence Analysis
Glycosylationi101 – 1011N-linked (GlcNAc...)Sequence Analysis
Glycosylationi110 – 1101N-linked (GlcNAc...)Sequence Analysis
Glycosylationi169 – 1691N-linked (GlcNAc...)Sequence Analysis
Glycosylationi218 – 2181N-linked (GlcNAc...)Sequence Analysis
Glycosylationi465 – 4651N-linked (GlcNAc...)Sequence Analysis
Glycosylationi490 – 4901N-linked (GlcNAc...)Sequence Analysis
Glycosylationi665 – 6651N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi5085.CADAFUAP00007859.

Structurei

3D structure databases

ProteinModelPortaliB0Y6C5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S9B family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000189891.
OrthoDBiEOG72VHFG.
PhylomeDBiB0Y6C5.

Family and domain databases

Gene3Di2.140.10.30. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR001375. Peptidase_S9.
IPR002469. Peptidase_S9B.
[Graphical view]
PfamiPF00930. DPPIV_N. 1 hit.
PF00326. Peptidase_S9. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

B0Y6C5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKWSILLLVG CAAAIDVPRQ PYAPTGSGKK RLTFNETVVK RAISPSAISV
60 70 80 90 100
EWISTSEDGD YVYQDQDGSL KIQSIVTNHT QTLVPADKVP EDAYSYWIHP
110 120 130 140 150
NLSSVLWATN YTKQYRYSYF ADYFIQDVQS MKLRPLAPDQ SGDIQYAQWS
160 170 180 190 200
PTGDAIAFVR DNNVFVWTNA STSQITNDGG PDLFNGVPDW IYEEEILGDR
210 220 230 240 250
FALWFSPDGA YLAFLRFNET GVPTFTVPYY MDNEEIAPPY PRELELRYPK
260 270 280 290 300
VSQTNPTVEL NLLELRTGER TPVPIDAFDA KELIIGEVAW LTGKHDVVAV
310 320 330 340 350
KAFNRVQDRQ KVVAVDVASL RSKTISERDG TDGWLDNLLS MAYIGPIGES
360 370 380 390 400
KEEYYIDISD QSGWAHLWLF PVAGGEPIAL TKGEWEVTNI LSIDKPRQLV
410 420 430 440 450
YFLSTKHHST ERHLYSVSWK TKEITPLVDD TVPAVWSASF SSQGGYYILS
460 470 480 490 500
YRGPDVPYQD LYAINSTAPL RTITSNAAVL NALKEYTLPN ITYFELALPS
510 520 530 540 550
GETLNVMQRL PVKFSPKKKY PVLFTPYGGP GAQEVSKAWQ ALDFKAYIAS
560 570 580 590 600
DPELEYITWT VDNRGTGYKG RAFRCQVASR LGELEAADQV FAAQQAAKLP
610 620 630 640 650
YVDAQHIAIW GWSYGGYLTG KVIETDSGAF SLGVQTAPVS DWRFYDSMYT
660 670 680 690 700
ERYMKTLESN AAGYNASAIR KVAGYKNVRG GVLIQHGTGD DNVHFQNAAA
710 720 730 740 750
LVDTLVGAGV TPEKLQVQWF TDSDHGIRYH GGNVFLYRQL SKRLYEEKKR
760
KEKGEAHQWS KKSVL
Length:765
Mass (Da):85,876
Last modified:April 8, 2008 - v1
Checksum:i544F27B6134F9B1B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti117 – 1171Y → H in AAC34310 (PubMed:9234752).Curated
Sequence conflicti161 – 1611D → G in AAC34310 (PubMed:9234752).Curated
Sequence conflicti538 – 5381A → P in AAC34310 (PubMed:9234752).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U87950 Genomic DNA. Translation: AAC34310.1.
DS499598 Genomic DNA. Translation: EDP50310.1.

Genome annotation databases

EnsemblFungiiCADAFUBT00006595; CADAFUBP00006467; CADAFUBG00006595.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U87950 Genomic DNA. Translation: AAC34310.1.
DS499598 Genomic DNA. Translation: EDP50310.1.

3D structure databases

ProteinModelPortaliB0Y6C5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5085.CADAFUAP00007859.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAFUBT00006595; CADAFUBP00006467; CADAFUBG00006595.

Phylogenomic databases

HOGENOMiHOG000189891.
OrthoDBiEOG72VHFG.
PhylomeDBiB0Y6C5.

Family and domain databases

Gene3Di2.140.10.30. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR001375. Peptidase_S9.
IPR002469. Peptidase_S9B.
[Graphical view]
PfamiPF00930. DPPIV_N. 1 hit.
PF00326. Peptidase_S9. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Dipeptidyl-peptidase IV secreted by Aspergillus fumigatus, a fungus pathogenic to humans."
    Beauvais A., Monod M., Wyniger J., Debeaupuis J.P., Grouzmann E., Brakch N., Svab J., Hovanessian A.G., Latge J.P.
    Infect. Immun. 65:3042-3047(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CEA10 / CBS 144.89 / FGSC A1163.

Entry informationi

Entry nameiDPP4_ASPFC
AccessioniPrimary (citable) accession number: B0Y6C5
Secondary accession number(s): O14425
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: April 8, 2008
Last modified: March 4, 2015
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.