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B0Y6C5 (DPP4_ASPFC) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable dipeptidyl peptidase 4

EC=3.4.14.5
Alternative name(s):
Dipeptidyl peptidase IV
Short name=DPP IV
Short name=DppIV
Gene names
Name:dpp4
ORF Names:AFUB_066450
OrganismNeosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus) [Complete proteome]
Taxonomic identifier451804 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length765 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1

Catalytic activity

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

Subcellular location

Secreted Ref.1.

Sequence similarities

Belongs to the peptidase S9B family.

Biophysicochemical properties

Kinetic parameters:

KM=0.38 mM for Gly-Pro pNA and Ala-Pro pNA Ref.1

KM=0.15 mM for Arg-Pro pNA

pH dependence:

Optimum pH is 6.7 to 7.0.

Ontologies

Keywords
   Biological processVirulence
   Cellular componentSecreted
   DomainSignal
   Molecular functionAminopeptidase
Hydrolase
Protease
Serine protease
   PTMGlycoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processpathogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Inferred from electronic annotation. Source: InterPro

   Molecular_functionaminopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

serine-type peptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1414 Potential
Chain15 – 765751Probable dipeptidyl peptidase 4
PRO_0000397810

Sites

Active site6131Charge relay system By similarity
Active site6901Charge relay system By similarity
Active site7251Charge relay system By similarity

Amino acid modifications

Glycosylation351N-linked (GlcNAc...) Potential
Glycosylation781N-linked (GlcNAc...) Potential
Glycosylation1011N-linked (GlcNAc...) Potential
Glycosylation1101N-linked (GlcNAc...) Potential
Glycosylation1691N-linked (GlcNAc...) Potential
Glycosylation2181N-linked (GlcNAc...) Potential
Glycosylation4651N-linked (GlcNAc...) Potential
Glycosylation4901N-linked (GlcNAc...) Potential
Glycosylation6651N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict1171Y → H in AAC34310. Ref.1
Sequence conflict1611D → G in AAC34310. Ref.1
Sequence conflict5381A → P in AAC34310. Ref.1

Sequences

Sequence LengthMass (Da)Tools
B0Y6C5 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 544F27B6134F9B1B

FASTA76585,876
        10         20         30         40         50         60 
MKWSILLLVG CAAAIDVPRQ PYAPTGSGKK RLTFNETVVK RAISPSAISV EWISTSEDGD 

        70         80         90        100        110        120 
YVYQDQDGSL KIQSIVTNHT QTLVPADKVP EDAYSYWIHP NLSSVLWATN YTKQYRYSYF 

       130        140        150        160        170        180 
ADYFIQDVQS MKLRPLAPDQ SGDIQYAQWS PTGDAIAFVR DNNVFVWTNA STSQITNDGG 

       190        200        210        220        230        240 
PDLFNGVPDW IYEEEILGDR FALWFSPDGA YLAFLRFNET GVPTFTVPYY MDNEEIAPPY 

       250        260        270        280        290        300 
PRELELRYPK VSQTNPTVEL NLLELRTGER TPVPIDAFDA KELIIGEVAW LTGKHDVVAV 

       310        320        330        340        350        360 
KAFNRVQDRQ KVVAVDVASL RSKTISERDG TDGWLDNLLS MAYIGPIGES KEEYYIDISD 

       370        380        390        400        410        420 
QSGWAHLWLF PVAGGEPIAL TKGEWEVTNI LSIDKPRQLV YFLSTKHHST ERHLYSVSWK 

       430        440        450        460        470        480 
TKEITPLVDD TVPAVWSASF SSQGGYYILS YRGPDVPYQD LYAINSTAPL RTITSNAAVL 

       490        500        510        520        530        540 
NALKEYTLPN ITYFELALPS GETLNVMQRL PVKFSPKKKY PVLFTPYGGP GAQEVSKAWQ 

       550        560        570        580        590        600 
ALDFKAYIAS DPELEYITWT VDNRGTGYKG RAFRCQVASR LGELEAADQV FAAQQAAKLP 

       610        620        630        640        650        660 
YVDAQHIAIW GWSYGGYLTG KVIETDSGAF SLGVQTAPVS DWRFYDSMYT ERYMKTLESN 

       670        680        690        700        710        720 
AAGYNASAIR KVAGYKNVRG GVLIQHGTGD DNVHFQNAAA LVDTLVGAGV TPEKLQVQWF 

       730        740        750        760 
TDSDHGIRYH GGNVFLYRQL SKRLYEEKKR KEKGEAHQWS KKSVL 

« Hide

References

« Hide 'large scale' references
[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]"Genomic islands in the pathogenic filamentous fungus Aspergillus fumigatus."
Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M. expand/collapse author list , Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J., Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C., White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., Wortman J.R., Jiang B., Denning D.W., Nierman W.C.
PLoS Genet. 4:E1000046-E1000046(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CEA10 / CBS 144.89 / FGSC A1163.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U87950 Genomic DNA. Translation: AAC34310.1.
DS499598 Genomic DNA. Translation: EDP50310.1.

3D structure databases

ProteinModelPortalB0Y6C5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5085.CADAFUAP00007859.

Protein family/group databases

MEROPSS09.008.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUBT00006595; CADAFUBP00006467; CADAFUBG00006595.

Phylogenomic databases

HOGENOMHOG000189891.
OrthoDBEOG72VHFG.
PhylomeDBB0Y6C5.

Family and domain databases

Gene3D2.140.10.30. 1 hit.
3.40.50.1820. 1 hit.
InterProIPR029058. AB_hydrolase.
IPR001375. Peptidase_S9.
IPR002469. Peptidase_S9B.
[Graphical view]
PfamPF00930. DPPIV_N. 1 hit.
PF00326. Peptidase_S9. 1 hit.
[Graphical view]
SUPFAMSSF53474. SSF53474. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDPP4_ASPFC
AccessionPrimary (citable) accession number: B0Y6C5
Secondary accession number(s): O14425
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: April 8, 2008
Last modified: June 11, 2014
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries