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Q4WPH9 (DPP4_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 62. 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:AFUA_4G09320
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length765 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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 By similarity.

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 By similarity.

Sequence similarities

Belongs to the peptidase S9B family.

Ontologies

Keywords
   Biological processVirulence
   Cellular componentSecreted
   DomainSignal
   Molecular functionAminopeptidase
Hydrolase
Protease
Serine protease
   PTMGlycoprotein
   Technical termComplete proteome
Reference 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

peptidase activity

Inferred from direct assay PubMed 9234752. Source: ASPGD

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_0000397812

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

Sequences

Sequence LengthMass (Da)Tools
Q4WPH9 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: DA7BF150DB0D686E

FASTA76585,864
        10         20         30         40         50         60 
MKWSILLLVG CAAAIDVPRQ PYAPTGSGKK RLTFNETVVK RAISPSAISV EWISTSEDGD 

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

       130        140        150        160        170        180 
ADYFIQDVQS MKLRPLAPDQ SGDIQYAQWT 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

[1]"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. expand/collapse author list , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAHF01000005 Genomic DNA. Translation: EAL89855.1.
RefSeqXP_751893.1. XM_746800.1.

3D structure databases

ProteinModelPortalQ4WPH9.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS09.008.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00007859; CADAFUAP00007859; CADAFUAG00007859.
GeneID3509739.
KEGGafm:AFUA_4G09320.

Phylogenomic databases

eggNOGCOG1506.
HOGENOMHOG000189891.
KOK01278.
OMAWAVNYTK.
OrthoDBEOG72VHFG.

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_ASPFU
AccessionPrimary (citable) accession number: Q4WPH9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: July 5, 2005
Last modified: June 11, 2014
This is version 62 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