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D4CZ59 (DPP4_TRIVH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 17. 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:TRV_00096
OrganismTrichophyton verrucosum (strain HKI 0517) [Complete proteome]
Taxonomic identifier663202 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesArthrodermataceaemitosporic ArthrodermataceaeTrichophyton

Protein attributes

Sequence length753 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
Gene Ontology (GO)
   Biological_processpathogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

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 endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 753735Probable dipeptidyl peptidase 4
PRO_0000397815

Sites

Active site6161Charge relay system By similarity
Active site6681Charge relay system By similarity
Active site7031Charge relay system By similarity

Amino acid modifications

Glycosylation841N-linked (GlcNAc...) Potential
Glycosylation1141N-linked (GlcNAc...) Potential
Glycosylation2221N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
D4CZ59 [UniParc].

Last modified May 18, 2010. Version 1.
Checksum: 02B1752AB9C6F26E

FASTA75385,635
        10         20         30         40         50         60 
MKTSQFLSLL LLAGIAQAIV PPREPRPPTG GGNKLLTYKE CVPRATISPR STSLAWINSD 

        70         80         90        100        110        120 
EDGQYISQSD DGALILQNIV TNTNKTLVAA DKVPKGYYDY WFKPDLSAVL WATNYTKQYR 

       130        140        150        160        170        180 
HSYFANYFIL DIEKGSLTPL AQDQAGDIQY AQWSPMDNSI AYVRGNDLYI WNNGKTKRIT 

       190        200        210        220        230        240 
ENGGPDIFNG VPDWVYEEEI FGDRFALWFS PDGEYLAYLR FNETGVPTYT IPYYKNKQKI 

       250        260        270        280        290        300 
APAYPRELEI RYPKVSAKNP TVQFHLLNIA SSQETTIPVT AFPENDLVIG EVAWLSSGHD 

       310        320        330        340        350        360 
SVAYRAFNRV QDREKIVSVK VESKESKVIR ERDGTDGWID NLLSMSYIGD VNGKEYYVDI 

       370        380        390        400        410        420 
SDASGWAHIY LYPVDGGKEI ALTTGEWEVV AILKVDTMKK LIYFTSTKYH STTRHVYSVS 

       430        440        450        460        470        480 
YDTKVMTPLV NDKEAAYYTA SFSAKGGYYI LSYQGPNVPY QELYSTKDSK KPLKTITSND 

       490        500        510        520        530        540 
ALLEKLKEYK LPKVSFFEIK LPSGETLNVK QRLPPNFNPH KKYPVLFTPY GGPGAQEVSQ 

       550        560        570        580        590        600 
AWNSLDFKSY ITSDPELEYV TWTVDNRGTG YKGRKFRSAV AKRLGFLEPQ DQVFAAKELL 

       610        620        630        640        650        660 
KNRWADKDHI GIWGWSYGGF LTAKTLETDS GVFTFGISTA PVSDFRLYDS MYTERYMKTV 

       670        680        690        700        710        720 
ELNADGCDDN VHFQNAAVLS NTLMNGGVTA DKLTTQWFTD SDHGIRYDMD STYQYKQLAK 

       730        740        750 
MVYDQKQRRP ERPPMHQWSK RVLAALFGER AEE 

« Hide

References

[1]"Comparative and functional genomics provide insights into the pathogenicity of dermatophytic fungi."
Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S., Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M., Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O., Schroeckh V. expand/collapse author list , Hertweck C., Hube B., White T.C., Platzer M., Guthke R., Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.
Genome Biol. 12:R7.1-R7.16(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HKI 0517.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
ACYE01000004 Genomic DNA. Translation: EFE45114.1.
RefSeqXP_003025725.1. XM_003025679.1.

3D structure databases

ProteinModelPortalD4CZ59.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID9581968.
KEGGtve:TRV_00096.

Phylogenomic databases

KOK01278.
OrthoDBEOG72VHFG.

Family and domain databases

Gene3D2.140.10.30. 1 hit.
InterProIPR002471. Pept_S9_AS.
IPR001375. Peptidase_S9.
IPR002469. Peptidase_S9B.
[Graphical view]
PfamPF00930. DPPIV_N. 1 hit.
PF00326. Peptidase_S9. 1 hit.
[Graphical view]
PROSITEPS00708. PRO_ENDOPEP_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDPP4_TRIVH
AccessionPrimary (citable) accession number: D4CZ59
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: May 18, 2010
Last modified: April 16, 2014
This is version 17 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