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B6V868 (DPP4_TRITO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 18. 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:
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
OrganismTrichophyton tonsurans (Scalp ringworm fungus)
Taxonomic identifier34387 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesArthrodermataceaemitosporic ArthrodermataceaeTrichophyton

Protein attributes

Sequence length775 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
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 – 1515 Potential
Chain16 – 775760Dipeptidyl peptidase 4
PRO_0000384090

Sites

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

Amino acid modifications

Glycosylation811N-linked (GlcNAc...) Potential
Glycosylation1111N-linked (GlcNAc...) Potential
Glycosylation1701N-linked (GlcNAc...) Potential
Glycosylation2191N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
B6V868 [UniParc].

Last modified December 16, 2008. Version 1.
Checksum: 74E1364F7B960473

FASTA77588,009
        10         20         30         40         50         60 
MKLLSLLMLA GIAQAIVPPR EPRPPTGGGN KLLTYKECVP RATISPRSTS LAWINSDEDG 

        70         80         90        100        110        120 
QYISQSDDGA LILQNIVTNT NKTLVAADKV PKGYYDYWFK PDLSAVLWAT NYTKQYRHSY 

       130        140        150        160        170        180 
FANYFILDIE KGSLTPLAQD QAGDIQYAQW SPVDNSIAYV RGNDLYIWNN GTTKRITENG 

       190        200        210        220        230        240 
GPDIFNGVPD WVYEEEIFGD RFALWFSPDG EYLAYLRFNE TGVPTYTIPY YKNKQKIAPA 

       250        260        270        280        290        300 
YPRELEIRYP KVSAKNPTVQ FHLLNIASSQ ESTIPVTAFP ENDLVIGEVA WLSSGHDSVA 

       310        320        330        340        350        360 
YRAFNRVQDR EKIVSIKVES KESKVIRERD GTDGWIDNLL SMSYIGDVNG KEYYVDISDA 

       370        380        390        400        410        420 
SGWAHIYLYP VDGGKEIALT KGEWEVVAIL KVDTKKKLIY FTSTKYHSTT RHVYSVSYDT 

       430        440        450        460        470        480 
NVMTPLVNDK EAAYYTASFS AKGGYYILSY QGPNVPYQEL YSTKDSKKPL KTITSNDALL 

       490        500        510        520        530        540 
EKLKEYKLPM VSFFEIKLPS GETLNVKQRL PPNFNPHKKY PVLFTPYGGP GAQEVSQAWN 

       550        560        570        580        590        600 
SLDFKSYITS DPELEYVTWT VDNRGTGYKG RKFRSAVAKR LGFLEAQDQV FAAKELLKNR 

       610        620        630        640        650        660 
WADKDHIGIW GWSYGGFLTA KTLETDSGVF TFGISTAPVS DFRLYDSMYT ERYMKTVELN 

       670        680        690        700        710        720 
ADGYSETAVH KVDGFKNLKG HYLIQHGTGD DNVHFQNAAV LSNTLMNGGV TADKLTTQWF 

       730        740        750        760        770 
TDSDHGIRYD MDSTYQYKQL AKMVYDQKQR RPERPPMHQW SKRVLAALFG ERAEE 

« Hide

References

[1]"Comparing putative pathogenicity factors between Trichophyton tonsurans and Trichophyton equinum."
Preuett B.L., Abdel-Rahman S.M.
Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FJ267691 Genomic DNA. Translation: ACJ06659.1.

3D structure databases

ProteinModelPortalB6V868.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS09.008.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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_TRITO
AccessionPrimary (citable) accession number: B6V868
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: December 16, 2008
Last modified: April 16, 2014
This is version 18 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