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A0S5V9 (DPP4_ARTOT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 24. 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
OrganismArthroderma otae (Microsporum canis)
Taxonomic identifier63405 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesArthrodermataceaeArthroderma

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. 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 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

   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_5000171326

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
Glycosylation2191N-linked (GlcNAc...) Potential
Glycosylation7311N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
A0S5V9 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: 311C8FA3E063EA23

FASTA77587,917
        10         20         30         40         50         60 
MKFLSLLLLV GVAQAIVPPR EPRPPTGGGK KLLTYKECVP RATLAPRSTS LAWINSDEDG 

        70         80         90        100        110        120 
QYISQSDDGA LILQNIVTNT NKTLVAADKV PKGFYDYWIK PDLTAVLWAT NYTKQYRHSY 

       130        140        150        160        170        180 
FANYFILDIE KGSLTPLAED QSGDIQYAQW NPVDNSIAYV RGNDLYVWNS GKTKRITENG 

       190        200        210        220        230        240 
GPDTFNGVPD WVYEEEIFGD RFALWFSPDG EYLAYLRFNE TGVPTYTVPY YKNKQKIAPA 

       250        260        270        280        290        300 
YPRELEIRYP KVSAKNPTVQ FHLLNLASSE ETSIPVTAFP EDDLIIGEVA WLSSGHDSVA 

       310        320        330        340        350        360 
FRAFNRVQDT EKIVNVKVGS KESKVIRERD GTDGWIDNLL SMSYIGKVNG KEYYVDISDA 

       370        380        390        400        410        420 
SGWAHLYLYP VDGGKEIALT KGEWEVTAIL KVDTKSKLIY FTSTKFHSTT RHVYSVSYDT 

       430        440        450        460        470        480 
KVMTPLVNDR EAAYYSASFS AKGGYYILSY QGPNVPYQEL YSVKDKKKPI KTITSNDALI 

       490        500        510        520        530        540 
EKLKDYKLPK ITFFEIKLPS GESLNVMQRL PPNFNPFKKY PVLFTPYGGP GAQEVSQAWK 

       550        560        570        580        590        600 
ALDFKAYITS DPELEYVTWT VDNRGTGFKG RKFRSTVTKR LGFLEPQDQV FAAKEILKNR 

       610        620        630        640        650        660 
WADKDHVGMW GWSYGGFLTA KTMETDSGVF TFGMSTAPVS DFRLYDSMYT ERYMKTVELN 

       670        680        690        700        710        720 
ADGYSETAVH KTDGFKNLKG HYLIQHGTGD DNVHFQNSAV LSNTLMNGGV TPDRLTTQWF 

       730        740        750        760        770 
TDSDHGVRYD NDSTFQYKQL TKMVYDQKQP RPQTTPLHQW SKRVLAALFG EEAEE 

« Hide

References

[1]"RNA silencing in the dermatophyte Microsporum canis."
Vermout S., Tabart J., Baldo A., Monod M., Losson B., Mignon B.
FEMS Microbiol. Lett. 275:38-45(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ286524 Genomic DNA. Translation: ABB89928.1.

3D structure databases

ProteinModelPortalA0S5V9.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS09.008.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.140.10.30. 1 hit.
3.40.50.1820. 1 hit.
InterProIPR029058. AB_hydrolase.
IPR002471. Pept_S9_AS.
IPR001375. Peptidase_S9.
IPR002469. Peptidase_S9B.
[Graphical view]
PfamPF00930. DPPIV_N. 1 hit.
PF00326. Peptidase_S9. 1 hit.
[Graphical view]
SUPFAMSSF53474. SSF53474. 1 hit.
PROSITEPS00708. PRO_ENDOPEP_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDPP4_ARTOT
AccessionPrimary (citable) accession number: A0S5V9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: January 9, 2007
Last modified: June 11, 2014
This is version 24 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