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B6V868

- DPP4_TRITO

UniProt

B6V868 - DPP4_TRITO

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Protein
Dipeptidyl peptidase 4
Gene
DPP4
Organism
Trichophyton tonsurans (Scalp ringworm fungus)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

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 activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei613 – 6131Charge relay system By similarity
Active sitei690 – 6901Charge relay system By similarity
Active sitei725 – 7251Charge relay system By similarity

GO - Molecular functioni

  1. aminopeptidase activity Source: UniProtKB-KW
  2. serine-type endopeptidase activity Source: InterPro

GO - Biological processi

  1. pathogenesis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease, Serine protease

Keywords - Biological processi

Virulence

Protein family/group databases

MEROPSiS09.008.

Names & Taxonomyi

Protein namesi
Recommended name:
Dipeptidyl peptidase 4 (EC:3.4.14.5)
Alternative name(s):
Dipeptidyl peptidase IV
Short name:
DPP IV
Short name:
DppIV
Gene namesi
Name:DPP4
OrganismiTrichophyton tonsurans (Scalp ringworm fungus)
Taxonomic identifieri34387 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesArthrodermataceaemitosporic ArthrodermataceaeTrichophyton

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
  2. membrane Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1515 Reviewed prediction
Add
BLAST
Chaini16 – 775760Dipeptidyl peptidase 4
PRO_0000384090Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi81 – 811N-linked (GlcNAc...) Reviewed prediction
Glycosylationi111 – 1111N-linked (GlcNAc...) Reviewed prediction
Glycosylationi170 – 1701N-linked (GlcNAc...) Reviewed prediction
Glycosylationi219 – 2191N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliB6V868.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S9B family.

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.140.10.30. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002471. Pept_S9_AS.
IPR001375. Peptidase_S9.
IPR002469. Peptidase_S9B.
[Graphical view]
PfamiPF00930. DPPIV_N. 1 hit.
PF00326. Peptidase_S9. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00708. PRO_ENDOPEP_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

B6V868-1 [UniParc]FASTAAdd to Basket

« Hide

MKLLSLLMLA GIAQAIVPPR EPRPPTGGGN KLLTYKECVP RATISPRSTS    50
LAWINSDEDG QYISQSDDGA LILQNIVTNT NKTLVAADKV PKGYYDYWFK 100
PDLSAVLWAT NYTKQYRHSY FANYFILDIE KGSLTPLAQD QAGDIQYAQW 150
SPVDNSIAYV RGNDLYIWNN GTTKRITENG GPDIFNGVPD WVYEEEIFGD 200
RFALWFSPDG EYLAYLRFNE TGVPTYTIPY YKNKQKIAPA YPRELEIRYP 250
KVSAKNPTVQ FHLLNIASSQ ESTIPVTAFP ENDLVIGEVA WLSSGHDSVA 300
YRAFNRVQDR EKIVSIKVES KESKVIRERD GTDGWIDNLL SMSYIGDVNG 350
KEYYVDISDA SGWAHIYLYP VDGGKEIALT KGEWEVVAIL KVDTKKKLIY 400
FTSTKYHSTT RHVYSVSYDT NVMTPLVNDK EAAYYTASFS AKGGYYILSY 450
QGPNVPYQEL YSTKDSKKPL KTITSNDALL EKLKEYKLPM VSFFEIKLPS 500
GETLNVKQRL PPNFNPHKKY PVLFTPYGGP GAQEVSQAWN SLDFKSYITS 550
DPELEYVTWT VDNRGTGYKG RKFRSAVAKR LGFLEAQDQV FAAKELLKNR 600
WADKDHIGIW GWSYGGFLTA KTLETDSGVF TFGISTAPVS DFRLYDSMYT 650
ERYMKTVELN ADGYSETAVH KVDGFKNLKG HYLIQHGTGD DNVHFQNAAV 700
LSNTLMNGGV TADKLTTQWF TDSDHGIRYD MDSTYQYKQL AKMVYDQKQR 750
RPERPPMHQW SKRVLAALFG ERAEE 775
Length:775
Mass (Da):88,009
Last modified:December 16, 2008 - v1
Checksum:i74E1364F7B960473
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
FJ267691 Genomic DNA. Translation: ACJ06659.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
FJ267691 Genomic DNA. Translation: ACJ06659.1 .

3D structure databases

ProteinModelPortali B6V868.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi S09.008.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 2.140.10.30. 1 hit.
3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR002471. Pept_S9_AS.
IPR001375. Peptidase_S9.
IPR002469. Peptidase_S9B.
[Graphical view ]
Pfami PF00930. DPPIV_N. 1 hit.
PF00326. Peptidase_S9. 1 hit.
[Graphical view ]
SUPFAMi SSF53474. SSF53474. 1 hit.
PROSITEi PS00708. PRO_ENDOPEP_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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].

Entry informationi

Entry nameiDPP4_TRITO
AccessioniPrimary (citable) accession number: B6V868
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: December 16, 2008
Last modified: June 11, 2014
This is version 20 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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