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B6V868

- DPP4_TRITO

UniProt

B6V868 - DPP4_TRITO

Protein

Dipeptidyl peptidase 4

Gene

DPP4

Organism
Trichophyton tonsurans (Scalp ringworm fungus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 21 (01 Oct 2014)
      Sequence version 1 (16 Dec 2008)
      Previous versions | rss
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    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.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.PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei613 – 6131Charge relay systemPROSITE-ProRule annotation
    Active sitei690 – 6901Charge relay systemPROSITE-ProRule annotation
    Active sitei725 – 7251Charge relay systemPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. pathogenesis Source: UniProtKB-KW

    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

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1515Sequence AnalysisAdd
    BLAST
    Chaini16 – 775760Dipeptidyl peptidase 4PRO_0000384090Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Glycoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliB6V868.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase S9B family.Curated

    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

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    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: October 1, 2014
    This is version 21 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