ID   DPP4_TRIRU              Reviewed;         775 AA.
AC   Q5J6J3;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Dipeptidyl peptidase 4;
DE            EC=3.4.14.5;
DE   AltName: Full=Dipeptidyl peptidase IV;
DE            Short=DPP IV;
DE            Short=DppIV;
DE   Flags: Precursor;
GN   Name=DPP4;
OS   Trichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=5551;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, FUNCTION, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=15632434; DOI=10.1099/mic.0.27484-0;
RA   Monod M., Lechenne B., Jousson O., Grand D., Zaugg C., Stoecklin R.,
RA   Grouzmann E.;
RT   "Aminopeptidases and dipeptidyl-peptidases secreted by the dermatophyte
RT   Trichophyton rubrum.";
RL   Microbiology 151:145-155(2005).
CC   -!- FUNCTION: Extracellular dipeptidyl-peptidase which removes N-terminal
CC       dipeptides sequentially from polypeptides having unsubstituted N-
CC       termini provided that the penultimate residue is proline. Contributes
CC       to pathogenicity. {ECO:0000269|PubMed:15632434}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a
CC         polypeptide, preferentially when Yaa is Pro, provided Zaa is neither
CC         Pro nor hydroxyproline.; EC=3.4.14.5; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10084};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.0-9.0. {ECO:0000269|PubMed:15632434};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15632434}.
CC   -!- SIMILARITY: Belongs to the peptidase S9B family. {ECO:0000305}.
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DR   EMBL; AY497021; AAS76665.1; -; Genomic_DNA.
DR   ESTHER; artbc-dpp4; DPP4N_Peptidase_S9.
DR   MEROPS; S09.008; -.
DR   VEuPathDB; FungiDB:TERG_05735; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002471; Pept_S9_AS.
DR   InterPro; IPR001375; Peptidase_S9.
DR   InterPro; IPR002469; Peptidase_S9B_N.
DR   Pfam; PF00930; DPPIV_N; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
DR   PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE   1: Evidence at protein level;
KW   Aminopeptidase; Glycoprotein; Hydrolase; Protease; Secreted;
KW   Serine protease; Signal; Virulence.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..775
FT                   /note="Dipeptidyl peptidase 4"
FT                   /id="PRO_0000384089"
FT   ACT_SITE        613
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT   ACT_SITE        690
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT   ACT_SITE        725
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT   CARBOHYD        81
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        111
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        154
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        219
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   775 AA;  88021 MW;  157774F128C6BFDB CRC64;
     MKLLSLLMLA GIAQAIVPPR EPRSPTGGGN KLLTYKECVP RATISPRSTS LAWINSEEDG
     RYISQSDDGA LILQNIVTNT NKTLVAADKV PKGYYDYWFK PDLSAVLWAT NYTKQYRHSY
     FANYFILDIK KGSLTPLAQD QAGDIQYAQW SPMNNSIAYV RXNDLYIWNN GKTKRITENG
     GPDIFNGVPD WVYEEEIFGD RFALWFSPDG EYLAYLRFNE TGVPTYTIPY YKNKQKIAPA
     YPRELEIRYP KVSAKNPTVQ FHLLNIASSQ ETTIPVTAFP ENDLVIGEVA WLSSGHDSVA
     YRAFNRVQDR EKIVSVKVES KESKVIRERD GTDGWIDNLL SMSYIGNVNG KEYYVDISDA
     SGWAHIYLYP VDGGKEIALT KGEWEVVAIL KVDTKKKLIY FTSTKYHSTT RHVYSVSYDT
     KVMTPLVNDK EAAYYTASFS AKGGYYILSY QGPNVPYQEL YSTKDSKKPL KTITSNDALL
     EKLKEYKLPK VSFFEIKLPS GETLNVKQRL PPNFNPHKKY PVLFTPYGGP GAQEVSQAWN
     SLDFKSYITS DPELEYVTWT VDNRGTGYKG RKFRSAVAKR LGFLEAQDQV FAAKEVLKNR
     WADKDHIGIW GXSYGGFLTA KTLETDSGVF TFGISTAPVS DFRLYDSMYT ERYMKTVELN
     ADGYSETAVH KVDGFKNLKG HYLIQHGTGD DNVHFQNAAV LSNTLMNGGV TADKLTTQWF
     TDSDHGIRYD MDSTYQYKQL SKMVYDQKQR RPESPPMHQW SKRVLAALFG ERAEE