ID   DPP4_ARTOT              Reviewed;         775 AA.
AC   A0S5V9;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 45.
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   Arthroderma otae (Microsporum canis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX   NCBI_TaxID=63405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=17681006; DOI=10.1111/j.1574-6968.2007.00870.x;
RA   Vermout S., Tabart J., Baldo A., Monod M., Losson B., Mignon B.;
RT   "RNA silencing in the dermatophyte Microsporum canis.";
RL   FEMS Microbiol. Lett. 275:38-45(2007).
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:17681006}.
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S9B family. {ECO:0000305}.
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DR   EMBL; DQ286524; ABB89928.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0S5V9; -.
DR   SMR; A0S5V9; -.
DR   ESTHER; artot-dpp4; DPP4N_Peptidase_S9.
DR   MEROPS; S09.008; -.
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; PS00708; PRO_ENDOPEP_SER; 1.
PE   3: Inferred from homology;
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_5000171326"
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        219
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        731
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   775 AA;  87917 MW;  311C8FA3E063EA23 CRC64;
     MKFLSLLLLV GVAQAIVPPR EPRPPTGGGK KLLTYKECVP RATLAPRSTS LAWINSDEDG
     QYISQSDDGA LILQNIVTNT NKTLVAADKV PKGFYDYWIK PDLTAVLWAT NYTKQYRHSY
     FANYFILDIE KGSLTPLAED QSGDIQYAQW NPVDNSIAYV RGNDLYVWNS GKTKRITENG
     GPDTFNGVPD WVYEEEIFGD RFALWFSPDG EYLAYLRFNE TGVPTYTVPY YKNKQKIAPA
     YPRELEIRYP KVSAKNPTVQ FHLLNLASSE ETSIPVTAFP EDDLIIGEVA WLSSGHDSVA
     FRAFNRVQDT EKIVNVKVGS KESKVIRERD GTDGWIDNLL SMSYIGKVNG KEYYVDISDA
     SGWAHLYLYP VDGGKEIALT KGEWEVTAIL KVDTKSKLIY FTSTKFHSTT RHVYSVSYDT
     KVMTPLVNDR EAAYYSASFS AKGGYYILSY QGPNVPYQEL YSVKDKKKPI KTITSNDALI
     EKLKDYKLPK ITFFEIKLPS GESLNVMQRL PPNFNPFKKY PVLFTPYGGP GAQEVSQAWK
     ALDFKAYITS DPELEYVTWT VDNRGTGFKG RKFRSTVTKR LGFLEPQDQV FAAKEILKNR
     WADKDHVGMW GWSYGGFLTA KTMETDSGVF TFGMSTAPVS DFRLYDSMYT ERYMKTVELN
     ADGYSETAVH KTDGFKNLKG HYLIQHGTGD DNVHFQNSAV LSNTLMNGGV TPDRLTTQWF
     TDSDHGVRYD NDSTFQYKQL TKMVYDQKQP RPQTTPLHQW SKRVLAALFG EEAEE