ID   DPP5_ARTOT              Reviewed;         726 AA.
AC   A0S5W0;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Dipeptidyl-peptidase 5;
DE            EC=3.4.14.-;
DE   AltName: Full=Dipeptidyl-peptidase V;
DE            Short=DPP V;
DE            Short=DppV;
DE   Flags: Precursor;
GN   Name=DPP5;
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. Contributes to pathogenicity (By similarity). {ECO:0000250,
CC       ECO:0000269|PubMed:17681006}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S9C family. {ECO:0000305}.
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DR   EMBL; DQ286525; ABB89929.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0S5W0; -.
DR   SMR; A0S5W0; -.
DR   ESTHER; artot-dpp5; Prolyl_oligopeptidase_S9.
DR   MEROPS; S09.012; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.120.10.30; -; 1.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001375; Peptidase_S9.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Glycoprotein; Hydrolase; Protease; Secreted;
KW   Serine protease; Signal; Virulence.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..726
FT                   /note="Dipeptidyl-peptidase 5"
FT                   /id="PRO_5000171327"
FT   REGION          268..292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        558
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        641
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        673
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        96
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        252
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        485
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        605
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        699
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   726 AA;  79992 MW;  286D98447002C89B CRC64;
     MAPAKWLIAS LAFASTGLAF TPEDFISAPR RGEAIPDPKG QFAVFPVSKY NFDTKDRPSG
     WNLLNLKTGD ISVLTTDADV SEITWLGEGT NLLYVNGTDS VKGGVGIWIS DAKNFGNAYK
     AGSIPGAFQG FKLAKSGDKI NFVGYGQSTT KGDLYNEAAI EKPVSSARIY DSLFVRHWDA
     YVGTQFNAVF SGALTKNGNK YSFDGKLKNL VQPVKYAESP YPPFGGSGDY DLSPDGKTVA
     FMSKAPELPK ANLTTSYIFT VPHDGSKVAE PINKRNGPRT PHGIEGASSS PVFSPDSKRI
     AYLQMATKNY ESDRRVIHIA EVGSNKPAQR IASNWDRSPE SIKWSSDGRT LYVTAEEHAT
     GKLFTLPSDA RDNHMPSAVK HDGSVSAFSF VGSSKSVLIT GNSLWSNALY QIATPGRPNR
     KLFYANEHDP QLKGLGPNDI EPLWVDGART KIHSWIVKPT GFDKNKVYPL AFLIHGGPQG
     SWGDNWSTRW NPRVWADQGY VVIAPNPTGS TGFGQKLTDD ITNDWGGAPY KDLFKIWEHV
     RDNLKYVDTD NGIAAGASFG GFMINWIQGQ ELGRKFKALV SHDGTFVGSS KIGTDELFFI
     EHDFNGTFFE ARQNYDRWDC SKPEYVAKWS TPQLVVHSDY DFRLSVAEGV GLFNVLQEKG
     VPSRLLNFPD ESHCVTKPEN SLVWHQQVLG WINKFSGINK SNPKAIKLSD CKVEVIDHEA
     GSYFDY