ID   DPP5_TRISH              Reviewed;         726 AA.
AC   Q8J1L4;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   22-FEB-2023, entry version 63.
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   AltName: Allergen=Tri s 4;
DE   Flags: Precursor;
GN   Name=DPPV;
OS   Trichophyton schoenleinii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=34386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=VKPGF 235/25;
RA   Probst S., Polyakov I., Ivanova L., Graeser Y.;
RT   "Development of DNA markers to explore the genetic relatedness of strains
RT   of the two dermatophyte species causing Favus of human and mouse.";
RL   Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- ALLERGEN: Causes an allergic reaction in human.
CC   -!- SIMILARITY: Belongs to the peptidase S9C family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ430626; CAD23374.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8J1L4; -.
DR   SMR; Q8J1L4; -.
DR   ESTHER; artbe-DPP5; Prolyl_oligopeptidase_S9.
DR   MEROPS; S09.012; -.
DR   GlyCosmos; Q8J1L4; 5 sites, No reported glycans.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR011659; PD40.
DR   InterPro; IPR001375; Peptidase_S9.
DR   PANTHER; PTHR42776:SF11; DIPEPTIDYL-PEPTIDASE 5-RELATED; 1.
DR   PANTHER; PTHR42776; SERINE PEPTIDASE S9 FAMILY MEMBER; 1.
DR   Pfam; PF07676; PD40; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF69322; Tricorn protease domain 2; 1.
PE   1: Evidence at protein level;
KW   Allergen; Glycoprotein; Hydrolase; Protease; Secreted; Serine protease;
KW   Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..726
FT                   /note="Dipeptidyl-peptidase 5"
FT                   /id="PRO_0000027226"
FT   REGION          269..291
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        605
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        638
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;  79997 MW;  1DA505AB4F0AB133 CRC64;
     MAAAKWLIAS LAFASSGLAF TPEDFISAPR RGEAIPDPKG ELAVFHVSKY NFDKKDRPSG
     WNLLNLKNGD ISVLTTDSDV SEITWLGDGT KVVYVNGTDS VEGGVGIWIS DAKNFGNAYK
     AGSVNGAFSG LKLAKAGDKI NFVGYGQSTT KGDLYNEAAA KEAVSSARIY DGLFVRHWDT
     YVGTQFNAVF SGSLTKNGDK YSFDGKLKNL VQPVKYAESP YPPFGGSGDY DLSSDGKTVA
     FMSKAPELPK ANLTTSYIFL VPHDGSRVAE PINKRNGPRT PQGIEGASSS PVFSPDGKRI
     AYLQMATKNY ESDRRVIHIA EVGSNKPVQR IASSWDRSPE AVKWSSDGRT LYVTAEDHAT
     GKLFTLPADA RDNHKPSVVK HDGSVSSFYF IGSSKSVLIS GNSLWSNALY QVATPGRPNR
     KLFYANEHDP ELKGLGPKDI EPLWVDGART KIHSWIVKPT GFDKNKVYPL AFLIHGGPQG
     SWGDSWSTRW NPRVWADQGY VVVAPNPTGS TGFGQKLTDD ITNDWGGAPY KDLVKIWEHV
     RDHIKYIDTD NGIAAGASFG GFMVNWIQGQ DLGRKFKALV SHDGTFVGSS KIGTDELFFI
     EHDFNGTFFE ARQNYDRWDC SKPELVAKWS TPQLVIHNDS DFRLSVAEGV GLFNVLQEKG
     IPSRFLNFPD ETHWVTKPEN SLVWHQQVLG WINKWSGINK SNPKSIKLSD CPIEVIDHEA
     HSYFDY
//