DPP5_TRISH
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 03-AUG-2022, entry version 61.
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}.
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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 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; 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; IPR011659; PD40.
DR InterPro; IPR001375; Peptidase_S9.
DR Pfam; PF07676; PD40; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; SSF53474; 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
