DPP5_TRIRU
ID DPP5_TRIRU Reviewed; 726 AA.
AC Q9UW98; Q6E7G5;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 84.
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 r 4;
DE Flags: Precursor;
GN Name=DPPV;
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 [MRNA].
RX PubMed=9792655; DOI=10.1074/jbc.273.45.29489;
RA Woodfolk J.A., Wheatley L.M., Piyasena R.V., Benjamin D.C.,
RA Platts-Mills T.A.E.;
RT "Trichophyton antigens associated with IgE antibodies and delayed type
RT hypersensitivity. Sequence homology to two families of serine
RT proteinases.";
RL J. Biol. Chem. 273:29489-29496(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 14001;
RX PubMed=15243098; DOI=10.1128/jcm.42.7.3298-3299.2004;
RA Gao J., Takashima A.;
RT "Cloning and characterization of Trichophyton rubrum genes encoding actin,
RT Tri r2, and Tri r4.";
RL J. Clin. Microbiol. 42:3298-3299(2004).
RN [3]
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).
RN [4]
RP INDUCTION.
RX PubMed=19098130; DOI=10.1128/ec.00208-08;
RA Zaugg C., Monod M., Weber J., Harshman K., Pradervand S., Thomas J.,
RA Bueno M., Giddey K., Staib P.;
RT "Gene expression profiling in the human pathogenic dermatophyte
RT Trichophyton rubrum during growth on proteins.";
RL Eukaryot. Cell 8:241-250(2009).
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:15632434}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15632434}.
CC -!- INDUCTION: Expression is strongly increased during growth on protein-
CC rich medium containing keratin. {ECO:0000269|PubMed:19098130}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE and
CC associated with delayed type hypersensitivity.
CC -!- SIMILARITY: Belongs to the peptidase S9C family. {ECO:0000305}.
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DR EMBL; AF082514; AAD52012.1; -; mRNA.
DR EMBL; AY525331; AAS19461.1; -; Genomic_DNA.
DR EMBL; AF407232; AAN03632.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9UW98; -.
DR SMR; Q9UW98; -.
DR Allergome; 3506; Tri r 4.0101.
DR Allergome; 653; Tri r 4.
DR ESTHER; triru-DPPV; Prolyl_oligopeptidase_S9.
DR MEROPS; S09.012; -.
DR PRIDE; Q9UW98; -.
DR VEuPathDB; FungiDB:TERG_02001; -.
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; 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; 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_0000027225"
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 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; 80121 MW; 83609D55F06783A4 CRC64;
MAAAKWLIAS LAFASSGLAF TPEDFISAPR RGEAIPDPKG ELAVFHVSKY NFDKKDRPSG
WNLLNLKNGD INVLTTDSDV SEITWLGDGT KVVYINGTDS VKGGVGIWIS DAKNFGNAYK
AGSVNGAFSG LKLAKSGDKI NFVGYGQSTT KGDLYNEAAA KEAVSSARIY DSLFVRHWDT
YVGTQFNAVF SGTLTKSGDK YSFDGKLKNL VQPVKYAESP YPPFGGSGDY DLSSDGKTVA
FMSKAPELPK ANLTTSYIFL VPHDGSRVAE PINKRNGPRT PQGIEGASSS PVFSPDGKRI
AYLQMAAKNY ESDRRVIHIA EVGTNKPVQR IASNWDRSPE AVKWSSDGRT LYVTAEDHAT
GKLFTLPADA RDNHKPAVVK HDGSVSSFYF IGSSKSVLIS GNSLWSNALY QVATPDRPNR
KLFYANEHDP ELKGLGPNDI EPLWVDGART KIHSWIVKPT GFDKNKVYPL AFLIHGGPQG
SWGDNWSTRW NPRVWADQGY VVVAPNPTGS TGFGQKLTDD ITNDWGGAPY KDLVKIWEHV
HDHIKYIDTD NGIAAGASFG GFMVNWIQGQ DLGRKFKALV SHDGTFVGSS KIGTDELFFI
EHDFNGTFFE ARQNYDRWDC SKPELVAKWS TPQLVVHNDF DFRLSVAEGV GLFNVLQEKG
VPSRFLNFPD ETHWVTKPEN SLVWHQQVLG WVNKWSGINK SNPKSIKLSD CPIEVVDHEA
HSYFDY
