DPP5_ASPFC
ID DPP5_ASPFC Reviewed; 721 AA.
AC B0XRV0; O13479; Q4X1R6;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 57.
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 ORFNames=AFUB_024920;
OS Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 19-42; 435-448 AND
RP 593-603, AND CHARACTERIZATION.
RX PubMed=9045640; DOI=10.1074/jbc.272.10.6238;
RA Beauvais A., Monod M., Debeaupuis J.-P., Diaquin M., Kobayashi H.,
RA Latge J.-P.;
RT "Biochemical and antigenic characterization of a new dipeptidyl-peptidase
RT isolated from Aspergillus fumigatus.";
RL J. Biol. Chem. 272:6238-6244(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- FUNCTION: May be involved in metabolism of dipeptides or may affect
CC host defense mechanisms. Has a substrate specificity limited to the
CC hydrolysis of X-Ala, His-Ser, and Ser-Tyr dipeptides at a neutral pH
CC optimum.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.5.;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed in mycelia and conidia.
CC -!- PTM: N-glycosylated.
CC -!- SIMILARITY: Belongs to the peptidase S9C family. {ECO:0000305}.
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DR EMBL; L48074; AAB67282.1; -; Genomic_DNA.
DR EMBL; DS499595; EDP54436.1; -; Genomic_DNA.
DR AlphaFoldDB; B0XRV0; -.
DR SMR; B0XRV0; -.
DR Allergome; 8984; Asp f DPPV.
DR ESTHER; aspfc-dpp5; Prolyl_oligopeptidase_S9.
DR MEROPS; S09.012; -.
DR EnsemblFungi; EDP54436; EDP54436; AFUB_024920.
DR VEuPathDB; FungiDB:AFUB_024920; -.
DR HOGENOM; CLU_008615_0_1_1; -.
DR PhylomeDB; B0XRV0; -.
DR Proteomes; UP000001699; Unassembled WGS sequence.
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 Direct protein sequencing; Glycoprotein; Hydrolase; Protease; Secreted;
KW Serine protease; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:9045640"
FT CHAIN 19..721
FT /note="Dipeptidyl-peptidase 5"
FT /id="PRO_0000372615"
FT REGION 271..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 560
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 643
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 675
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 380
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 450
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 607
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 317..318
FT /note="RV -> AL (in Ref. 1; AAB67282)"
FT /evidence="ECO:0000305"
FT CONFLICT 521
FT /note="D -> T (in Ref. 1; AAB67282)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 721 AA; 79743 MW; 4355BA317C7434F0 CRC64;
MGAFRWLSIA AAASTALALT PEQLITAPRR SEAIPDPSGK VAVFSTSQYS FETHKRTSWW
SLLDLKTGQT KVLTNDSSVS EIVWLSDDSI LYVNSTNADI PGGVELWVTQ ASSFAKGYKA
ASLPASFSGL KAAKTKSGDI RFVAYGQSYP NGTAYNEELA TAPLSSARIY DSIYVRHWDY
WLSTTFNAVF SGTLKKGHGK NGYSLDGELK NLVSPVKNAE SPYPPFGGAS DYDLSPDGKW
VAFKSKAPEL PKANFTTSYI YLVPHDASET ARPINGPDSP GTPKGIKGDS SSPVFSPNGD
KLAYFQMRDE TYESDRRVLY VYSLGSKKTI PSVAGDWDRS PDSVKWTPDG KTLIVGSEDL
GRTRLFSLPA NAKDDYKPKN FTDGGSVSAY YFLPDSSLLV TGSALWTNWN VYTAKPEKGV
IKKIASANEI DPELKGLGPS DISEFYFQGN FTDIHAWVIY PENFDKSKKY PLIFFIHGGP
QGNWADGWST RWNPKAWADQ GYVVVAPNPT GSTGFGQALT DAIQNNWGGA PYDDLVKCWE
YVHENLDYVD TDHGVAAGAS YGGFMINWIQ GSPLGRKFKA LVSHDGTFVA DAKVSTEELW
FMQREFNGTF WDARDNYRRW DPSAPERILQ FATPMLVIHS DKDYRLPVAE GLSLFNVLQE
RGVPSRFLNF PDENHWVVNP ENSLVWHQQA LGWINKYSGV EKSNPNAVSL EDTVVPVVNY
N
