DPP5_ASPNC
ID DPP5_ASPNC Reviewed; 726 AA.
AC A2QZF1;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Probable 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; ORFNames=An12g04700;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
CC -!- FUNCTION: Extracellular dipeptidyl-peptidase which removes N-terminal
CC dipeptides sequentially from polypeptides having unsubstituted N-
CC termini. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S9C family. {ECO:0000305}.
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DR EMBL; AM270269; CAK97161.1; -; Genomic_DNA.
DR RefSeq; XP_001395540.1; XM_001395503.1.
DR AlphaFoldDB; A2QZF1; -.
DR SMR; A2QZF1; -.
DR ESTHER; aspng-DPP5; Prolyl_oligopeptidase_S9.
DR MEROPS; S09.012; -.
DR PaxDb; A2QZF1; -.
DR EnsemblFungi; CAK97161; CAK97161; An12g04700.
DR GeneID; 4985819; -.
DR KEGG; ang:ANI_1_596104; -.
DR VEuPathDB; FungiDB:An12g04700; -.
DR HOGENOM; CLU_008615_0_1_1; -.
DR Proteomes; UP000006706; Chromosome 3L.
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; Reference proteome;
KW Secreted; Serine protease; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..726
FT /note="Probable dipeptidyl-peptidase 5"
FT /id="PRO_5000220740"
FT ACT_SITE 564
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 647
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 679
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 399
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 454
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 530
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 611
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 726 AA; 79278 MW; 9D374437AD6DFD04 CRC64;
MGALQWLSIT AAAASAVSAL TPEQMIGAPR RTEVIPNPSG DTGLFSTSQW SFDTHSESTW
WSLIDLQSGK TTTLTDDSDI EEIIWLGSDN STLLYINSTN AQVPGGVELW IADSSDFANA
YKAASLSAGF LGIKSTVTDS GDVHFILRGK SYPNGTAYND QLAETYPSTA RIYDSIFVRH
WDTYLTTASH AVFSGTLQSS TSDDGNVQYT SSGGLTNLVN PVKGAESPFP PFGGNDDYDL
SPDGKWVTFK SKAPELPLAN NTAAYVYLVP HDGSATAFAV NGPDSPATPE GVEGESNNPV
FSPDSDKIAY FQMATNTYES DRNVLYVYSI ADDTITPLAK DWDRSPSSVT WVDGDNLVVA
SQDLGRTRLF AIPGDAGDDF KPTNFTDGGS VSAQYVLSNS TLLVTSSAFW TSWSVYTASP
DEGVINTLAS ANEIDPELSG LSSSDFEEFY FDGNWTTLQG WITYPQDFDS SKKYPLAFLI
HGGPEDAWAD EWNLKWHSKV FADQGYVVVQ PNPTGSTGFG QQLTDAIQLN WTGAAYDDLT
KAWQYVHDTY DFIDTDNGVA AGPSFGAFMI TWIQGDDFGR KFKALVSHDG PFIGDAWVET
DELWFVEHEF NGTFWQARDA FHNTDPSGPS RVLAYSTPQL VIHSDKDYRI PVANGIGLFN
TLQERGVPSR FLNFPDEDHW VTGQENSLVW YQQVLGWINR YSGVGGSNPD AIALEDTVNP
VVDLNP
