ID   DPP5_ASPOR              Reviewed;         725 AA.
AC   Q9Y8E3;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 2.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Dipeptidyl-peptidase 5;
DE            EC=3.4.14.-;
DE   AltName: Full=Alanyl dipeptidyl peptidase;
DE   AltName: Full=Dipeptidyl-peptidase V;
DE            Short=DPP V;
DE            Short=DppV;
DE   Flags: Precursor;
GN   ORFNames=AO090011000795-A;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Doumas A., Monod M.;
RT   "Secreted alanyl dipeptidyl peptidase (DppV) of Aspergillus oryzae.";
RL   Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the peptidase S9C family. {ECO:0000305}.
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DR   EMBL; AF125190; AAD41777.1; -; Genomic_DNA.
DR   EMBL; AP007171; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_003190827.1; XM_003190779.1.
DR   AlphaFoldDB; Q9Y8E3; -.
DR   SMR; Q9Y8E3; -.
DR   ESTHER; aspor-Q9Y8E3; Prolyl_oligopeptidase_S9.
DR   MEROPS; S09.012; -.
DR   Proteomes; UP000006564; Chromosome 7.
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   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Protease; Reference proteome; Secreted;
KW   Serine protease; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..725
FT                   /note="Dipeptidyl-peptidase 5"
FT                   /id="PRO_0000027224"
FT   ACT_SITE        563
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        646
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        678
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        75
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        96
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        153
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        258
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        383
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        453
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        610
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        715
FT                   /note="N -> D (in Ref. 1; AAD41777)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   725 AA;  80383 MW;  AD5C77759F5D666E CRC64;
     MGALRWLSIA ATASTALALN PEGLISAPRR SEAIPNPSGD VAVFSQSQYS FKTHKTTSQW
     NVLDLKSGDI KLLTNDSDVS EIVWLGSDDS TVLYVNGTNA DIPGGVELWV SDISDFANGY
     KAASLPASFS GFKVVTTDSG DVRYVAYAES WANGTAYNEE LVAKPLSSAR IYDSIYVRHW
     DYYLTTRFNA VFSGTLKKSE GKGKATYKAD GDLKNLVSPV KNAESPYPPF GGASDYDLSP
     DGKWVAFKSK AHDIPRANYT TAYIFLVPHD GSKTAVPING PDSPGTPEGV KGDAGSPVFS
     PDSKKIAYWQ MADESYEADH RTLYVYTVGS EETIPSLAAD WDRSLDSVKW ADDDNLIIGV
     EDAGRSRLFS IPADAGDDYK PKNFTDGGVV SAYYQLPDST YLVTSTAIWT SWNVYIASPE
     KGVIKTLATA NKIDPELKGL GPEIVDEFYY EGNWTKIQAF VIYPENFDKS KSYPLLYYIH
     GGPQSSWLDS WSTRWNPKVF ADQGYVVVAP NPTGSSGFGD ALQDAIQNQW GGYPYEDLVK
     GWEYVNENFD FIDTDNGVAA GASYGGFMIN WIQGSDLGRK FKALVSHDGT FVADAKVSTE
     ELWFMQHEFN GTFWDNRENY RRWDPSAPER ILKFSTPMLI IHSDLDYRLP VSEGLSLFNI
     LQERGVPSRF LNFPDENHWV QNKENSLVWH QQVLGWLNKY SGVEESNEDA VSLDNTVIPV
     VDYNP