ID   DPP4_ASPFN              Reviewed;         771 AA.
AC   B8N970;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Probable dipeptidyl peptidase 4;
DE            EC=3.4.14.5;
DE   AltName: Full=Dipeptidyl peptidase IV;
DE            Short=DPP IV;
DE            Short=DppIV;
DE   Flags: Precursor;
GN   Name=dpp4; ORFNames=AFLA_110160;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
CC   -!- FUNCTION: Extracellular dipeptidyl-peptidase which removes N-terminal
CC       dipeptides sequentially from polypeptides having unsubstituted N-
CC       termini provided that the penultimate residue is proline.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a
CC         polypeptide, preferentially when Yaa is Pro, provided Zaa is neither
CC         Pro nor hydroxyproline.; EC=3.4.14.5;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S9B family. {ECO:0000305}.
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DR   EMBL; EQ963475; EED53639.1; -; Genomic_DNA.
DR   RefSeq; XP_002376885.1; XM_002376844.1.
DR   AlphaFoldDB; B8N970; -.
DR   SMR; B8N970; -.
DR   STRING; 5059.CADAFLAP00004750; -.
DR   ESTHER; aspor-DPPIV; DPP4N_Peptidase_S9.
DR   MEROPS; S09.008; -.
DR   EnsemblFungi; EED53639; EED53639; AFLA_110160.
DR   VEuPathDB; FungiDB:AFLA_110160; -.
DR   eggNOG; KOG2100; Eukaryota.
DR   HOGENOM; CLU_006105_0_2_1; -.
DR   OMA; AYVWKND; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001375; Peptidase_S9.
DR   InterPro; IPR002469; Peptidase_S9B_N.
DR   Pfam; PF00930; DPPIV_N; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Glycoprotein; Hydrolase; Protease; Secreted;
KW   Serine protease; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..771
FT                   /note="Probable dipeptidyl peptidase 4"
FT                   /id="PRO_0000397811"
FT   ACT_SITE        618
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        695
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        730
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        37
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        80
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        114
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        173
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        222
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        470
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        495
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   771 AA;  86875 MW;  25A9C096B0258A7B CRC64;
     MKYSKLLLLL VSVVQALDVP RKPHAPTGEG SKRLTFNETV VKQAITPTSR SVQWLSGAED
     GSYVYAAEDG SLTIENIVTN ESRTLIPADK IPTGKEAFNY WIHPDLSSVL WASNHTKQYR
     HSFFADYYVQ DVESLKSVPL MPDQEGDIQY AQWSPVGNTI AFVRENDLYV WDNGTVTRIT
     DDGGPDMFHG VPDWIYEEEI LGDRYALWFS PDGEYLAYLS FNETGVPTYT VQYYMDNQEI
     APAYPWELKI RYPKVSQTNP TVTLSLLNIA SKEVKQAPID AFESTDLIIG EVAWLTDTHT
     TVAAKAFNRV QDQQKVVAVD TASNKATVIS DRDGTDGWLD NLLSMKYIGP IKPSDKDAYY
     IDISDHSGWA HLYLFPVSGG EPIPLTKGDW EVTSILSIDQ ERQLVYYLST QHHSTERHLY
     SVSYSTFAVT PLVDDTVAAY WSASFSANSG YYILTYGGPD VPYQELYTTN STKPLRTITD
     NAKVLEQIKD YALPNITYFE LPLPSGETLN VMQRLPPGFS PDKKYPILFT PYGGPGAQEV
     TKRWQALNFK AYVASDSELE YVTWTVDNRG TGFKGRKFRS AVTRQLGLLE AEDQIYAAQQ
     AANIPWIDAD HIGIWGWSFG GYLTSKVLEK DSGAFTLGVI TAPVSDWRFY DSMYTERYMK
     TLSTNEEGYE TSAVRKTDGF KNVEGGFLIQ HGTGDDNVHF QNSAALVDLL MGDGVSPEKL
     HSQWFTDSDH GISYHGGGVF LYKQLARKLY QEKNRQTQVL MHQWTKKDLE E