ID   DPP4_ASPOR              Reviewed;         771 AA.
AC   Q2UH35; O42812;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   RecName: Full=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=AO090023000602;
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], SUBCELLULAR LOCATION, FUNCTION, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=9835566; DOI=10.1128/aem.64.12.4809-4815.1998;
RA   Doumas A., van den Broek P., Affolter M., Monod M.;
RT   "Characterization of the prolyl dipeptidyl peptidase gene (dppIV) from the
RT   koji mold Aspergillus oryzae.";
RL   Appl. Environ. Microbiol. 64:4809-4815(1998).
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   -!- 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:0000269|PubMed:9835566}.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.0. is active between pH 4.0 and 9.0.
CC         {ECO:0000269|PubMed:9835566};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9835566}.
CC   -!- SIMILARITY: Belongs to the peptidase S9B family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA05343.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AJ002369; CAA05343.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AP007157; BAE59130.1; -; Genomic_DNA.
DR   RefSeq; XP_001821132.1; XM_001821080.2.
DR   AlphaFoldDB; Q2UH35; -.
DR   SMR; Q2UH35; -.
DR   STRING; 510516.Q2UH35; -.
DR   ESTHER; aspor-DPPIV; DPP4N_Peptidase_S9.
DR   MEROPS; S09.008; -.
DR   GlyCosmos; Q2UH35; 7 sites, No reported glycans.
DR   EnsemblFungi; BAE59130; BAE59130; AO090023000602.
DR   GeneID; 5993134; -.
DR   KEGG; aor:AO090023000602; -.
DR   VEuPathDB; FungiDB:AO090023000602; -.
DR   HOGENOM; CLU_006105_0_2_1; -.
DR   OMA; SLMFAKF; -.
DR   OrthoDB; 2876738at2759; -.
DR   Proteomes; UP000006564; Chromosome 3.
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; IDA:AspGD.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IDA:AspGD.
DR   GO; GO:0051603; P:proteolysis involved in protein catabolic process; IDA:AspGD.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 2.140.10.30; Dipeptidylpeptidase IV, N-terminal domain; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001375; Peptidase_S9.
DR   InterPro; IPR002469; Peptidase_S9B_N.
DR   PANTHER; PTHR11731:SF162; DIPEPTIDYL PEPTIDASE 4-RELATED; 1.
DR   PANTHER; PTHR11731; PROTEASE FAMILY S9B,C DIPEPTIDYL-PEPTIDASE IV-RELATED; 1.
DR   Pfam; PF00930; DPPIV_N; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
PE   1: Evidence at protein level;
KW   Aminopeptidase; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW   Secreted; Serine protease; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..771
FT                   /note="Dipeptidyl peptidase 4"
FT                   /id="PRO_5000064328"
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
//