DPP4_ASPOR
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 03-AUG-2022, entry version 89.
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 EnsemblFungi; BAE59130; BAE59130; AO090023000602.
DR GeneID; 5993134; -.
DR KEGG; aor:AO090023000602; -.
DR VEuPathDB; FungiDB:AO090023000602; -.
DR HOGENOM; CLU_006105_0_2_1; -.
DR OMA; AYVWKND; -.
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; -; 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 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
