DPP4_ASPFC
ID DPP4_ASPFC Reviewed; 765 AA.
AC B0Y6C5; O14425;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 62.
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=AFUB_066450;
OS Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, FUNCTION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9234752; DOI=10.1128/iai.65.8.3042-3047.1997;
RA Beauvais A., Monod M., Wyniger J., Debeaupuis J.P., Grouzmann E.,
RA Brakch N., Svab J., Hovanessian A.G., Latge J.P.;
RT "Dipeptidyl-peptidase IV secreted by Aspergillus fumigatus, a fungus
RT pathogenic to humans.";
RL Infect. Immun. 65:3042-3047(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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. Contributes
CC to pathogenicity. {ECO:0000269|PubMed:9234752}.
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 Kinetic parameters:
CC KM=0.38 mM for Gly-Pro pNA and Ala-Pro pNA
CC {ECO:0000269|PubMed:9234752};
CC KM=0.15 mM for Arg-Pro pNA {ECO:0000269|PubMed:9234752};
CC pH dependence:
CC Optimum pH is 6.7 to 7.0. {ECO:0000269|PubMed:9234752};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9234752}.
CC -!- SIMILARITY: Belongs to the peptidase S9B family. {ECO:0000305}.
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DR EMBL; U87950; AAC34310.1; -; Genomic_DNA.
DR EMBL; DS499598; EDP50310.1; -; Genomic_DNA.
DR AlphaFoldDB; B0Y6C5; -.
DR SMR; B0Y6C5; -.
DR ESTHER; aspfu-DPP4; DPP4N_Peptidase_S9.
DR MEROPS; S09.008; -.
DR EnsemblFungi; EDP50310; EDP50310; AFUB_066450.
DR VEuPathDB; FungiDB:AFUB_066450; -.
DR HOGENOM; CLU_006105_0_2_1; -.
DR PhylomeDB; B0Y6C5; -.
DR Proteomes; UP000001699; 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 1: Evidence at protein level;
KW Aminopeptidase; Glycoprotein; Hydrolase; Protease; Secreted;
KW Serine protease; Signal; Virulence.
FT SIGNAL 1..14
FT /evidence="ECO:0000255"
FT CHAIN 15..765
FT /note="Probable dipeptidyl peptidase 4"
FT /id="PRO_0000397810"
FT ACT_SITE 613
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 690
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 725
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 490
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 665
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 117
FT /note="Y -> H (in Ref. 1; AAC34310)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="D -> G (in Ref. 1; AAC34310)"
FT /evidence="ECO:0000305"
FT CONFLICT 538
FT /note="A -> P (in Ref. 1; AAC34310)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 765 AA; 85876 MW; 544F27B6134F9B1B CRC64;
MKWSILLLVG CAAAIDVPRQ PYAPTGSGKK RLTFNETVVK RAISPSAISV EWISTSEDGD
YVYQDQDGSL KIQSIVTNHT QTLVPADKVP EDAYSYWIHP NLSSVLWATN YTKQYRYSYF
ADYFIQDVQS MKLRPLAPDQ SGDIQYAQWS PTGDAIAFVR DNNVFVWTNA STSQITNDGG
PDLFNGVPDW IYEEEILGDR FALWFSPDGA YLAFLRFNET GVPTFTVPYY MDNEEIAPPY
PRELELRYPK VSQTNPTVEL NLLELRTGER TPVPIDAFDA KELIIGEVAW LTGKHDVVAV
KAFNRVQDRQ KVVAVDVASL RSKTISERDG TDGWLDNLLS MAYIGPIGES KEEYYIDISD
QSGWAHLWLF PVAGGEPIAL TKGEWEVTNI LSIDKPRQLV YFLSTKHHST ERHLYSVSWK
TKEITPLVDD TVPAVWSASF SSQGGYYILS YRGPDVPYQD LYAINSTAPL RTITSNAAVL
NALKEYTLPN ITYFELALPS GETLNVMQRL PVKFSPKKKY PVLFTPYGGP GAQEVSKAWQ
ALDFKAYIAS DPELEYITWT VDNRGTGYKG RAFRCQVASR LGELEAADQV FAAQQAAKLP
YVDAQHIAIW GWSYGGYLTG KVIETDSGAF SLGVQTAPVS DWRFYDSMYT ERYMKTLESN
AAGYNASAIR KVAGYKNVRG GVLIQHGTGD DNVHFQNAAA LVDTLVGAGV TPEKLQVQWF
TDSDHGIRYH GGNVFLYRQL SKRLYEEKKR KEKGEAHQWS KKSVL
