DPP4_NEOFI
ID DPP4_NEOFI Reviewed; 765 AA.
AC A1CX29;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=NFIA_106690;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
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.
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; DS027685; EAW25181.1; -; Genomic_DNA.
DR RefSeq; XP_001267078.1; XM_001267077.1.
DR AlphaFoldDB; A1CX29; -.
DR SMR; A1CX29; -.
DR STRING; 36630.CADNFIAP00010057; -.
DR ESTHER; aspfu-DPP4; DPP4N_Peptidase_S9.
DR MEROPS; S09.008; -.
DR EnsemblFungi; EAW25181; EAW25181; NFIA_106690.
DR GeneID; 4593808; -.
DR KEGG; nfi:NFIA_106690; -.
DR VEuPathDB; FungiDB:NFIA_106690; -.
DR eggNOG; KOG2100; Eukaryota.
DR HOGENOM; CLU_006105_0_2_1; -.
DR OMA; AYVWKND; -.
DR OrthoDB; 269253at2759; -.
DR Proteomes; UP000006702; 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; Reference proteome;
KW Secreted; Serine protease; Signal.
FT SIGNAL 1..14
FT /evidence="ECO:0000255"
FT CHAIN 15..765
FT /note="Probable dipeptidyl peptidase 4"
FT /id="PRO_0000397814"
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"
SQ SEQUENCE 765 AA; 85823 MW; 490FAB631D986EA1 CRC64;
MKWSILLLVG CAAAIDVPRQ PYAPTGSGKK RLTFNETVVK RAISPSAISV EWISTSEDGD
YVYQDQDGSL KIQSIVTNNT QTLVPADKVP EDAYSYWIHP NLSSVLWATN YTKQYRHSYF
ADYFIQDVQS MNLRPLAPDQ SGDIQYAQWS PTGDAIAFVR GNDVFVWTNA STSQITNDGG
PDLFNGVPDW IYEEEILGDR FALWFSPDGA YLAFLRFNET GVPTFTVPYY MDNEEIAPPY
PRELELRYPK VSQTNPTVEL NLLELRTGER TPVPIDAFDA KELIIGEVAW LTEKHDVVAV
KAFNRVQDRQ KVVAVDVASL RTKTINERDG TDGWLDNLLS MAYIGPIGES KEEYYIDISD
QSGWAHLWLF PVAGGEPIAL TKGEWEVTAI LSIDKPRQLV YFLSTKHHST ERHLYSVSWK
TMEITPLVDD TVPAVWSASF SSQGGYYILS YRGPDVPYQD LYAINSTAPL RTITSNAAVL
DGLKEYTLPN ITYFELALPS GETLNVMQRL PVKFSSKKKY PVLFTPYGGP GAQEVSKAWQ
ALDFKAYIAS DPELEYITWT VDNRGTGYKG RAFRCQVTSR LGELEAADQV FAAQQAAKLP
YVDADHIAIW GWSYGGYLTG KVIETDSGAF SLGVQTAPVS DWRFYDSMYT ERYMKTLESN
AAGYNASAIR KVAGYKNVRG GVLIQHGTGD DNVHFQNAAA LVDTLVGAGV TPEKLQVQWF
TDSDHGIRYH GGNVFLYRQL SKRLYEEKKR KEKGEAHQWS KKSVL
