DPP4_EMENI
ID DPP4_EMENI Reviewed; 773 AA.
AC Q5AZ42; C8V0E7;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=AN6438;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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; AACD01000108; EAA58460.1; -; Genomic_DNA.
DR EMBL; BN001301; CBF69472.1; -; Genomic_DNA.
DR RefSeq; XP_664042.1; XM_658950.1.
DR AlphaFoldDB; Q5AZ42; -.
DR SMR; Q5AZ42; -.
DR STRING; 162425.CADANIAP00006538; -.
DR ESTHER; emeni-q5az42; DPP4N_Peptidase_S9.
DR MEROPS; S09.008; -.
DR EnsemblFungi; CBF69472; CBF69472; ANIA_06438.
DR EnsemblFungi; EAA58460; EAA58460; AN6438.2.
DR GeneID; 2871333; -.
DR KEGG; ani:AN6438.2; -.
DR VEuPathDB; FungiDB:AN6438; -.
DR eggNOG; KOG2100; Eukaryota.
DR HOGENOM; CLU_006105_0_2_1; -.
DR InParanoid; Q5AZ42; -.
DR OMA; AYVWKND; -.
DR OrthoDB; 269253at2759; -.
DR Proteomes; UP000000560; Chromosome I.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IDA:AspGD.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IBA:GO_Central.
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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..773
FT /note="Probable dipeptidyl peptidase 4"
FT /id="PRO_0000397813"
FT ACT_SITE 619
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 696
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 731
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 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 496
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 671
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 773 AA; 86855 MW; DEEB398491278E67 CRC64;
MKLSVLSVLL VSVAQAAAAP WRPREPRAAG SKRLTFNETV ISAALSPSSI SVQWIATEND
GDYVYQEEDG SIKIESIVTN RSQTIVPAEK IPADAYSYWI SPDLSAVLWA TNYTKQYRHS
FFADYYIQDV ETLETVPLVE DMVGDIQYAE WSPSGDSIAF VRGNNLWTWS DGTVTAITKD
GGPDMFHGVP DWIYEEEILG DRFALWFSPD SELLAFLTFN ETGVPTFTVQ YFMDNQEIAP
PYPRELDIRY PKVSETNPTV KLNILQLSDN TVSTIPIDVF DPSELIVGEV AWVTDTHTEL
AVKAFNRVQD ESKVVIVETA SGETKIAHER DGTDGWLDNL LSISYVGPLA LGSGDASSAY
YVDLSDHSGW THLYLFSTSG GDPIPLTEGE WEVTSIVSID QERELVYYLS TQHHSTERHL
YSVSYRTFEI TPLVDDTVEA YWSVSFSAKA GYYILTYAGP SVPYQELYSV NQTAPLRTLT
SNAALIEKLE EYALPNISYF ELEIPSGEKL NVMQRLPVGF SPDKKYPVLF TPYGGPGAQE
VSKRWQSLDF NAYIASDPEL EYVTWTVDNR GTGYRGREFR SLVAKQLGKL EAEDQVYAAK
QAAKLDWVDS EHIAIWGWSY GGYLTGKVLE TDSGAFSLGL LTAPVSDWRL YDSMYTERYM
KTLSTNAEGY NTTAIRHTDG FKNVEGGFLI QHGTGDDNVH FQNAAALGDT LIGNGVTPEK
MQVQWFTDSD HSIRYNGGNV FLYRQLAQRL YKEKNRAKKE QHQWSKRSQD WVV
