DPP4_ASPCL
ID DPP4_ASPCL Reviewed; 768 AA.
AC A1CHP1;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=ACLA_048680;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS027054; EAW10396.1; -; Genomic_DNA.
DR RefSeq; XP_001271822.1; XM_001271821.1.
DR AlphaFoldDB; A1CHP1; -.
DR SMR; A1CHP1; -.
DR STRING; 5057.CADACLAP00004923; -.
DR ESTHER; aspcl-dpp4; DPP4N_Peptidase_S9.
DR MEROPS; S09.008; -.
DR EnsemblFungi; EAW10396; EAW10396; ACLA_048680.
DR GeneID; 4704099; -.
DR KEGG; act:ACLA_048680; -.
DR VEuPathDB; FungiDB:ACLA_048680; -.
DR eggNOG; KOG2100; Eukaryota.
DR HOGENOM; CLU_006105_0_2_1; -.
DR OMA; AYVWKND; -.
DR OrthoDB; 269253at2759; -.
DR Proteomes; UP000006701; 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..17
FT /evidence="ECO:0000255"
FT CHAIN 18..768
FT /note="Probable dipeptidyl peptidase 4"
FT /id="PRO_0000397809"
FT ACT_SITE 616
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 693
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 728
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 468
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 668
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 768 AA; 86453 MW; 124A589592FEF512 CRC64;
MKLGKWSVLL LVGCTAAIDI PRKPFPPTGS GHKRLTFNET VVKPVIAPSS TAVEWISTAE
DGDYVFQDSD GSLKIQSIVT NHTQTLVPAD KVPDDAYSYW IHPNLSSVLW ATNYTKQYRY
SYFASYYIQD LQSFKLAPLA SNQAGDIQYA NWSPTGDAIA FVRANNVYVW TAKSTTQITT
DGSADLFNGV PDWIYEEEIL GDRHALWFSP DAEYLAFLRF NETGVPTFRV PYYMDNEEVA
PPYPRELELR YPKVSQTNPT VEVRLLSRAT GEVSSVSIKA FNATDLVIGE VAWLTETHSQ
VAVKAFNRVQ DQQKVVTVDV LSLKTKTISE RDGTDGWLDN ALSITYIGQI GDSKAEYYID
ISDESGWAHL WLFPVAGGRP MALTKGEWEV TAILSIDKQR QLVYYLSTQH HSTERHVYSV
SWKTFTATPL VDDTVAAVWS ASFSSQGGYY ILSYRGPDVP YQELYAINST KPLCTITSNA
AVYDVLKQYT LPKISYFELR LPSGETLNVM QRLPVSFSPR KKYPILFTPY GGPGAQEVSK
AWQSQTFKSY IASDPELEFV TWTVDNRGTG YKGRRFRGQV AKQLGRLEAQ DQVWAAQQAA
KLPFIDAEHI AIWGWSYGGY LTGKVIETDS GVFSLGVLTA PVSDWRFYDS MYTERYMKTL
QENANGYNAS AIWDVAGYKN VRGGVLIQHG TGDDNVHFQN AAALVDRLVG EGVSPDKLQV
QWFTDSDHGI RYHGGSVFLY RQLAKRLYEE KHRKKSEGHQ WSKRSLEF
