DAP4_PSEMX
ID DAP4_PSEMX Reviewed; 745 AA.
AC Q6F3I7;
DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Dipeptidyl aminopeptidase 4 {ECO:0000312|EMBL:BAD27580.1};
DE EC=3.4.14.5 {ECO:0000269|PubMed:15866709, ECO:0000269|PubMed:8988635};
DE AltName: Full=Dipeptidyl aminopeptidase IV {ECO:0000312|EMBL:BAD27580.1};
DE Short=DAP IV {ECO:0000303|PubMed:15866709, ECO:0000303|PubMed:8988635};
DE Flags: Precursor;
GN Name=dap4 {ECO:0000312|EMBL:BAD27580.1};
OS Pseudoxanthomonas mexicana.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=128785;
RN [1] {ECO:0000312|EMBL:BAD27580.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), PROTEIN SEQUENCE OF
RP N-TERMINUS, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP MET-1 AND MET-12.
RC STRAIN=WO24 {ECO:0000312|EMBL:BAD27580.1};
RX PubMed=15866709; DOI=10.1016/j.pep.2004.10.027;
RA Ogasawara W., Tanaka C., Suzuki M., Kobayashi G., Ogawa Y., Okada H.,
RA Morikawa Y.;
RT "Isoforms of dipeptidyl aminopeptidase IV from Pseudomonas sp. WO24: role
RT of the signal sequence and overexpression in Escherichia coli.";
RL Protein Expr. Purif. 41:241-251(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-46 (ISOFORMS 1 AND 2), PROTEIN
RP SEQUENCE OF N-TERMINUS, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT, AND SIGNAL.
RC STRAIN=WO24 {ECO:0000303|PubMed:8988635};
RX PubMed=8988635; DOI=10.1271/bbb.60.2032;
RA Ogasawara W., Ogawa Y., Yano K., Okada H., Morikawa Y.;
RT "Dipeptidyl aminopeptidase IV from Pseudomonas sp. WO24.";
RL Biosci. Biotechnol. Biochem. 60:2032-2037(1996).
CC -!- FUNCTION: Catalyzes the sequential release of Tyr-Pro, Phe-Pro and Gly-
CC Pro from the N-terminus of peptides and proteins. Is able to cleaves
CC bioactive peptide beta-casomorphin. {ECO:0000269|PubMed:8988635}.
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 Evidence={ECO:0000269|PubMed:15866709, ECO:0000269|PubMed:8988635};
CC -!- ACTIVITY REGULATION: Completely inhibited by the serine protease
CC inhibitor diisopropyl fluorophosphate (DFP) and moderately by N-tosyl-
CC L-phenyl-alanyl chloromethyl ketone (TPCK). Somewhat inhibited by
CC phenylmethanesulfonyl fluoride (PMSF). Activity is not affected by
CC thiol- or metalloprotease inhibitors, such as iodoacetate (IAA), EDTA,
CC N-tosyl-L-lysyl chloromethyl ketone (TLCK), o-phenanthlorine, N-
CC ethylmaleimide (NEM) or dithiothreitol (DTT).
CC {ECO:0000269|PubMed:8988635}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.142 mM for Gly-Pro-pNA (at pH 8.0 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:8988635};
CC Vmax=16.7 umol/min/mg enzyme with Gly-Pro-pNA as substrate (at pH 8.0
CC and 37 degrees Celsius) {ECO:0000269|PubMed:8988635};
CC pH dependence:
CC Optimum pH is 8.0 for the hydrolysis of Gly-Pro-pNA. No hydrolysis is
CC detected at a pH below 5.5 or above 11.0.
CC {ECO:0000269|PubMed:8988635};
CC Temperature dependence:
CC Optimum temperature is between 40 and 50 degrees Celsius for the
CC hydrolysis of Gly-Pro-pNA. Stable for at least 30 min below 30
CC degrees Celsius. {ECO:0000269|PubMed:8988635};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8988635}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:15866709}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Periplasm
CC {ECO:0000269|PubMed:15866709}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=Q6F3I7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6F3I7-2; Sequence=VSP_057834;
CC -!- SIMILARITY: Belongs to the peptidase S9B family. {ECO:0000305}.
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DR EMBL; AB183425; BAD27580.1; -; Genomic_DNA.
DR PDB; 5YP1; X-ray; 2.47 A; A/B/C/D=1-745.
DR PDB; 5YP2; X-ray; 2.13 A; A/B=1-745.
DR PDB; 5YP3; X-ray; 2.44 A; A/B/C/D=1-745.
DR PDB; 5YP4; X-ray; 1.90 A; A/B/C/D=1-745.
DR PDBsum; 5YP1; -.
DR PDBsum; 5YP2; -.
DR PDBsum; 5YP3; -.
DR PDBsum; 5YP4; -.
DR AlphaFoldDB; Q6F3I7; -.
DR SMR; Q6F3I7; -.
DR ESTHER; 9psed-q6f3i7; DPP4N_Peptidase_S9.
DR MEROPS; S09.009; -.
DR BRENDA; 3.4.14.5; 27338.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042597; C:periplasmic space; IDA:UniProtKB.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IDA:UniProtKB.
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 3D-structure; Alternative initiation; Aminopeptidase; Cytoplasm;
KW Direct protein sequencing; Hydrolase; Periplasm; Protease; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:15866709,
FT ECO:0000269|PubMed:8988635"
FT CHAIN 23..745
FT /note="Dipeptidyl aminopeptidase 4"
FT /id="PRO_0000433643"
FT ACT_SITE 613
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q12884,
FT ECO:0000255|PROSITE-ProRule:PRU10084"
FT ACT_SITE 689
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q12884"
FT ACT_SITE 721
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q12884"
FT BINDING 208
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q12884"
FT BINDING 209
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q12884"
FT VAR_SEQ 1..11
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000269|PubMed:8988635,
FT ECO:0000303|PubMed:15866709"
FT /id="VSP_057834"
FT MUTAGEN 1
FT /note="M->G: Localizes to the cytoplasm."
FT /evidence="ECO:0000269|PubMed:15866709"
FT MUTAGEN 12
FT /note="M->I: Localizes to the periplasm."
FT /evidence="ECO:0000269|PubMed:15866709"
FT CONFLICT 37
FT /note="S -> L (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT HELIX 27..31
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 50..58
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 65..72
FT /evidence="ECO:0007829|PDB:5YP4"
FT TURN 73..76
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:5YP4"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:5YP4"
FT HELIX 96..104
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 122..129
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 132..139
FT /evidence="ECO:0007829|PDB:5YP4"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:5YP2"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 165..172
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:5YP4"
FT TURN 181..184
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 195..200
FT /evidence="ECO:0007829|PDB:5YP4"
FT HELIX 204..209
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 225..231
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 237..244
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 247..254
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 264..270
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 288..298
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 301..308
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 311..320
FT /evidence="ECO:0007829|PDB:5YP4"
FT TURN 321..323
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 326..333
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 352..356
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 363..367
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 369..372
FT /evidence="ECO:0007829|PDB:5YP1"
FT STRAND 374..378
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 380..382
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 384..391
FT /evidence="ECO:0007829|PDB:5YP4"
FT TURN 392..395
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 396..401
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 409..415
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 427..435
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 439..447
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 449..451
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 454..459
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 464..469
FT /evidence="ECO:0007829|PDB:5YP4"
FT HELIX 481..484
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 490..496
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 503..509
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 520..525
FT /evidence="ECO:0007829|PDB:5YP4"
FT HELIX 544..553
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 557..561
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 566..569
FT /evidence="ECO:0007829|PDB:5YP4"
FT HELIX 571..574
FT /evidence="ECO:0007829|PDB:5YP4"
FT HELIX 575..577
FT /evidence="ECO:0007829|PDB:5YP4"
FT TURN 581..583
FT /evidence="ECO:0007829|PDB:5YP4"
FT HELIX 584..597
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 602..612
FT /evidence="ECO:0007829|PDB:5YP4"
FT HELIX 614..625
FT /evidence="ECO:0007829|PDB:5YP4"
FT TURN 627..629
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 631..637
FT /evidence="ECO:0007829|PDB:5YP4"
FT HELIX 642..644
FT /evidence="ECO:0007829|PDB:5YP4"
FT HELIX 647..654
FT /evidence="ECO:0007829|PDB:5YP4"
FT HELIX 657..659
FT /evidence="ECO:0007829|PDB:5YP4"
FT HELIX 661..667
FT /evidence="ECO:0007829|PDB:5YP4"
FT HELIX 669..672
FT /evidence="ECO:0007829|PDB:5YP4"
FT HELIX 673..675
FT /evidence="ECO:0007829|PDB:5YP4"
FT TURN 678..680
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 681..686
FT /evidence="ECO:0007829|PDB:5YP4"
FT TURN 690..694
FT /evidence="ECO:0007829|PDB:5YP4"
FT HELIX 695..707
FT /evidence="ECO:0007829|PDB:5YP4"
FT STRAND 712..716
FT /evidence="ECO:0007829|PDB:5YP4"
FT HELIX 725..743
FT /evidence="ECO:0007829|PDB:5YP4"
FT INIT_MET Q6F3I7-2:1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8988635"
SQ SEQUENCE 745 AA; 82295 MW; AF845A8E2F47BD4B CRC64;
MRLALFALFA LMTVATALPA HAEKLTLEAI TGSAPLSGPT LTKPQIAPDG SRVTFLRGKD
RDRNRLDLWE YDIASGQTRL LVDSSVVLPG EEVLSDEEKA RRERQRIAAL SGIVDYQWSP
DGKALLFPLG GELYFYDLTK SGRDAVRKLT NGGGFATDPK ISPKGGFVSF IRDRNLWAID
LASGKEVQLT RDGSDTIGNG VAEFVADEEM DRHTGYWWAP DDAAIAFARI DETPVPVQKR
YEVYPDRTEV VEQRYPAAGD HNVRVQLGVI APKTGARPRW IDLGKDPDIY LARVDWRDPQ
RLTFQRQSRD QKKIELIETT LTNGTQRTLV TETSTTWVPL HNDLRFLKDG RFLWSSERSG
FEHLYVASED GSTLTALTQG EWVVDSLLAI DEAAGLAYVS GTRDGATEAH VYAVPLSGGE
PRRLTQAPGM HAATFARNAS VFVDSWSSDT TLPQIELFKA DGTKLATLLV NDVSDATHPY
AKYRAAHQPT AYGTLTAADG TTPLHYSLIK PAGFDPKKQY PVVVFVYGGP AAQTVTRAWP
GRSDSFFNQY LAQQGYVVFT LDNRGTPRRG AAFGGALYGK QGTVEVDDQL RGIEWLKSQA
FVDPARIGVY GWSNGGYMTL MLLAKHDEAY ACGVAGAPVT DWALYDTHYT ERYMDLPKAN
EAGYREASVF THVDGIGAGK LLLIHGMADD NVLFTNSTKL MSELQKRGTP FELMTYPGAK
HGLRGSDLLH RYRLTEDFFA RCLKP
