VDDP4_VESVU
ID VDDP4_VESVU Reviewed; 776 AA.
AC B1A4F7;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Venom dipeptidyl peptidase 4;
DE EC=3.4.14.5;
DE AltName: Full=Venom dipeptidyl peptidase IV;
DE AltName: Allergen=Ves v 3;
DE Flags: Precursor;
OS Vespula vulgaris (Yellow jacket) (Wasp).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC Vespidae; Vespinae; Vespula.
OX NCBI_TaxID=7454;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 83-86; 301-309; 536-539;
RP 548-555 AND 606-613, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION,
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND ALLERGEN.
RC TISSUE=Venom, and Venom duct;
RX PubMed=20348419; DOI=10.4049/jimmunol.0803709;
RA Blank S., Seismann H., Bockisch B., Braren I., Cifuentes L., McIntyre M.,
RA Ruhl D., Ring J., Bredehorst R., Ollert M.W., Grunwald T., Spillner E.;
RT "Identification, recombinant expression, and characterization of the 100
RT kDa high molecular weight hymenoptera venom allergens Api m 5 and Ves v
RT 3.";
RL J. Immunol. 184:5403-5413(2010).
CC -!- FUNCTION: Venom dipeptidyl-peptidase which removes N-terminal
CC dipeptides sequentially from polypeptides having unsubstituted N-
CC termini provided that the penultimate residue is proline. May process
CC venom proteins into their active forms and/or modulate the chemotactic
CC activity of immune cells after the insect sting.
CC {ECO:0000269|PubMed:20348419}.
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:20348419};
CC -!- ACTIVITY REGULATION: Inhibited by diprotin A.
CC {ECO:0000269|PubMed:20348419}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20348419}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:20348419}.
CC -!- ALLERGEN: Causes an allergic reaction in human.
CC {ECO:0000269|PubMed:20348419}.
CC -!- SIMILARITY: Belongs to the peptidase S9B family. DPPIV subfamily.
CC {ECO:0000305}.
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DR EMBL; EU420987; ACA00159.1; -; mRNA.
DR AlphaFoldDB; B1A4F7; -.
DR SMR; B1A4F7; -.
DR Allergome; 5767; Ves v 3.
DR Allergome; 5768; Ves v 3.0101.
DR ESTHER; vesvu-vddp4; DPP4N_Peptidase_S9.
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:InterPro.
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 Allergen; Aminopeptidase; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Hydrolase; Protease; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..776
FT /note="Venom dipeptidyl peptidase 4"
FT /id="PRO_0000401924"
FT ACT_SITE 638
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 717
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 749
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 504
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 577
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 688
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 693
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 449..452
FT /evidence="ECO:0000250"
FT DISULFID 462..480
FT /evidence="ECO:0000250"
FT DISULFID 658..769
FT /evidence="ECO:0000250"
SQ SEQUENCE 776 AA; 88924 MW; 04A9ECBC4FFFC0B2 CRC64;
MVPLRSFVLL NSLFLVLLAA RTVVTRVIDK DNSDRIVKTQ NDQNLSKVPF NLEETYTADF
LAYVFNGTWT SDTTIVYTDR RTGDILQFDV IKQRSTLIVD SSVMDAYIVS NYVLSPKGRY
LLIGYDLKKG YRYSTFMRYV IYDIEHRAYH KIGNDMHIAL AKWAPLTDDL IYILDNDIYY
MRFSNNGFND VQRVTYDGIS GIVYNGVPDW VYEEEVLQDS SAIWFSPDGN HLAYASFDDR
NVQEILYLHY GEPGNLDDQY PTEVKIKYPK VGTLNPVVSL TLVDLHDPTL NKIDLKAPHY
AVGTDNLLYN VQWKDFDHVV VTWSNRVQNK TEIVWYNMYG EIVKTLHVVE HKGWLDIKHL
FFYKGSVYIR KLQPSGTKAG RFHHVTRYDE TFKQSPTQMD LTPDAIEVQN ICTIDQSNGR
IYYLASGLGK PSQKNLYSVP ADGSEKPTCI SCNVLTPEGN VCTYADAIFS PLGQYYVLVC
HGPDPAFVSI FNNAHQKVYS WENNLSLRKK LAKRHLPLVK DLDVRANGYE SKVRLFLPHN
FDESKSYPML VNVYAGPNTL KIIDAASYGH QVYMTTNRSV IYAYIDGRGS SNKGSKMLFS
IYRKLGTVEV EDQITVTRQL QEMFPWIDSK RTGVWGWSYG GFSTAMILAK DTSFVFKCGI
AIAPVSSWIY YDSIYTERFM GFPTPEDNLS GYNETDVSRR VEDIRGKKFM LIHGSGDDNV
HYQQSLALAK ALEKADVMFE QITYTDEAHA LFGVLPHLYH TMDRFWSDCF SLSHAH
