VDPP4_APIME
ID VDPP4_APIME Reviewed; 775 AA.
AC B2D0J4;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Venom dipeptidyl peptidase 4;
DE AltName: Full=Allergen C;
DE AltName: Full=Venom dipeptidyl peptidase IV;
DE EC=3.4.14.5;
DE AltName: Allergen=Api m 5;
DE Flags: Precursor;
OS Apis mellifera (Honeybee).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea; Apidae;
OC Apis.
OX NCBI_TaxID=7460;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 50-63; 76-88; 178-193 AND
RP 606-619, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY,
RP ACTIVITY REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP 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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17073008; DOI=10.1038/nature05260;
RG Honeybee genome sequencing consortium;
RT "Insights into social insects from the genome of the honeybee Apis
RT mellifera.";
RL Nature 443:931-949(2006).
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 promelittin into its active form 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 duct.
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; EU564832; ACB70230.1; -; mRNA.
DR RefSeq; NP_001119715.1; NM_001126243.1.
DR AlphaFoldDB; B2D0J4; -.
DR SMR; B2D0J4; -.
DR STRING; 7460.GB45028-PA; -.
DR Allergome; 5754; Api m 5.
DR Allergome; 5755; Api m 5.0101.
DR ESTHER; apime-vdpp4; DPP4N_Peptidase_S9.
DR PaxDb; B2D0J4; -.
DR GeneID; 410337; -.
DR KEGG; ame:410337; -.
DR eggNOG; KOG2100; Eukaryota.
DR OrthoDB; 269253at2759; -.
DR PhylomeDB; B2D0J4; -.
DR Proteomes; UP000005203; Unplaced.
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; Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..775
FT /note="Venom dipeptidyl peptidase 4"
FT /id="PRO_5000336987"
FT ACT_SITE 639
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 718
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 750
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 473
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 505
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 578
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 631
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 689
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 694
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 450..453
FT /evidence="ECO:0000250"
FT DISULFID 463..481
FT /evidence="ECO:0000250"
FT DISULFID 659..770
FT /evidence="ECO:0000250"
SQ SEQUENCE 775 AA; 87937 MW; 7C31C89636EBDEF2 CRC64;
MEVLVQLALL LVVHGSLVVL VAGKSVPRVI DQDLERYEPL EEEDHRGARV PFNLEETYDQ
SFRANSFNGT WKTDREILYS DNYVGDIRLF DVTTGSGTVL LDSSVTADFD KASVMFSFDN
SHVAIGHDYV NGFRYSIHQK CTVYNIKSRT FTDIANGDRI PLFKWSPTRN ALIYVHKNDI
YYQVFFEGGS DTRRITNTGV PDIVFNGIPD WVYEEEVLGS PVAFWISPDG RHLAFATFND
TNVRDIVISK YGSPGNSRDQ YPNEIRIKYP KAGTTNPFVS LSVIDLHDPS SKLIDLPPPV
DVVGADNVLY TANWRRDGEI VATWTNRVQN KAQLVLYDTK GNANNIYYEE ETEGWLRIQP
PLYHDRYVIV AKLQDSGTKA GRFLHATRLE YRNGALVDET DLTPGTCEVI SLLLVDHARA
RLYYLGTELG KPSHKNLYSV QLSGNEPPVC LSCDVLTPEG NRCTYAYAYF STNGSHYALY
CAGPDPVFIA IVNANHRQIS IWEENRSLRR KLAARTQPIV KNFNVNANGY TNKVKLYLPP
DFDETKKYPL LITVYAGPNT IRITEEATYG FESYIVTNRS VIYGRIDGRG SAYKGSKMLF
EIYRRLGTVE IEDQIIITRT LQEKYSWIDS NRTGIWGWSY GGFSAAMVLA TDAESVFKCG
ISVAPVTSWI YYDSLYTERF MGLPTPEDNQ SGYNDTDVSR RVEGMRGKKY MLIHGTADDN
VHYQQTMMLN KALVNSDIMF QQQTYTDEAH ALGNVFPHLY HTTDRFWANC LGYSH
