PA1_VESVU
ID PA1_VESVU Reviewed; 336 AA.
AC P49369;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Phospholipase A1 {ECO:0000305};
DE EC=3.1.1.32 {ECO:0000305|PubMed:8828537};
DE EC=3.1.1.4 {ECO:0000305|PubMed:8828537};
DE AltName: Full=Allergen Ves v I;
DE AltName: Allergen=Ves v 1 {ECO:0000303|PubMed:8828537};
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 37-65; 165-183; 247-263 AND
RP 273-294, SUBCELLULAR LOCATION, AND ALLERGEN.
RC TISSUE=Venom, and Venom gland;
RX PubMed=8828537; DOI=10.1016/s0091-6749(96)70093-3;
RA King T.P., Lu G., Gonzalez M., Qian N., Soldatova L.;
RT "Yellow jacket venom allergens, hyaluronidase and phospholipase: sequence
RT similarity and antigenic cross-reactivity with their hornet and wasp
RT homologs and possible implications for clinical allergy.";
RL J. Allergy Clin. Immunol. 98:588-600(1996).
CC -!- FUNCTION: Catalyzes the hydrolysis of phosphatidylcholine with
CC phospholipase A1 (EC 3.1.1.32) and phospholipase A2 (EC 3.1.1.4)
CC activities. Shows hemolytic activity. {ECO:0000250|UniProtKB:P0DMB7,
CC ECO:0000305|PubMed:8828537}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32;
CC Evidence={ECO:0000305|PubMed:8828537};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC Evidence={ECO:0000305|PubMed:8828537};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8828537}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:8828537}.
CC -!- ALLERGEN: Causes an allergic reaction in human (By similarity). It
CC exhibits some cross-reactivity with antibodies from mouse immunizated
CC to other Hymenoptera phospholipases (PubMed:8828537).
CC {ECO:0000250|UniProtKB:A2VBC4, ECO:0000269|PubMed:8828537}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; L43561; AAB48072.1; -; mRNA.
DR AlphaFoldDB; P49369; -.
DR SMR; P49369; -.
DR Allergome; 3520; Ves v 1.0101.
DR Allergome; 668; Ves v 1.
DR ESTHER; vesvu-pa1; Insect_Phospholipase.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0052739; F:phosphatidylserine 1-acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008970; F:phospholipase A1 activity; IEA:UniProtKB-EC.
DR GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00707; Pancreat_lipase_like; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002334; Allerg_PlipaseA1.
DR InterPro; IPR013818; Lipase.
DR InterPro; IPR033906; Lipase_N.
DR InterPro; IPR000734; TAG_lipase.
DR PANTHER; PTHR11610; PTHR11610; 1.
DR Pfam; PF00151; Lipase; 1.
DR PRINTS; PR00825; DOLALLERGEN.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 1: Evidence at protein level;
KW Allergen; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Lipid degradation; Lipid metabolism; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT PROPEP 28..36
FT /evidence="ECO:0000269|PubMed:8828537"
FT /id="PRO_0000425190"
FT CHAIN 37..336
FT /note="Phospholipase A1"
FT /id="PRO_0000017813"
FT ACT_SITE 173
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT ACT_SITE 201
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 265
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT DISULFID 40..123
FT /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT DISULFID 212..217
FT /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT DISULFID 255..263
FT /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT DISULFID 280..304
FT /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT DISULFID 281..329
FT /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT DISULFID 297..302
FT /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT CONFLICT 37
FT /note="G -> F (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 336 AA; 37676 MW; 65548B7F5BE56456 CRC64;
MEENMNLKYL LLFVYFVQVL NCCYGHGDPL SYELDRGPKC PFNSDTVSII IETRENRNRD
LYTLQTLQNH PEFKKKTITR PVVFITHGFT SSASETNFIN LAKALVDKDN YMVISIDWQT
AACTNEAAGL KYLYYPTAAR NTRLVGQYIA TITQKLVKHY KISMANIRLI GHSLGAHASG
FAGKKVQELK LGKYSEIIGL DPARPSFDSN HCSERLCETD AEYVQIIHTS NYLGTEKTLG
TVDFYMNNGK NQPGCGRFFS EVCSHSRAVI YMAECIKHEC CLIGIPKSKS SQPISSCTKQ
ECVCVGLNAK KYPSRGSFYV PVESTAPFCN NKGKII
