ID   PA1_VESMC               Reviewed;         300 AA.
AC   P51528;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   22-FEB-2023, entry version 89.
DE   RecName: Full=Phospholipase A1 {ECO:0000305|PubMed:8199462};
DE            Short=PLA1 {ECO:0000305};
DE            EC=3.1.1.32 {ECO:0000250|UniProtKB:P0DMB4};
DE   AltName: Full=Allergen Ves m I;
DE   AltName: Allergen=Ves m 1 {ECO:0000303|PubMed:8199462};
OS   Vespula maculifrons (Eastern 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=7453;
RN   [1]
RP   PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=8199462; DOI=10.1159/000236728;
RA   Hoffman D.R.;
RT   "Allergens in hymenoptera venom. XXVI: the complete amino acid sequences of
RT   two vespid venom phospholipases.";
RL   Int. Arch. Allergy Immunol. 104:184-190(1994).
CC   -!- FUNCTION: Catalyzes the hydrolysis of phosphatidylcholine with
CC       phospholipase A1 activity (By similarity). May act as an allergen and
CC       induce hemolytic activity (By similarity).
CC       {ECO:0000250|UniProtKB:P0DMB4, ECO:0000250|UniProtKB:P0DMB7}.
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:0000250|UniProtKB:P0DMB4};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8199462}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:8199462}.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
CC       {ECO:0000250|UniProtKB:A2VBC4}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {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   PIR; A44564; A44564.
DR   AlphaFoldDB; P51528; -.
DR   SMR; P51528; -.
DR   Allergome; 3514; Ves m 1.0101.
DR   Allergome; 661; Ves m 1.
DR   ESTHER; vesmc-ppla1; 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; alpha/beta hydrolase; 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; LIPASE; 1.
DR   Pfam; PF00151; Lipase; 1.
DR   PRINTS; PR00825; DOLALLERGEN.
DR   PRINTS; PR00821; TAGLIPASE.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 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.
FT   CHAIN           1..300
FT                   /note="Phospholipase A1"
FT                   /evidence="ECO:0000269|PubMed:8199462"
FT                   /id="PRO_0000090378"
FT   ACT_SITE        137
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   ACT_SITE        165
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   ACT_SITE        229
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT   DISULFID        4..87
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   DISULFID        176..181
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   DISULFID        219..227
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   DISULFID        244..268
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   DISULFID        245..293
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   DISULFID        261..266
FT                   /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT   VARIANT         97
FT                   /note="A -> M"
FT   VARIANT         191
FT                   /note="I -> P"
FT   VARIANT         202
FT                   /note="I -> L"
SQ   SEQUENCE   300 AA;  33540 MW;  8EE2DE20BD69CCF6 CRC64;
     GPKCPFNSDT VSIIIETREN RNRDLYTLQT LQNHPEFKKK TITRPVVFIT HGFTSSASEK
     NFINLAKALV DKDNYMVISI DWQTAACTNE YPGLKYAYYP TAASNTRLVG QYIATITQKL
     VKDYKISMAN IRLIGHSLGA HVSGFAGKRV QELKLGKYSE IIGLDPARPS FDSNHCSERL
     CETDAEYVQI IHTSNYLGTE KILGTVDFYM NNGKNNPGCG RFFSEVCSHT RAVIYMAECI
     KHECCLIGIP RSKSSQPISR CTKQECVCVG LNAKKYPSRG SFYVPVESTA PFCNNKGKII
//