PA1_VESMC
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 25-MAY-2022, entry version 87.
DE RecName: Full=Phospholipase A1 {ECO:0000305|PubMed:8199462};
DE EC=3.1.1.32 {ECO:0000305|PubMed:8199462};
DE EC=3.1.1.4 {ECO:0000305|PubMed:8199462};
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 (EC 3.1.1.32) and phospholipase A2 (EC 3.1.1.4)
CC activities. Shows hemolytic activity (By similarity).
CC {ECO:0000250|UniProtKB:P0DMB7, ECO:0000305|PubMed:8199462}.
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:8199462};
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:8199462};
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}.
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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; -; 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 PRINTS; PR00821; TAGLIPASE.
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.
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
