PA1_VESBA
ID PA1_VESBA Reviewed; 300 AA.
AC A0A0M3KKW3;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 11-NOV-2015, sequence version 1.
DT 25-MAY-2022, entry version 26.
DE RecName: Full=Phospholipase A1 {ECO:0000303|PubMed:26603193};
DE Short=vPLA2 {ECO:0000303|PubMed:26603193};
DE EC=3.1.1.32;
OS Vespa basalis (Hornet).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC Vespidae; Vespinae; Vespa.
OX NCBI_TaxID=7444;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS),
RP 3D-STRUCTURE MODELING IN COMPLEX WITH PHOSPHOLIPID PC, AND DISULFIDE BOND.
RC TISSUE=Venom;
RX PubMed=26603193; DOI=10.1016/j.ibmb.2015.11.002;
RA Hou M.H., Chuang C.Y., Ko T.P., Hu N.J., Chou C.C., Shih Y.P., Ho C.L.,
RA Wang A.H.;
RT "Crystal structure of vespid phospholipase A(1) reveals insights into the
RT mechanism for cause of membrane dysfunction.";
RL Insect Biochem. Mol. Biol. 68:79-88(2016).
RN [2]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=7687388; DOI=10.1016/0041-0101(93)90115-y;
RA Ho C.L., Hwang L.L., Chen C.T.;
RT "Edema-inducing activity of a lethal protein with phospholipase A1 activity
RT isolated from the black-bellied hornet (Vespa basalis) venom.";
RL Toxicon 31:605-613(1993).
CC -!- FUNCTION: Catalyzes the hydrolysis of phosphatidylcholine with
CC phospholipase A1 activity (By similarity). Shows potent hemolytic
CC activity that is responsible for its lethal effect (PubMed:26603193).
CC In vivo, induces local inflammatory effects (PubMed:7687388).
CC {ECO:0000250|UniProtKB:P0DMB4, ECO:0000269|PubMed:7687388,
CC ECO:0000305|PubMed:26603193}.
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 -!- ACTIVITY REGULATION: Local inflammatory effects are inhibited by
CC antiserotonin drugs (cyproheptadine and methysergide), indomethacin,
CC betamethasone, and antihistamine (chlorpheniramine).
CC {ECO:0000269|PubMed:7687388}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7687388}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:7687388}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
CC -!- CAUTION: Nucleotide sequence indicated is deduced from the source
CC 'expression system E.coli' written in PDB 4QNN file.
CC {ECO:0000305|PubMed:26603193}.
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DR PDB; 4QNN; X-ray; 2.50 A; A/B/C/D=1-300.
DR PDBsum; 4QNN; -.
DR AlphaFoldDB; A0A0M3KKW3; -.
DR SMR; A0A0M3KKW3; -.
DR ESTHER; vesba-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:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002334; Allerg_PlipaseA1.
DR InterPro; IPR013818; Lipase.
DR InterPro; IPR000734; TAG_lipase.
DR PANTHER; PTHR11610; PTHR11610; 1.
DR Pfam; PF00151; Lipase; 1.
DR PRINTS; PR00825; DOLALLERGEN.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytolysis; Disulfide bond; Hemolysis; Hydrolase; Secreted.
FT CHAIN 1..300
FT /note="Phospholipase A1"
FT /evidence="ECO:0000305|PubMed:26603193"
FT /id="PRO_0000446188"
FT ACT_SITE 137
FT /note="Nucleophile"
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:0000269|PubMed:26603193,
FT ECO:0000312|PDB:4QNN"
FT DISULFID 176..181
FT /evidence="ECO:0000269|PubMed:26603193,
FT ECO:0000312|PDB:4QNN"
FT DISULFID 218..227
FT /evidence="ECO:0000269|PubMed:26603193,
FT ECO:0000312|PDB:4QNN"
FT DISULFID 244..268
FT /evidence="ECO:0000269|PubMed:26603193,
FT ECO:0000312|PDB:4QNN"
FT DISULFID 245..293
FT /evidence="ECO:0000269|PubMed:26603193,
FT ECO:0000312|PDB:4QNN"
FT DISULFID 261..266
FT /evidence="ECO:0000269|PubMed:26603193,
FT ECO:0000312|PDB:4QNN"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:4QNN"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:4QNN"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:4QNN"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:4QNN"
FT STRAND 44..50
FT /evidence="ECO:0007829|PDB:4QNN"
FT HELIX 60..70
FT /evidence="ECO:0007829|PDB:4QNN"
FT STRAND 73..81
FT /evidence="ECO:0007829|PDB:4QNN"
FT TURN 83..90
FT /evidence="ECO:0007829|PDB:4QNN"
FT HELIX 95..124
FT /evidence="ECO:0007829|PDB:4QNN"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:4QNN"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:4QNN"
FT HELIX 138..152
FT /evidence="ECO:0007829|PDB:4QNN"
FT STRAND 158..165
FT /evidence="ECO:0007829|PDB:4QNN"
FT TURN 169..173
FT /evidence="ECO:0007829|PDB:4QNN"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:4QNN"
FT STRAND 184..192
FT /evidence="ECO:0007829|PDB:4QNN"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:4QNN"
FT STRAND 204..214
FT /evidence="ECO:0007829|PDB:4QNN"
FT TURN 221..224
FT /evidence="ECO:0007829|PDB:4QNN"
FT HELIX 225..241
FT /evidence="ECO:0007829|PDB:4QNN"
FT STRAND 245..250
FT /evidence="ECO:0007829|PDB:4QNN"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:4QNN"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:4QNN"
FT STRAND 280..283
FT /evidence="ECO:0007829|PDB:4QNN"
SQ SEQUENCE 300 AA; 33185 MW; ABBF64ED381DB849 CRC64;
FNPCPYSDDT VKMIILTREN KKHDFYTLDT IKKHNEFKKS TIKHQVVFIT HGFTSSADTE
NFLAMAKALS DKGNYLVILI DWRVAACTEE MSGIQLAYYS YAASNTRLVG NYIATVTKML
VQKYNVPMAN IRLIGHSLGA HTSGFAGKKV QELGLGKYSE IIGLDPAGPS FKSNDCSERI
CKTDAHYVQI IHTSNHLGTL VTLGTVDFMN NGYNQPGCGL PLIGETCSHT RAVKYFTECI
KHECCLIGVP QSKKPQPVSK CTRNECVCVG LNAKTYPKTG SFYVPVESKA PYCNNKGKII
