ID PA1_DINQU Reviewed; 379 AA.
AC P0DSI2;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Phospholipase A1 {ECO:0000250|UniProtKB:Q68KK0};
DE Short=PLA1 {ECO:0000250|UniProtKB:Q68KK0};
DE EC=3.1.1.32 {ECO:0000250|UniProtKB:P0DMB4};
DE AltName: Full=Venom allergen 1 {ECO:0000250|UniProtKB:Q68KK0};
DE Flags: Precursor;
OS Dinoponera quadriceps (South American ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Ponerinae; Ponerini; Dinoponera.
OX NCBI_TaxID=609295;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=24498135; DOI=10.1371/journal.pone.0087556;
RA Torres A.F., Huang C., Chong C.M., Leung S.W., Prieto-da-Silva A.R.,
RA Havt A., Quinet Y.P., Martins A.M., Lee S.M., Radis-Baptista G.;
RT "Transcriptome analysis in venom gland of the predatory giant ant
RT Dinoponera quadriceps: insights into the polypeptide toxin arsenal of
RT hymenopterans.";
RL PLoS ONE 9:E87556-E87556(2014).
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:0000305|PubMed:24498135}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:24498135}.
CC -!- PTM: Contains five disulfide bonds. {ECO:0000305}.
CC -!- ALLERGEN: Causes an allergic reaction in human.
CC {ECO:0000250|UniProtKB:Q68KK0}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=National Center for Biotechnology Information
CC (NCBI);
CC URL="https://www.ncbi.nlm.nih.gov/nuccore/GANS01000019";
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DR AlphaFoldDB; P0DSI2; -.
DR SMR; P0DSI2; -.
DR ESTHER; dinqu-pa1; Insect_Phospholipase.
DR Proteomes; UP000515204; Unplaced.
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:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013818; Lipase.
DR InterPro; IPR000734; TAG_lipase.
DR PANTHER; PTHR11610:SF184; LD47264P; 1.
DR PANTHER; PTHR11610; LIPASE; 1.
DR Pfam; PF00151; Lipase; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 2: Evidence at transcript level;
KW Allergen; Cytolysis; Disulfide bond; Glycoprotein; Hemolysis; Hydrolase;
KW Lipid degradation; Lipid metabolism; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..73
FT /evidence="ECO:0000250|UniProtKB:Q68KK0"
FT /id="PRO_0000447046"
FT CHAIN 74..379
FT /note="Phospholipase A1"
FT /evidence="ECO:0000250|UniProtKB:Q68KK0"
FT /id="PRO_0000447047"
FT ACT_SITE 204
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT ACT_SITE 232
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 293
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 76..154
FT /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT DISULFID 243..248
FT /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT DISULFID 285..291
FT /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
SQ SEQUENCE 379 AA; 42135 MW; 6E93258A253B41A1 CRC64;
MKFITAILVI FCVYLLSTAG DSKILPLKKL PSKIFGHLKS HVDNTVKKPL KVFGHLKSHV
ENSVGPLRMN KLTPNCIFGV KSMSMVLFTK NIPDGKYISL DSDLGRDLDL TKTIYFTAHG
FISNVNHSLS NRLSRALVEK DYTVFSLDWS DAACTTGGLP LVKLLGYPSA VQNTREIGNL
MADYVMSLID HGASLRNMAF IGHSLGSHVC GFASKKIYES GYGKVPLLFA ADPAQPLFQL
KQCPDRLCDT DAKLVITLHT SQIGLGYPIG GLDLYFNGGF VQPKCHLDIT CAHIRSVLYL
INMVEKKCSF PGIPATYKQI LNPFSKFPYP NSKTTDCFVM DDSIFNPRRK SLQNLAGGIY
YMFVDPDTFC TRKNFNCQR
//
