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   25-MAY-2022, entry version 10.
DE   RecName: Full=Phospholipase A1 {ECO:0000250|UniProtKB:Q68KK0};
DE            EC=3.1.1.32 {ECO:0000250|UniProtKB:Q68KK0};
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. Shows hemolytic activity.
CC       {ECO:0000250|UniProtKB:Q68KK0}.
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:Q68KK0};
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   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:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR013818; Lipase.
DR   InterPro; IPR000734; TAG_lipase.
DR   PANTHER; PTHR11610; PTHR11610; 1.
DR   Pfam; PF00151; Lipase; 1.
DR   SUPFAM; SSF53474; SSF53474; 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"
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