PA12_DOLMA
ID PA12_DOLMA Reviewed; 303 AA.
AC P53357;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Phospholipase A1 2;
DE EC=3.1.1.32 {ECO:0000305|PubMed:8199462};
DE EC=3.1.1.4 {ECO:0000305|PubMed:8199462};
DE AltName: Full=Allergen Dol m 1 {ECO:0000303|PubMed:8199462};
DE AltName: Allergen=Dol m 1 {ECO:0000303|PubMed:8199462};
OS Dolichovespula maculata (Bald-faced hornet) (Vespula maculata).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC Vespidae; Vespinae; Dolichovespula.
OX NCBI_TaxID=7441;
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; A44563; A44563.
DR AlphaFoldDB; P53357; -.
DR SMR; P53357; -.
DR Allergome; 1668; Dol m 1.02.
DR Allergome; 328; Dol m 1.
DR ESTHER; dolma-ppla12; 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..303
FT /note="Phospholipase A1 2"
FT /id="PRO_0000090375"
FT ACT_SITE 140
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT ACT_SITE 168
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 232
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT DISULFID 6..90
FT /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT DISULFID 179..184
FT /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT DISULFID 247..271
FT /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT DISULFID 248..296
FT /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT DISULFID 264..269
FT /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT VARIANT 55
FT /note="G -> E"
FT VARIANT 295
FT /note="F -> Y"
SQ SEQUENCE 303 AA; 33782 MW; 85816A837C0F3AF8 CRC64;
GILPECKLVP EEISFVLSTR ENRDGVYLTL QKLKNGKMFK NSDLSSKKVP FLIHGFISSA
TNKNYADMTR ALLDKDDIMV ISIDWRDGAC SNEFALLKFI GYPKAVENTR AVGKYIADFS
KILIQKYKVL LENIRLIGHS LGAQIAGFAG KEFQRFKLGK YPEIIGLDPA GPSFKKKDCP
ERICETDAHY VQILHTSSNL GTERTLGTVD FYINDGSNQP GCTYIIGETC SHTRAVKYLT
ECIRRECCLI GVPQSKNPQP VSKCTRNECV CVGLNAKEYP KKGSFYVPVE AKAPFCNNNG
KII
