PA11_DOLMA
ID PA11_DOLMA Reviewed; 317 AA.
AC Q06478;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Phospholipase A1 1 {ECO:0000303|PubMed:8458431};
DE EC=3.1.1.32 {ECO:0000305|PubMed:8458431};
DE EC=3.1.1.4 {ECO:0000305|PubMed:8458431};
DE AltName: Full=Allergen Dol m I {ECO:0000303|PubMed:8458431};
DE AltName: Allergen=Dol m 1 {ECO:0000305};
DE Flags: Precursor; Fragment;
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 NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom, and Venom gland;
RX PubMed=8458431; DOI=10.1016/0014-5793(93)80080-e;
RA Soldatova L., Kochoumian L., King T.P.;
RT "Sequence similarity of a hornet (D. maculata) venom allergen phospholipase
RT A1 with mammalian lipases.";
RL FEBS Lett. 320:145-149(1993).
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:8458431}.
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:8458431};
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:8458431};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=280 umol/min/mg enzyme toward egg yolk
CC {ECO:0000269|PubMed:8458431};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8458431}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:8458431}.
CC -!- ALLERGEN: Causes an allergic reaction in human.
CC {ECO:0000305|PubMed:8458431}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; X66869; CAA47341.1; -; mRNA.
DR PIR; S32406; S32406.
DR AlphaFoldDB; Q06478; -.
DR SMR; Q06478; -.
DR Allergome; 1667; Dol m 1.0101.
DR Allergome; 328; Dol m 1.
DR ESTHER; dolma-ppla1; Insect_Phospholipase.
DR iPTMnet; Q06478; -.
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 SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 1: Evidence at protein level;
KW Allergen; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hydrolase; Lipid degradation; Lipid metabolism; Secreted; Signal.
FT SIGNAL <1..7
FT /evidence="ECO:0000255"
FT PROPEP 8..17
FT /evidence="ECO:0000305|PubMed:8458431"
FT /id="PRO_0000425186"
FT CHAIN 18..317
FT /note="Phospholipase A1 1"
FT /evidence="ECO:0000269|PubMed:8458431"
FT /id="PRO_0000017812"
FT ACT_SITE 154
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT ACT_SITE 182
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 246
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:8458431"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 21..104
FT /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT DISULFID 193..198
FT /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT DISULFID 236..244
FT /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT DISULFID 261..285
FT /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT DISULFID 262..310
FT /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT DISULFID 278..283
FT /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT VARIANT 271
FT /note="N -> S"
FT /evidence="ECO:0000269|PubMed:8458431"
FT NON_TER 1
SQ SEQUENCE 317 AA; 35708 MW; 0B2135FD453512D9 CRC64;
RLIMFVGDPS SSNELDRFSV CPFSNDTVKM IFLTRENRKH DFYTLDTMNR HNEFKKSIIK
RPVVFITHGF TSSATEKNFV AMSEALMHTG DFLIIMVDWR MAACTDEYPG LKYMFYKAAV
GNTRLVGNFI AMIAKKLVEQ YKVPMTNIRL VGHSLGAHIS GFAGKRVQEL KLGKFSEIIG
LDPAGPSFKK NDCSERICET DAHYVQILHT SSNLGTERTL GTVDFYINNG SNQPGCRYII
GETCSHTRAV KYFTECIRRE CCLIGVPQSK NPQPVSKCTR NECVCVGLNA KKYPKRGSFY
VPVEAEAPYC NNNGKII
