PA1_POLPI
ID PA1_POLPI Reviewed; 322 AA.
AC A2VBC4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=Phospholipase A1 {ECO:0000303|PubMed:17761205};
DE EC=3.1.1.32 {ECO:0000269|PubMed:17761205};
DE AltName: Allergen=Poly p 1 {ECO:0000303|PubMed:17761205};
DE Flags: Precursor;
OS Polybia paulista (Neotropical social wasp) (Swarm-founding polistine wasp).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC Vespidae; Polistinae; Epiponini; Polybia.
OX NCBI_TaxID=291283;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Santos L.D., Santos K.S., de Souza B.M., Neto E.C., Castro F.M.,
RA Kalil J.E., Palma M.S.;
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Santos L.D.;
RT "Proteomic analysis of immunodominant allergens from the venom of the
RT social wasp Polybia paulista.";
RL Thesis (2007), Sao Paulo State University (UNESP), Brazil.
RN [3]
RP PROTEIN SEQUENCE OF 19-322, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MASS
RP SPECTROMETRY, ALLERGEN, AND 3D-STRUCTURE MODELING.
RC TISSUE=Venom;
RX PubMed=17761205; DOI=10.1016/j.toxicon.2007.06.027;
RA Santos L.D., Santos K.S., de Souza B.M., Arcuri H.A., Cunha-Neto E.,
RA Castro F.M., Kalil J.E., Palma M.S.;
RT "Purification, sequencing and structural characterization of the
RT phospholipase A(1) from the venom of the social wasp Polybia paulista
RT (Hymenoptera, Vespidae).";
RL Toxicon 50:923-937(2007).
CC -!- FUNCTION: Catalyzes the hydrolysis of phosphatidylcholine with
CC phospholipase A1 (EC 3.1.1.32) activity (PubMed:17761205). Shows
CC hemolytic activity (PubMed:17761205). {ECO:0000269|PubMed:17761205}.
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:0000269|PubMed:17761205};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17761205}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:17761205}.
CC -!- PTM: Contains six disulfide bonds. {ECO:0000269|PubMed:17761205}.
CC -!- PTM: Is not glycosylated. {ECO:0000269|PubMed:17761205}.
CC -!- MASS SPECTROMETRY: Mass=33961; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:17761205};
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
CC {ECO:0000269|PubMed:17761205}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; EF101736; ABN13879.1; -; mRNA.
DR EMBL; AM491805; CAM33429.1; -; mRNA.
DR AlphaFoldDB; A2VBC4; -.
DR SMR; A2VBC4; -.
DR Allergome; 3608; Poly p 1.
DR Allergome; 3609; Poly p 1.0101.
DR ESTHER; polpi-pa1; Insect_Phospholipase.
DR BRENDA; 3.1.1.32; 9385.
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 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; Cytolysis; Direct protein sequencing; Disulfide bond; Hemolysis;
KW Hydrolase; Lipid degradation; Lipid metabolism; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:17761205"
FT CHAIN 19..322
FT /note="Phospholipase A1"
FT /evidence="ECO:0000269|PubMed:17761205"
FT /id="PRO_5000223755"
FT ACT_SITE 156
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT ACT_SITE 184
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 248
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT DISULFID 23..106
FT /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT DISULFID 195..200
FT /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT DISULFID 238..246
FT /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT DISULFID 263..290
FT /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT DISULFID 264..315
FT /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
FT DISULFID 283..288
FT /evidence="ECO:0000250|UniProtKB:A0A0M3KKW3"
SQ SEQUENCE 322 AA; 36082 MW; 64A39D6D33AD86A8 CRC64;
MNFKYSILFI CFGTLDRGLI PECPFNEYDI LFFVYTRQQR DGIVLTEETL QNYDLFKKST
ISRQVVFIDH GFLSNGNNEN FIAMAKALIE KDNFLVISVD WKKGACNAFA STLDYLGYST
AVGNTRHVGK YVADFTKLLV EQYKVSMSNI RLIGHSLGAH TSGFAGKEVQ ELKLNKYSNI
DGLDPAGPSF DSNDCPERLC ETDAEYVQII HTSNILGVYS KIGTVDFYMN YGSHQPGCGR
FFSPSCSHTK AVKYLTECIK HECCLIGTPW KKYFSTPKPI SQCTKDTCVC VGLNAKSYPA
RGSFYVPVEA TAPYCHNEGI KL
