PA2_APIME
ID PA2_APIME Reviewed; 167 AA.
AC P00630; A5JGM7; Q8WPH5;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2002, sequence version 3.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Phospholipase A2;
DE Short=bvPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Allergen Api m I;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE AltName: Allergen=Api m 1;
DE Flags: Precursor;
OS Apis mellifera (Honeybee).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea; Apidae;
OC Apis.
OX NCBI_TaxID=7460;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=12167627; DOI=10.1074/jbc.m206647200;
RA Moreira L.A., Ito J., Ghosh A., Devenport M., Zieler H., Abraham E.G.,
RA Crisanti A., Nolan T., Catteruccia F., Jacobs-Lorena M.;
RT "Bee venom phospholipase inhibits malaria parasite development in
RT transgenic mosquitoes.";
RL J. Biol. Chem. 277:40839-40843(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Venom gland;
RX PubMed=17466468; DOI=10.1016/j.gene.2007.03.007;
RA Valdez-Cruz N.A., Segovia L., Corona M., Possani L.D.;
RT "Sequence analysis and phylogenetic relationship of genes encoding
RT heterodimeric phospholipases A2 from the venom of the scorpion Anuroctonus
RT phaiodactylus.";
RL Gene 396:149-158(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-167.
RC TISSUE=Venom gland;
RX PubMed=2776767; DOI=10.1111/j.1432-1033.1989.tb15014.x;
RA Kuchler K., Gmachl M., Sippl M.J., Kreil G.;
RT "Analysis of the cDNA for phospholipase A2 from honeybee venom glands. The
RT deduced amino acid sequence reveals homology to the corresponding
RT vertebrate enzymes.";
RL Eur. J. Biochem. 184:249-254(1989).
RN [4]
RP PROTEIN SEQUENCE OF 34-167.
RC TISSUE=Venom;
RX PubMed=4448181; DOI=10.1111/j.1432-1033.1974.tb03787.x;
RA Shipolini R.A., Callewaert G.L., Cottrell R.C., Vernon C.A.;
RT "The amino-acid sequence and carbohydrate content of phospholipase A2 from
RT bee venom.";
RL Eur. J. Biochem. 48:465-476(1974).
RN [5]
RP PROTEIN SEQUENCE OF 34-60, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP SEASONAL VARIATION.
RX PubMed=20403370; DOI=10.1016/j.toxicon.2010.03.023;
RA Ferreira Junior R.S., Sciani J.M., Marques-Porto R., Junior A.L.,
RA Orsi R.D., Barraviera B., Pimenta D.C.;
RT "Africanized honey bee (Apis mellifera) venom profiling: Seasonal variation
RT of melittin and phospholipase A(2) levels.";
RL Toxicon 56:355-362(2010).
RN [6]
RP DISULFIDE BONDS.
RX PubMed=4614976; DOI=10.1111/j.1432-1033.1974.tb03788.x;
RA Shipolini R.A., Doonan S., Vernon C.A.;
RT "The disulphide bridges of phospholipase A2 from bee venom.";
RL Eur. J. Biochem. 48:477-483(1974).
RN [7]
RP GLYCOSYLATION.
RX PubMed=8504812; DOI=10.1111/j.1432-1033.1993.tb17870.x;
RA Kubelka V., Altmann F., Staudacher E., Tretter V., Marz L., Hard K.,
RA Kamerling J.P., Vliegenthart J.F.;
RT "Primary structures of the N-linked carbohydrate chains from honeybee venom
RT phospholipase A2.";
RL Eur. J. Biochem. 213:1193-1204(1993).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 34-167 IN COMPLEX WITH CALCIUM
RP ION, COFACTOR, AND DISULFIDE BONDS.
RX PubMed=2274788; DOI=10.1126/science.2274788;
RA Scott D.L., Otwinowski Z., Gelb M.H., Sigler P.B.;
RT "Crystal structure of bee-venom phospholipase A2 in a complex with a
RT transition-state analogue.";
RL Science 250:1563-1566(1990).
CC -!- FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC groups in 3-sn-phosphoglycerides.
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:0000255|PROSITE-ProRule:PRU10035};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000305|PubMed:2274788};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000305|PubMed:2274788};
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- PTM: N-glycosylated; contains mannose, N-acetylglucosamine and fucose
CC alphal-6 and/or alphal-3 linked to the innermost N-acetylglucosamine.
CC {ECO:0000269|PubMed:8504812}.
CC -!- ALLERGEN: Causes an allergic reaction in human.
CC -!- MISCELLANEOUS: The secretion of this protein into venom follows a
CC seasonal pattern. This variation is synchronized with melittin
CC variation, i.e. their production increase in the same months.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group III
CC subfamily. {ECO:0000305}.
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DR EMBL; AF438408; AAL30844.1; -; mRNA.
DR EMBL; EF373554; ABQ28728.1; -; Genomic_DNA.
DR EMBL; X16709; CAA34681.1; -; mRNA.
DR PIR; S05650; PSHBA.
DR RefSeq; NP_001011614.1; NM_001011614.1.
DR PDB; 1POC; X-ray; 2.00 A; A=34-167.
DR PDBsum; 1POC; -.
DR AlphaFoldDB; P00630; -.
DR SMR; P00630; -.
DR STRING; 7460.GB48228-PA; -.
DR BindingDB; P00630; -.
DR ChEMBL; CHEMBL4807; -.
DR Allergome; 2493; Api m A1-A2.
DR Allergome; 2778; Api m A1-A2-A3.
DR Allergome; 3088; Api m 1.0101.
DR Allergome; 45; Api m 1.
DR GlyConnect; 496; 16 N-Linked glycans (1 site).
DR PaxDb; P00630; -.
DR EnsemblMetazoa; NM_001011614; NP_001011614; GeneID_406141.
DR GeneID; 406141; -.
DR KEGG; ame:406141; -.
DR CTD; 406141; -.
DR eggNOG; ENOG502S1MS; Eukaryota.
DR HOGENOM; CLU_118255_0_0_1; -.
DR InParanoid; P00630; -.
DR OMA; TTGCKEY; -.
DR OrthoDB; 1422829at2759; -.
DR PhylomeDB; P00630; -.
DR BRENDA; 3.1.1.4; 387.
DR EvolutionaryTrace; P00630; -.
DR PRO; PR:P00630; -.
DR Proteomes; UP000005203; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR Gene3D; 1.20.90.10; -; 1.
DR InterPro; IPR016090; PLipase_A2_dom.
DR InterPro; IPR036444; PLipase_A2_dom_sf.
DR InterPro; IPR033113; PLipase_A2_His_AS.
DR Pfam; PF05826; Phospholip_A2_2; 1.
DR SMART; SM00085; PA2c; 1.
DR SUPFAM; SSF48619; SSF48619; 1.
DR PROSITE; PS00118; PA2_HIS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allergen; Calcium; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism;
KW Metal-binding; Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..33
FT /evidence="ECO:0000269|PubMed:20403370,
FT ECO:0000269|PubMed:4448181"
FT /id="PRO_0000022982"
FT CHAIN 34..167
FT /note="Phospholipase A2"
FT /evidence="ECO:0000269|PubMed:2274788"
FT /id="PRO_0000022983"
FT ACT_SITE 67
FT /evidence="ECO:0000305|PubMed:2274788"
FT ACT_SITE 97
FT /evidence="ECO:0000305|PubMed:2274788"
FT BINDING 41
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:2274788,
FT ECO:0007744|PDB:1POC"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:2274788,
FT ECO:0007744|PDB:1POC"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:2274788,
FT ECO:0007744|PDB:1POC"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:2274788,
FT ECO:0007744|PDB:1POC"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:8504812"
FT /id="CAR_000001"
FT DISULFID 42..64
FT /evidence="ECO:0000269|PubMed:2274788,
FT ECO:0000269|PubMed:4614976"
FT DISULFID 63..103
FT /evidence="ECO:0000269|PubMed:2274788,
FT ECO:0000269|PubMed:4614976"
FT DISULFID 70..96
FT /evidence="ECO:0000269|PubMed:2274788,
FT ECO:0000269|PubMed:4614976"
FT DISULFID 94..128
FT /evidence="ECO:0000269|PubMed:2274788,
FT ECO:0000269|PubMed:4614976"
FT DISULFID 138..146
FT /evidence="ECO:0000269|PubMed:2274788,
FT ECO:0000269|PubMed:4614976"
FT CONFLICT 72
FT /note="D -> N (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="N -> D (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 89..90
FT /note="Missing (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 95..99
FT /note="DCDDK -> NNND (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 102..104
FT /note="Missing (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="D -> N (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:1POC"
FT HELIX 58..68
FT /evidence="ECO:0007829|PDB:1POC"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:1POC"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:1POC"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:1POC"
FT HELIX 94..105
FT /evidence="ECO:0007829|PDB:1POC"
FT HELIX 110..122
FT /evidence="ECO:0007829|PDB:1POC"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:1POC"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:1POC"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:1POC"
SQ SEQUENCE 167 AA; 19058 MW; 88D5086A0E47DCC1 CRC64;
MQVVLGSLFL LLLSTSHGWQ IRDRIGDNEL EERIIYPGTL WCGHGNKSSG PNELGRFKHT
DACCRTHDMC PDVMSAGESK HGLTNTASHT RLSCDCDDKF YDCLKNSADT ISSYFVGKMY
FNLIDTKCYK LEHPVTGCGE RTEGRCLHYT VDKSKPKVYQ WFDLRKY