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Phospholipase A2 (bvPLA2) (EC 3.1.1.4) (Allergen Api m I) (Phosphatidylcholine 2-acylhydrolase) (allergen Api m 1)

 PA2_APIME               Reviewed;         167 AA.
P00630; A5JGM7; Q8WPH5;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
25-OCT-2002, sequence version 3.
23-MAY-2018, entry version 155.
RecName: Full=Phospholipase A2;
Short=bvPLA2;
EC=3.1.1.4;
AltName: Full=Allergen Api m I;
AltName: Full=Phosphatidylcholine 2-acylhydrolase;
AltName: Allergen=Api m 1;
Flags: Precursor;
Apis mellifera (Honeybee).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Hymenoptera; Apocrita; Aculeata;
Apoidea; Apidae; Apis.
NCBI_TaxID=7460;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Venom gland;
PubMed=12167627; DOI=10.1074/jbc.M206647200;
Moreira L.A., Ito J., Ghosh A., Devenport M., Zieler H., Abraham E.G.,
Crisanti A., Nolan T., Catteruccia F., Jacobs-Lorena M.;
"Bee venom phospholipase inhibits malaria parasite development in
transgenic mosquitoes.";
J. Biol. Chem. 277:40839-40843(2002).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Venom gland;
PubMed=17466468; DOI=10.1016/j.gene.2007.03.007;
Valdez-Cruz N.A., Segovia L., Corona M., Possani L.D.;
"Sequence analysis and phylogenetic relationship of genes encoding
heterodimeric phospholipases A2 from the venom of the scorpion
Anuroctonus phaiodactylus.";
Gene 396:149-158(2007).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 6-167.
TISSUE=Venom gland;
PubMed=2776767; DOI=10.1111/j.1432-1033.1989.tb15014.x;
Kuchler K., Gmachl M., Sippl M.J., Kreil G.;
"Analysis of the cDNA for phospholipase A2 from honeybee venom glands.
The deduced amino acid sequence reveals homology to the corresponding
vertebrate enzymes.";
Eur. J. Biochem. 184:249-254(1989).
[4]
PROTEIN SEQUENCE OF 34-167.
TISSUE=Venom;
PubMed=4448181; DOI=10.1111/j.1432-1033.1974.tb03787.x;
Shipolini R.A., Callewaert G.L., Cottrell R.C., Vernon C.A.;
"The amino-acid sequence and carbohydrate content of phospholipase A2
from bee venom.";
Eur. J. Biochem. 48:465-476(1974).
[5]
PROTEIN SEQUENCE OF 34-60, IDENTIFICATION BY MASS SPECTROMETRY, AND
SEASONAL VARIATION.
PubMed=20403370; DOI=10.1016/j.toxicon.2010.03.023;
Ferreira Junior R.S., Sciani J.M., Marques-Porto R., Junior A.L.,
Orsi R.D., Barraviera B., Pimenta D.C.;
"Africanized honey bee (Apis mellifera) venom profiling: Seasonal
variation of melittin and phospholipase A(2) levels.";
Toxicon 56:355-362(2010).
[6]
DISULFIDE BONDS.
PubMed=4614976; DOI=10.1111/j.1432-1033.1974.tb03788.x;
Shipolini R.A., Doonan S., Vernon C.A.;
"The disulphide bridges of phospholipase A2 from bee venom.";
Eur. J. Biochem. 48:477-483(1974).
[7]
GLYCOSYLATION.
PubMed=8504812; DOI=10.1111/j.1432-1033.1993.tb17870.x;
Kubelka V., Altmann F., Staudacher E., Tretter V., Marz L., Hard K.,
Kamerling J.P., Vliegenthart J.F.;
"Primary structures of the N-linked carbohydrate chains from honeybee
venom phospholipase A2.";
Eur. J. Biochem. 213:1193-1204(1993).
[8]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 34-167 IN COMPLEX WITH
CALCIUM ION, COFACTOR, AND DISULFIDE BONDS.
PubMed=2274788; DOI=10.1126/science.2274788;
Scott D.L., Otwinowski Z., Gelb M.H., Sigler P.B.;
"Crystal structure of bee-venom phospholipase A2 in a complex with a
transition-state analogue.";
Science 250:1563-1566(1990).
-!- FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the
2-acyl groups in 3-sn-phosphoglycerides.
-!- CATALYTIC ACTIVITY: Phosphatidylcholine + H(2)O = 1-
acylglycerophosphocholine + a carboxylate. {ECO:0000255|PROSITE-
ProRule:PRU10035}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000305|PubMed:2274788};
Note=Binds 1 Ca(2+) ion. {ECO:0000305|PubMed:2274788};
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
-!- PTM: N-glycosylated; contains mannose, N-acetylglucosamine and
fucose alphal-6 and/or alphal-3 linked to the innermost N-
acetylglucosamine. {ECO:0000269|PubMed:8504812}.
-!- ALLERGEN: Causes an allergic reaction in human.
-!- MISCELLANEOUS: The secretion of this protein into venom follows a
seasonal pattern. This variation is synchronized with melittin
variation, i.e. their production increase in the same months.
-!- SIMILARITY: Belongs to the phospholipase A2 family. Group III
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF438408; AAL30844.1; -; mRNA.
EMBL; EF373554; ABQ28728.1; -; Genomic_DNA.
EMBL; X16709; CAA34681.1; -; mRNA.
PIR; S05650; PSHBA.
RefSeq; NP_001011614.1; NM_001011614.1.
UniGene; Ame.2; -.
PDB; 1POC; X-ray; 2.00 A; A=34-167.
PDBsum; 1POC; -.
ProteinModelPortal; P00630; -.
SMR; P00630; -.
STRING; 7460.GB13351-PA; -.
BindingDB; P00630; -.
ChEMBL; CHEMBL4807; -.
Allergome; 2493; Api m A1-A2.
Allergome; 2778; Api m A1-A2-A3.
Allergome; 3088; Api m 1.0101.
Allergome; 45; Api m 1.
GlyConnect; 496; -.
UniCarbKB; P00630; -.
PaxDb; P00630; -.
PRIDE; P00630; -.
EnsemblMetazoa; GB48228-RA; GB48228-PA; GB48228.
GeneID; 406141; -.
KEGG; ame:406141; -.
CTD; 406141; -.
eggNOG; ENOG410J1W3; Eukaryota.
eggNOG; ENOG410YVBF; LUCA.
HOGENOM; HOG000143527; -.
InParanoid; P00630; -.
KO; K01047; -.
OMA; TRLHCKC; -.
PhylomeDB; P00630; -.
BRENDA; 3.1.1.4; 387.
EvolutionaryTrace; P00630; -.
PRO; PR:P00630; -.
Proteomes; UP000005203; Linkage group 13.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
GO; GO:0102567; F:phospholipase A2 activity (consuming 1,2-dipalmitoylphosphatidylcholine); IEA:UniProtKB-EC.
GO; GO:0102568; F:phospholipase A2 activity consuming 1,2-dioleoylphosphatidylethanolamine); IEA:UniProtKB-EC.
GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
Gene3D; 1.20.90.10; -; 1.
InterPro; IPR016090; PLipase_A2_dom.
InterPro; IPR036444; PLipase_A2_dom_sf.
InterPro; IPR033113; PLipase_A2_His_AS.
Pfam; PF05826; Phospholip_A2_2; 1.
SMART; SM00085; PA2c; 1.
SUPFAM; SSF48619; SSF48619; 1.
PROSITE; PS00118; PA2_HIS; 1.
1: Evidence at protein level;
3D-structure; Allergen; Calcium; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
Lipid degradation; Lipid metabolism; Metal-binding;
Reference proteome; Secreted; Signal.
SIGNAL 1 18 {ECO:0000255}.
PROPEP 19 33 {ECO:0000269|PubMed:20403370,
ECO:0000269|PubMed:4448181}.
/FTId=PRO_0000022982.
CHAIN 34 167 Phospholipase A2.
{ECO:0000269|PubMed:2274788}.
/FTId=PRO_0000022983.
ACT_SITE 67 67 {ECO:0000305|PubMed:2274788}.
ACT_SITE 97 97 {ECO:0000305|PubMed:2274788}.
METAL 41 41 Calcium; via carbonyl oxygen.
{ECO:0000244|PDB:1POC,
ECO:0000269|PubMed:2274788}.
METAL 43 43 Calcium; via carbonyl oxygen.
{ECO:0000244|PDB:1POC,
ECO:0000269|PubMed:2274788}.
METAL 45 45 Calcium; via carbonyl oxygen.
{ECO:0000244|PDB:1POC,
ECO:0000269|PubMed:2274788}.
METAL 68 68 Calcium. {ECO:0000244|PDB:1POC,
ECO:0000269|PubMed:2274788}.
CARBOHYD 46 46 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:8504812}.
/FTId=CAR_000001.
DISULFID 42 64 {ECO:0000269|PubMed:2274788,
ECO:0000269|PubMed:4614976}.
DISULFID 63 103 {ECO:0000269|PubMed:2274788,
ECO:0000269|PubMed:4614976}.
DISULFID 70 96 {ECO:0000269|PubMed:2274788,
ECO:0000269|PubMed:4614976}.
DISULFID 94 128 {ECO:0000269|PubMed:2274788,
ECO:0000269|PubMed:4614976}.
DISULFID 138 146 {ECO:0000269|PubMed:2274788,
ECO:0000269|PubMed:4614976}.
CONFLICT 72 72 D -> N (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 85 85 N -> D (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 89 90 Missing (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 95 99 DCDDK -> NNND (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 102 104 Missing (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 125 125 D -> N (in Ref. 4; AA sequence).
{ECO:0000305}.
STRAND 40 45 {ECO:0000244|PDB:1POC}.
HELIX 58 68 {ECO:0000244|PDB:1POC}.
STRAND 71 74 {ECO:0000244|PDB:1POC}.
STRAND 87 89 {ECO:0000244|PDB:1POC}.
STRAND 91 93 {ECO:0000244|PDB:1POC}.
HELIX 94 105 {ECO:0000244|PDB:1POC}.
HELIX 110 122 {ECO:0000244|PDB:1POC}.
STRAND 128 133 {ECO:0000244|PDB:1POC}.
STRAND 135 137 {ECO:0000244|PDB:1POC}.
STRAND 158 162 {ECO:0000244|PDB:1POC}.
SEQUENCE 167 AA; 19058 MW; 88D5086A0E47DCC1 CRC64;
MQVVLGSLFL LLLSTSHGWQ IRDRIGDNEL EERIIYPGTL WCGHGNKSSG PNELGRFKHT
DACCRTHDMC PDVMSAGESK HGLTNTASHT RLSCDCDDKF YDCLKNSADT ISSYFVGKMY
FNLIDTKCYK LEHPVTGCGE RTEGRCLHYT VDKSKPKVYQ WFDLRKY


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