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Basic phospholipase A2 RV-4 (svPLA2) (EC 3.1.1.4) (F4) (Phosphatidylcholine 2-acylhydrolase) (S2) (Viperotoxin F) (Viperotoxin toxic basic component)

 PA2B4_DABSI             Reviewed;         138 AA.
Q02471;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 1.
23-MAY-2018, entry version 107.
RecName: Full=Basic phospholipase A2 RV-4;
Short=svPLA2;
EC=3.1.1.4;
AltName: Full=F4;
AltName: Full=Phosphatidylcholine 2-acylhydrolase;
AltName: Full=S2;
AltName: Full=Viperotoxin F;
AltName: Full=Viperotoxin toxic basic component;
Flags: Precursor;
Daboia siamensis (Eastern Russel's viper) (Daboia russelii siamensis).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Viperidae; Viperinae; Daboia.
NCBI_TaxID=343250;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-66, AND FUNCTION.
TISSUE=Venom, and Venom gland;
PubMed=1425670; DOI=10.1111/j.1432-1033.1992.tb17330.x;
Wang Y.-M., Lu P.-J., Ho C.-L., Tsai I.-H.;
"Characterization and molecular cloning of neurotoxic phospholipases
A2 from Taiwan viper (Vipera russelli formosensis).";
Eur. J. Biochem. 209:635-641(1992).
[2]
PROTEIN SEQUENCE OF 17-66, FUNCTION, AND LETHAL DOSE.
TISSUE=Venom;
PubMed=8835338; DOI=10.1016/0041-0101(95)00114-X;
Tsai I.-H., Lu P.-J., Su J.-C.;
"Two types of Russell's viper revealed by variation in phospholipases
A2 from venom of the subspecies.";
Toxicon 34:99-109(1996).
[3]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 17-138, AND DISULFIDE BONDS.
TISSUE=Venom;
PubMed=14501106; DOI=10.1107/S0907444903014987;
Perbandt M., Tsai I.-H., Fuchs A., Banumathi S., Rajashankar K.R.,
Georgieva D., Kalkura N., Singh T.P., Genov N., Betzel C.;
"Structure of the heterodimeric neurotoxic complex viperotoxin F (RV-
4/RV-7) from the venom of Vipera russelli formosensis at 1.9 A
resolution.";
Acta Crystallogr. D 59:1679-1687(2003).
-!- FUNCTION: Heterodimer RV-4/RV-7: acts as a presynaptic neurotoxin.
-!- FUNCTION: Monomer: snake venom phospholipase A2 (PLA2) that acts
as a presynaptic neurotoxin. 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, ECO:0000255|PROSITE-ProRule:PRU10036}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
Note=Binds 1 Ca(2+) ion. {ECO:0000250};
-!- SUBUNIT: Heterodimer of a weakly toxic basic protein having
phospholipase A2 activity (RV-4) and a non-toxic acidic protein
which inhibits its enzymatic activity but potentiates its lethal
potency and neurotoxicity (RV-7).
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
-!- TOXIC DOSE: LD(50) is 0.32 mg/kg by intravenous injection for RV-4
and 0.15 mg/kg for RV-4/RV-7 complex.
{ECO:0000269|PubMed:8835338}.
-!- SIMILARITY: Belongs to the phospholipase A2 family. Group II
subfamily. D49 sub-subfamily. {ECO:0000305}.
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EMBL; X68385; CAA48456.1; -; mRNA.
PDB; 1OQS; X-ray; 1.90 A; B/D/F/H=17-138.
PDBsum; 1OQS; -.
ProteinModelPortal; Q02471; -.
SMR; Q02471; -.
PRIDE; Q02471; -.
HOVERGEN; HBG008137; -.
EvolutionaryTrace; Q02471; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0072556; C:other organism presynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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:0090729; F:toxin activity; IEA:UniProtKB-KW.
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.
CDD; cd00125; PLA2c; 1.
Gene3D; 1.20.90.10; -; 1.
InterPro; IPR001211; PLipase_A2.
InterPro; IPR033112; PLipase_A2_Asp_AS.
InterPro; IPR016090; PLipase_A2_dom.
InterPro; IPR036444; PLipase_A2_dom_sf.
InterPro; IPR033113; PLipase_A2_His_AS.
PANTHER; PTHR11716; PTHR11716; 1.
Pfam; PF00068; Phospholip_A2_1; 1.
PRINTS; PR00389; PHPHLIPASEA2.
SMART; SM00085; PA2c; 1.
SUPFAM; SSF48619; SSF48619; 1.
PROSITE; PS00119; PA2_ASP; 1.
PROSITE; PS00118; PA2_HIS; 1.
1: Evidence at protein level;
3D-structure; Calcium; Direct protein sequencing; Disulfide bond;
Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding;
Neurotoxin; Presynaptic neurotoxin; Secreted; Signal; Toxin.
SIGNAL 1 16 {ECO:0000269|PubMed:1425670,
ECO:0000269|PubMed:8835338}.
CHAIN 17 138 Basic phospholipase A2 RV-4.
/FTId=PRO_0000022977.
ACT_SITE 63 63 {ECO:0000250}.
ACT_SITE 105 105 {ECO:0000250}.
METAL 43 43 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 45 45 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 47 47 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 64 64 Calcium. {ECO:0000250}.
DISULFID 42 131 {ECO:0000269|PubMed:14501106}.
DISULFID 44 60 {ECO:0000269|PubMed:14501106}.
DISULFID 59 111 {ECO:0000269|PubMed:14501106}.
DISULFID 65 138 {ECO:0000269|PubMed:14501106}.
DISULFID 66 104 {ECO:0000269|PubMed:14501106}.
DISULFID 73 97 {ECO:0000269|PubMed:14501106}.
DISULFID 91 102 {ECO:0000269|PubMed:14501106}.
HELIX 18 29 {ECO:0000244|PDB:1OQS}.
HELIX 33 37 {ECO:0000244|PDB:1OQS}.
STRAND 38 40 {ECO:0000244|PDB:1OQS}.
TURN 41 43 {ECO:0000244|PDB:1OQS}.
STRAND 44 46 {ECO:0000244|PDB:1OQS}.
HELIX 55 68 {ECO:0000244|PDB:1OQS}.
TURN 75 77 {ECO:0000244|PDB:1OQS}.
STRAND 82 85 {ECO:0000244|PDB:1OQS}.
STRAND 88 91 {ECO:0000244|PDB:1OQS}.
HELIX 97 114 {ECO:0000244|PDB:1OQS}.
TURN 115 118 {ECO:0000244|PDB:1OQS}.
HELIX 121 123 {ECO:0000244|PDB:1OQS}.
HELIX 128 131 {ECO:0000244|PDB:1OQS}.
SEQUENCE 138 AA; 15555 MW; BFD471C8BBFE7F77 CRC64;
MRTLWIVAVC LIGVEGNLFQ FARMINGKLG AFSVWNYISY GCYCGWGGQG TPKDATDRCC
FVHDCCYGGV KGCNPKLAIY SYSFQRGNIV CGRNNGCLRT ICECDRVAAN CFHQNKNTYN
KEYKFLSSSK CRQRSEQC


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