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Basic phospholipase A2 chain HDP-2P (svPLA2) (EC 3.1.1.4) (Heterodimeric neurotoxic phospholipases A2 basic subunit 2) (Phosphatidylcholine 2-acylhydrolase)

 PA2B2_VIPNI             Reviewed;         138 AA.
Q1RP78;
05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
16-MAY-2006, sequence version 1.
20-JUN-2018, entry version 61.
RecName: Full=Basic phospholipase A2 chain HDP-2P;
Short=svPLA2;
EC=3.1.1.4;
AltName: Full=Heterodimeric neurotoxic phospholipases A2 basic subunit 2;
AltName: Full=Phosphatidylcholine 2-acylhydrolase;
Flags: Precursor;
Vipera nikolskii (Nikolsky's adder).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Viperidae; Viperinae; Vipera.
NCBI_TaxID=110206;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-56; 59-71; 77-85;
87-92 AND 101-120, FUNCTION, AND MASS SPECTROMETRY.
TISSUE=Venom, and Venom gland;
PubMed=18083205; DOI=10.1016/j.toxicon.2007.11.001;
Ramazanova A.S., Zavada L.L., Starkov V.G., Kovyazina I.V.,
Subbotina T.F., Kostyukhina E.E., Dementieva I.N., Ovchinnikova T.V.,
Utkin Y.N.;
"Heterodimeric neurotoxic phospholipases A2 -- the first proteins from
venom of recently established species Vipera nikolskii: implication of
venom composition in viper systematics.";
Toxicon 51:524-537(2008).
[2]
CRYSTALLIZATION.
TISSUE=Venom;
PubMed=19500614; DOI=10.1016/j.toxicon.2009.05.024;
Gao W., Starkov V.G., He Z.X., Wang Q.H., Tsetlin V.I., Utkin Y.N.,
Lin Z.J., Bi R.C.;
"Functions, structures and Triton X-100 effect for the catalytic
subunits of heterodimeric phospholipases A2 from Vipera nikolskii
venom.";
Toxicon 54:709-716(2009).
-!- FUNCTION: Monomer: snake venom phospholipase A2 (PLA2) that
affects neuromuscular transmission presynaptically. It has
catalytic activity, anticoagulant activity and weakly inhibits
ADP-induced platelet aggregation. PLA2 catalyzes the calcium-
dependent hydrolysis of the 2-acyl groups in 3-sn-
phosphoglycerides. {ECO:0000269|PubMed:18083205}.
-!- FUNCTION: Heterodimer: shows the same activities as the monomer,
but with a lower potency. {ECO:0000269|PubMed:18083205}.
-!- 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};
-!- ENZYME REGULATION: Enzymatic activity and neurotoxicity are
inhibited by Triton X-100 (By similarity). Triton X-100 has been
determined to be located in the center of the hydrophobic channel
of the enzyme (PubMed:19500614). {ECO:0000250,
ECO:0000269|PubMed:19500614}.
-!- SUBUNIT: Heterodimer of an acidic and a basic chain; non-
covalently linked. The toxic basic protein has phospholipase A2
activity (chain HDP-2P) and the non-toxic acidic protein functions
as its inhibitor (chain HPD-1I (AC A4VBF0)).
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
-!- MASS SPECTROMETRY: Mass=13827; Mass_error=1; Method=MALDI;
Range=17-138; Evidence={ECO:0000269|PubMed:18083205};
-!- SIMILARITY: Belongs to the phospholipase A2 family. Group II
subfamily. D49 sub-subfamily. {ECO:0000305}.
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EMBL; AM238699; CAJ87659.1; -; mRNA.
ProteinModelPortal; Q1RP78; -.
PRIDE; Q1RP78; -.
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:InterPro.
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;
Blood coagulation cascade inhibiting toxin; Direct protein sequencing;
Disulfide bond; Hemostasis impairing toxin; Hydrolase; Metal-binding;
Neurotoxin; Platelet aggregation inhibiting toxin;
Presynaptic neurotoxin; Secreted; Signal; Toxin.
SIGNAL 1 16 {ECO:0000269|PubMed:18083205}.
CHAIN 17 138 Basic phospholipase A2 chain HDP-2P.
/FTId=PRO_5000079753.
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:0000250}.
DISULFID 44 60 {ECO:0000250}.
DISULFID 59 111 {ECO:0000250}.
DISULFID 65 138 {ECO:0000250}.
DISULFID 66 104 {ECO:0000250}.
DISULFID 73 97 {ECO:0000250}.
DISULFID 91 102 {ECO:0000250}.
SEQUENCE 138 AA; 15594 MW; 28D55BD516C3EA3E CRC64;
MRILWIVAVC LIGVEGNLFQ FAKMINGKLG AFSVWNYISY GCYCGWGGQG TPKDATDRCC
FVHDCCYGRV RGCNPKLAIY AYSFKKGNIV CGKNNGCLRD ICECDRVAAN CFHQNKNTYN
KNYRFLSSSR CRQTSEQC


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