PA2B_VIPRE
ID PA2B_VIPRE Reviewed; 138 AA.
AC F8QN54;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Basic phospholipase A2 vurtoxin {ECO:0000303|PubMed:21185324, ECO:0000303|PubMed:25522251};
DE Short=svPLA2;
DE EC=3.1.1.4 {ECO:0000269|PubMed:25522251};
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE Flags: Precursor;
OS Vipera renardi (Steppe viper) (Vipera ursinii renardi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Vipera.
OX NCBI_TaxID=927686;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MASS SPECTROMETRY, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Venom, and Venom gland;
RX PubMed=21185324; DOI=10.1016/j.toxicon.2010.12.012;
RA Tsai I.-H., Wang Y.M., Cheng A.C., Starkov V., Osipov A., Nikitin I.,
RA Makarova Y., Ziganshin R., Utkin Y.;
RT "cDNA cloning, structural, and functional analyses of venom phospholipases
RT A and a Kunitz-type protease inhibitor from steppe viper Vipera ursinii
RT renardi.";
RL Toxicon 57:332-341(2011).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP 3D-STRUCTURE MODELING.
RC TISSUE=Venom;
RX PubMed=25522251; DOI=10.1371/journal.pone.0115428;
RA Vulfius C.A., Kasheverov I.E., Starkov V.G., Osipov A.V., Andreeva T.V.,
RA Filkin S.Y., Gorbacheva E.V., Astashev M.E., Tsetlin V.I., Utkin Y.N.;
RT "Inhibition of nicotinic acetylcholine receptors, a novel facet in the
RT pleiotropic activities of snake venom phospholipases A2.";
RL PLoS ONE 9:e115428-e115428(2014).
CC -!- FUNCTION: Snake venom phospholipase A2 that may have a strong
CC anticoagulant activity (PubMed:21185324). Is able to suppress the
CC acetylcholine (ACh)-evoked current mediated by alpha-7-similar nAChRs
CC in L.stagnalis neurons (IC(50)=10.5 uM) and to compete with alpha-
CC bungarotoxin for binding to muscle- and alpha-7 neuronal nAChR types,
CC as well as to AChBPs (PubMed:25522251). In inhibition of alpha-
CC bungarotoxin binding, this toxin is mostly active against T.californica
CC nAChR (IC(50)=0.26 uM), it is moderately active against human alpha-7
CC nAChR (IC(50)=14 uM), and is not active against L.stagnalis and
CC A.californica AChBP (IC(50)>30 uM) (PubMed:25522251).
CC {ECO:0000269|PubMed:21185324, ECO:0000269|PubMed:25522251}.
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, ECO:0000255|PROSITE-
CC ProRule:PRU10036, ECO:0000269|PubMed:25522251};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=0.7 mmol/min/umol enzyme {ECO:0000269|PubMed:25522251};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21185324}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:21185324}.
CC -!- MASS SPECTROMETRY: Mass=13878; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:21185324};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR EMBL; GQ304908; ADG86232.1; -; mRNA.
DR AlphaFoldDB; F8QN54; -.
DR SMR; F8QN54; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030550; F:acetylcholine receptor inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
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 CDD; cd00125; PLA2c; 1.
DR Gene3D; 1.20.90.10; -; 1.
DR InterPro; IPR001211; PLipase_A2.
DR InterPro; IPR033112; PLipase_A2_Asp_AS.
DR InterPro; IPR016090; PLipase_A2_dom.
DR InterPro; IPR036444; PLipase_A2_dom_sf.
DR InterPro; IPR033113; PLipase_A2_His_AS.
DR PANTHER; PTHR11716; PTHR11716; 1.
DR Pfam; PF00068; Phospholip_A2_1; 1.
DR PRINTS; PR00389; PHPHLIPASEA2.
DR SMART; SM00085; PA2c; 1.
DR SUPFAM; SSF48619; SSF48619; 1.
DR PROSITE; PS00119; PA2_ASP; 1.
DR PROSITE; PS00118; PA2_HIS; 1.
PE 1: Evidence at protein level;
KW Acetylcholine receptor inhibiting toxin;
KW Blood coagulation cascade inhibiting toxin; Disulfide bond;
KW Hemostasis impairing toxin; Hydrolase; Lipid degradation; Lipid metabolism;
KW Metal-binding; Neurotoxin; Postsynaptic neurotoxin; Secreted; Signal;
KW Toxin.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:21185324"
FT CHAIN 17..138
FT /note="Basic phospholipase A2 vurtoxin"
FT /evidence="ECO:0000269|PubMed:21185324"
FT /id="PRO_0000419637"
FT ACT_SITE 63
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT ACT_SITE 105
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 42..131
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 44..60
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 59..111
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 65..138
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 66..104
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 73..97
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 91..102
FT /evidence="ECO:0000250|UniProtKB:P59071"
SQ SEQUENCE 138 AA; 15636 MW; 39D3F5DD3E780A6D CRC64;
MRTLWIVAVC LIGVEGSLLE FGMMILEETG KNPLTSYSFY GCYCGVGGKG TPKDATDRCC
FVHDCCYGNL PDCNPKIDRY KYHRKNGAIV CGKGTSCENR ICECDRAAAI CFRKNLKTYN
HIYKYYPDFL CKKESEKC
