PA2B_VIPBB
ID PA2B_VIPBB Reviewed; 138 AA.
AC P31854; Q7T1D5;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Basic phospholipase A2 Pla2Vb;
DE Short=VbbPLA2 {ECO:0000303|PubMed:8499481};
DE Short=svPLA2 {ECO:0000303|PubMed:18062812};
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE Flags: Precursor;
OS Vipera berus berus (Common viper).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Vipera.
OX NCBI_TaxID=31156;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12823540; DOI=10.1046/j.1432-1033.2003.03629.x;
RA Guillemin I., Bouchier C., Garrigues T., Wisner A., Choumet V.;
RT "Sequences and structural organization of phospholipase A2 genes from
RT Vipera aspis aspis, V. aspis zinnikeri and Vipera berus berus venom.
RT Identification of the origin of a new viper population based on ammodytin
RT I1 heterogeneity.";
RL Eur. J. Biochem. 270:2697-2706(2003).
RN [2]
RP PROTEIN SEQUENCE OF 17-138, TOXIC DOSE, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=8499481; DOI=10.1016/0304-4165(93)90081-i;
RA Krizaj I., Siigur J., Samel M., Cotic V., Gubensek F.;
RT "Isolation, partial characterization and complete amino acid sequence of
RT the toxic phospholipase A2 from the venom of the common viper, Vipera berus
RT berus.";
RL Biochim. Biophys. Acta 1157:81-85(1993).
RN [3]
RP FUNCTION AS AN ANTICOAGULANT, AND 3D-STRUCTURE MODELING.
RX PubMed=18062812; DOI=10.1186/1472-6807-7-82;
RA Faure G., Gowda V.T., Maroun R.C.;
RT "Characterization of a human coagulation factor Xa-binding site on
RT Viperidae snake venom phospholipases A2 by affinity binding studies and
RT molecular bioinformatics.";
RL BMC Struct. Biol. 7:82-82(2007).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that exhibits medium
CC anticoagulant effects by binding to factor Xa (F10) and inhibiting the
CC prothrombinase activity (IC(50) is 90 nM). PLA2 catalyzes the calcium-
CC dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
CC {ECO:0000269|PubMed:18062812}.
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};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8499481}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:8499481}.
CC -!- TOXIC DOSE: LD(50) is 0.95 mg/kg by intraperitoneal injection.
CC {ECO:0000269|PubMed:8499481}.
CC -!- MISCELLANEOUS: Is not neurotoxic. {ECO:0000305|PubMed:8499481}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR EMBL; AY158636; AAN59982.1; -; Genomic_DNA.
DR PIR; S33267; S33267.
DR AlphaFoldDB; P31854; -.
DR SMR; P31854; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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 Blood coagulation cascade inhibiting toxin; Calcium;
KW Direct protein sequencing; Disulfide bond; Hemostasis impairing toxin;
KW Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding; Secreted;
KW Signal; Toxin.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:8499481"
FT CHAIN 17..138
FT /note="Basic phospholipase A2 Pla2Vb"
FT /id="PRO_0000161719"
FT ACT_SITE 63
FT /evidence="ECO:0000250"
FT ACT_SITE 105
FT /evidence="ECO:0000250"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 42..131
FT /evidence="ECO:0000250"
FT DISULFID 44..60
FT /evidence="ECO:0000250"
FT DISULFID 59..111
FT /evidence="ECO:0000250"
FT DISULFID 65..138
FT /evidence="ECO:0000250"
FT DISULFID 66..104
FT /evidence="ECO:0000250"
FT DISULFID 73..97
FT /evidence="ECO:0000250"
FT DISULFID 91..102
FT /evidence="ECO:0000250"
FT CONFLICT 136
FT /note="D -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 138 AA; 15716 MW; 79B9F9E0D16C9CCB CRC64;
MRTLWIVAVW LMGVEGNLFQ FGNMINHMVG KHAVWSYLSY GCYCGWGGQG KPQDATDRCC
FVHDCCYGRA NGCDPKLSTY SYNFQNGNIV CGNKYGCLRH ICECDRVAAI CFQKNMNTYN
KKYKNYSSSN CQENSDKC
