PA2B_VIPAP
ID PA2B_VIPAP Reviewed; 138 AA.
AC Q8JFG0; Q6A358;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Basic phospholipase A2 vaspin B chain;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE AltName: Full=Vaspin toxic component;
DE Flags: Precursor;
OS Vipera aspis aspis (Aspic viper).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Vipera.
OX NCBI_TaxID=194601;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=12220671; DOI=10.1016/s0014-5793(02)03205-2;
RA Jan V., Maroun R.C., Robbe-Vincent A., De Haro L., Choumet V.;
RT "Toxicity evolution of Vipera aspis aspis venom: identification and
RT molecular modeling of a novel phospholipase A(2) heterodimer neurotoxin.";
RL FEBS Lett. 527:263-268(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=17904178; DOI=10.1016/j.toxicon.2007.07.024;
RA Jan V.M., Guillemin I., Robbe-Vincent A., Choumet V.;
RT "Phospholipase A2 diversity and polymorphism in European viper venoms:
RT paradoxical molecular evolution in Viperinae.";
RL Toxicon 50:1140-1161(2007).
CC -!- FUNCTION: Heterodimer: postsynaptic neurotoxin. {ECO:0000250}.
CC -!- FUNCTION: Monomer: snake venom phospholipase A2 (PLA2) that shows
CC postsynaptic neurotoxicity. PLA2 catalyzes the calcium-dependent
CC hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides (By
CC similarity). {ECO:0000250}.
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 -!- SUBUNIT: Heterodimer of a weakly toxic basic protein having
CC phospholipase A2 activity (B chain (AC Q8JFG1)) and a non-toxic acidic
CC protein functioning as its inhibitor (A chain).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR EMBL; AJ459807; CAD30850.1; -; mRNA.
DR EMBL; AY243576; AAO86504.1; -; Genomic_DNA.
DR EMBL; AJ580280; CAE47285.1; -; mRNA.
DR EMBL; AJ580281; CAE47286.1; -; mRNA.
DR EMBL; AJ580283; CAE47288.1; -; mRNA.
DR EMBL; AJ580284; CAE47289.1; -; mRNA.
DR EMBL; AJ580285; CAE47290.1; -; mRNA.
DR EMBL; AJ580293; CAE47298.1; -; mRNA.
DR AlphaFoldDB; Q8JFG0; -.
DR SMR; Q8JFG0; -.
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 2: Evidence at transcript level;
KW Calcium; Disulfide bond; Hydrolase; Lipid degradation; Lipid metabolism;
KW Metal-binding; Neurotoxin; Postsynaptic neurotoxin; Presynaptic neurotoxin;
KW Secreted; Signal; Toxin.
FT SIGNAL 1..16
FT /evidence="ECO:0000250"
FT CHAIN 17..138
FT /note="Basic phospholipase A2 vaspin B chain"
FT /id="PRO_0000022968"
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"
SQ SEQUENCE 138 AA; 15610 MW; 28C749D504D1EA3E CRC64;
MRILWIVAVC LIGVEGNLFQ FAKMINGKLG AFSVWNYISY GCYCGWGGQG TPKDATDRCC
FVHDCCYGRV RGCNPKLAIY SYSFKKGNIV CGKNNGCLRD ICECDRVAAN CFHQNKNTYN
KNYRFLSSSR CRQTSEQC
