PA2A8_DABPA
ID PA2A8_DABPA Reviewed; 137 AA.
AC Q9YGJ7;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Acidic phospholipase A2 VP8;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE Flags: Precursor;
OS Daboia palaestinae (Palestine viper) (Vipera palaestinae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Daboia.
OX NCBI_TaxID=1170828;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=9792822; DOI=10.1006/bbrc.1998.9528;
RA Kordis D., Bdolah A., Gubensek F.;
RT "Positive darwinian selection in Vipera palaestinae phospholipase A2 genes
RT is unexpectedly limited to the third exon.";
RL Biochem. Biophys. Res. Commun. 251:613-619(1998).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that is not toxic by
CC itself, but the synergistical mixture of a basic and this acidic
CC protein is lethal. PLA2 catalyzes the calcium-dependent hydrolysis of
CC the 2-acyl groups in 3-sn-phosphoglycerides (By similarity).
CC {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: Does not form a complex. {ECO:0000250}.
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; AF091854; AAC78084.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9YGJ7; -.
DR SMR; Q9YGJ7; -.
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 3: Inferred from homology;
KW Calcium; Disulfide bond; Hydrolase; Lipid degradation; Lipid metabolism;
KW Metal-binding; Secreted; Signal; Toxin.
FT SIGNAL 1..16
FT /evidence="ECO:0000250"
FT CHAIN 17..137
FT /note="Acidic phospholipase A2 VP8"
FT /id="PRO_0000022981"
FT ACT_SITE 62
FT /evidence="ECO:0000250"
FT ACT_SITE 104
FT /evidence="ECO:0000250"
FT BINDING 42
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 44
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 46
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 41..130
FT /evidence="ECO:0000250"
FT DISULFID 43..59
FT /evidence="ECO:0000250"
FT DISULFID 58..110
FT /evidence="ECO:0000250"
FT DISULFID 64..137
FT /evidence="ECO:0000250"
FT DISULFID 65..103
FT /evidence="ECO:0000250"
FT DISULFID 72..96
FT /evidence="ECO:0000250"
FT DISULFID 90..101
FT /evidence="ECO:0000250"
SQ SEQUENCE 137 AA; 15350 MW; 281ACB6F82E103D9 CRC64;
MRILWIVAVC LIGVEGNLYQ FGKMIFKMTR KSALSYSDYG CYCGWGGKGK PQDATDRCCF
VHDCCYGTVN GCDPKLSTYS YSFQNGDIVC GGDDPCLRAV CECDRVAAIC FGENMNTYDT
KYMLHSLFDC MEESEKC
