PA2B2_DABRR
ID PA2B2_DABRR Reviewed; 137 AA.
AC A8CG90;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Basic phospholipase A2 Drk-b2;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE Flags: Precursor;
OS Daboia russelii (Russel's viper) (Vipera russelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Daboia.
OX NCBI_TaxID=8707;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-27, FUNCTION, AND MASS
RP SPECTROMETRY.
RC STRAIN=Kolkata; TISSUE=Venom, and Venom gland;
RX PubMed=17611171; DOI=10.1016/j.bbapap.2007.04.012;
RA Tsai I.-H., Tsai H.-Y., Wang Y.-M., Pe T., Warrell D.-A.;
RT "Venom phospholipases of Russell's vipers from Myanmar and eastern India--
RT cloning, characterization and phylogeographic analysis.";
RL Biochim. Biophys. Acta 1774:1020-1028(2007).
CC -!- FUNCTION: Exhibits high hydrolytic activities and shows strong
CC preference for the anionic micelles (dPPC with deoxycholate) to the
CC zwitterionic micelles (dPPC with Triton X-100). PLA2 catalyzes the
CC calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-
CC phosphoglycerides. {ECO:0000269|PubMed:17611171}.
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.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: Mass=13704; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:17611171};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR EMBL; DQ090661; AAZ53183.1; -; mRNA.
DR AlphaFoldDB; A8CG90; -.
DR SMR; A8CG90; -.
DR PRIDE; A8CG90; -.
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 Direct protein sequencing; Disulfide bond; Hydrolase; Lipid degradation;
KW Lipid metabolism; Metal-binding; Secreted; Signal; Toxin.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:17611171"
FT CHAIN 17..137
FT /note="Basic phospholipase A2 Drk-b2"
FT /id="PRO_0000419218"
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..137
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 26..27
FT /note="FR -> NQ (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 137 AA; 15461 MW; E948F7D2B6B63DCD CRC64;
MRTLWIVAVC LIGVEGNLLQ FGRMIFRMTA KNPLSSYSNY GCYCGWGGKG KPQDATDRCC
FVHDCCYEKV NDCNPKTATY SYSFENGGIV CGDRDPCKRA VCECDRVAAT CFRDNLNTYD
KKYRKYPPSQ CTGTEQC
