PA2A1_DABRR
ID PA2A1_DABRR Reviewed; 138 AA.
AC A8CG86; Q2ES54;
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=Acidic phospholipase A2 Drk-a1;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE AltName: Full=Phospholipase A2 Drk-a1';
DE AltName: Full=Phospholipase A2-I;
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=Eastern India; 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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Madhukumar A.V., Reza M.A., Gowda T.V., Kini R.M.;
RT "A survey of Daboia russelii venom gland transcripts (cDNA): unraveling the
RT venom proteins and peptides.";
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that exhibits high
CC hydrolytic activities and shows strong preference for the anionic
CC micelles (dPPC with deoxycholate) to the zwitterionic micelles (dPPC
CC with Triton X-100). PLA2 catalyzes the calcium-dependent hydrolysis of
CC the 2-acyl groups in 3-sn-phosphoglycerides.
CC {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=13573; Method=Electrospray; Note=in Drk-a1.;
CC Evidence={ECO:0000269|PubMed:17611171};
CC -!- MASS SPECTROMETRY: Mass=13812; Method=Electrospray; Note=in Drk-a1'
CC which has only its protein sequence AA 17-27 sequenced.;
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; DQ090658; AAZ53180.1; -; mRNA.
DR EMBL; DQ365974; ABD24036.1; -; mRNA.
DR AlphaFoldDB; A8CG86; -.
DR SMR; A8CG86; -.
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 Calcium; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Lipid degradation; Lipid metabolism; Metal-binding; Secreted; Signal;
KW Toxin.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:17611171"
FT CHAIN 17..138
FT /note="Acidic phospholipase A2 Drk-a1"
FT /id="PRO_0000419215"
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 VARIANT 18
FT /note="L -> F (in Drk-a1')"
SQ SEQUENCE 138 AA; 15329 MW; 324139CF8B6FC15C CRC64;
MRTLWIVAVC LIGVEGNLFQ FAEMIVKMTG KEAVHSYAIY GCYCGWGGQG KPQDATDRCC
FVHDCCYGTV NDCNPKMATY SYSFENGDIV CGDNNLCLKT VCECDRAAAI CLGQNVNTYD
KNYENYAISH CTEESEQC
