PA2B3_BUNCE
ID PA2B3_BUNCE Reviewed; 137 AA.
AC Q6SLM0;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Basic phospholipase A2 3;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE Flags: Precursor; Fragment;
OS Bungarus caeruleus (Indian krait).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Bungarinae; Bungarus.
OX NCBI_TaxID=132961;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF
RP 20-137 (HOMOTRIMER), AND DISULFIDE BONDS.
RC TISSUE=Venom, and Venom gland;
RX PubMed=16508078; DOI=10.1107/s1744309104025503;
RA Singh G., Gourinath S., Saravanan K., Sharma S., Bhanumathi S., Betzel C.,
RA Srinivasan A., Singh T.P.;
RT "Sequence-induced trimerization of phospholipase A2: structure of a
RT trimeric isoform of PLA2 from common krait (Bungarus caeruleus) at 2.5 A
RT resolution.";
RL Acta Crystallogr. F 61:8-13(2005).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 20-137 (MONOMER), SUBUNIT, AND
RP DISULFIDE BONDS.
RX PubMed=17372360; DOI=10.1107/s0907444907007354;
RA Le Trong I., Stenkamp R.E.;
RT "An alternate description of two crystal structures of phospholipase A2
RT from Bungarus caeruleus.";
RL Acta Crystallogr. D 63:548-549(2007).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that shows anticoagulant
CC and neurotoxic activities. 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;
CC Evidence={ECO:0000250|UniProtKB:P14418};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P14418};
CC -!- SUBUNIT: Monomer, or homotrimer. Was firstly described as a trimer
CC (PubMed:16508078), but has been reinterpreted with the possibility of
CC being a monomer (PubMed:17372360). {ECO:0000269|PubMed:16508078,
CC ECO:0000269|PubMed:17372360}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
CC -!- CAUTION: The PDB entry 2OSN is a reinterpretation of the PDB entry
CC 1G2X. {ECO:0000305}.
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DR EMBL; AY455756; AAR19229.1; -; mRNA.
DR PDB; 1G2X; X-ray; 2.50 A; A/B/C=20-137.
DR PDB; 2OSN; X-ray; 2.50 A; A=20-137.
DR PDBsum; 1G2X; -.
DR PDBsum; 2OSN; -.
DR AlphaFoldDB; Q6SLM0; -.
DR SMR; Q6SLM0; -.
DR EvolutionaryTrace; Q6SLM0; -.
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 3D-structure; Blood coagulation cascade inhibiting toxin; Calcium;
KW Disulfide bond; Hemostasis impairing toxin; Hydrolase; Lipid degradation;
KW Lipid metabolism; Metal-binding; Neurotoxin; Presynaptic neurotoxin;
KW Secreted; Signal; Toxin.
FT SIGNAL <1..11
FT /evidence="ECO:0000255"
FT PROPEP 12..19
FT /evidence="ECO:0000250"
FT /id="PRO_0000414306"
FT CHAIN 20..137
FT /note="Basic phospholipase A2 3"
FT /id="PRO_0000414307"
FT ACT_SITE 65
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT ACT_SITE 111
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT BINDING 49
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT DISULFID 30..89
FT /evidence="ECO:0000269|PubMed:16508078,
FT ECO:0000269|PubMed:17372360, ECO:0007744|PDB:1G2X,
FT ECO:0007744|PDB:2OSN"
FT DISULFID 44..136
FT /evidence="ECO:0000269|PubMed:16508078,
FT ECO:0000269|PubMed:17372360, ECO:0007744|PDB:1G2X,
FT ECO:0007744|PDB:2OSN"
FT DISULFID 46..62
FT /evidence="ECO:0000269|PubMed:16508078,
FT ECO:0000269|PubMed:17372360, ECO:0007744|PDB:1G2X,
FT ECO:0007744|PDB:2OSN"
FT DISULFID 61..117
FT /evidence="ECO:0000269|PubMed:16508078,
FT ECO:0000269|PubMed:17372360, ECO:0007744|PDB:1G2X,
FT ECO:0007744|PDB:2OSN"
FT DISULFID 68..110
FT /evidence="ECO:0000269|PubMed:16508078,
FT ECO:0000269|PubMed:17372360, ECO:0007744|PDB:1G2X,
FT ECO:0007744|PDB:2OSN"
FT DISULFID 78..103
FT /evidence="ECO:0000269|PubMed:16508078,
FT ECO:0000269|PubMed:17372360, ECO:0007744|PDB:1G2X,
FT ECO:0007744|PDB:2OSN"
FT DISULFID 96..108
FT /evidence="ECO:0000269|PubMed:16508078,
FT ECO:0000269|PubMed:17372360, ECO:0007744|PDB:1G2X,
FT ECO:0007744|PDB:2OSN"
FT NON_TER 1
FT HELIX 21..31
FT /evidence="ECO:0007829|PDB:1G2X"
FT HELIX 36..39
FT /evidence="ECO:0007829|PDB:1G2X"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:1G2X"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:1G2X"
FT HELIX 57..72
FT /evidence="ECO:0007829|PDB:1G2X"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:1G2X"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:1G2X"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:1G2X"
FT HELIX 102..120
FT /evidence="ECO:0007829|PDB:1G2X"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:1G2X"
SQ SEQUENCE 137 AA; 14831 MW; E44E6B9C4BCECA52 CRC64;
LVAVCVSLLG AANIPPQPLN LQQFKNMIQC AGTRTWTAYI NYGCYCGKGG SGTPVDKLDR
CCYTHDHCYN QADSIPGCNP NIKTYSYTCT QPNITCTRTA DACAKFLCDC DRTAAICFAS
APYNINNIMI SASNSCQ
