PA2B_BUNCE
ID PA2B_BUNCE Reviewed; 145 AA.
AC Q9DF52;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Basic phospholipase A2 KPA2;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE Flags: Precursor;
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 (2.45 ANGSTROMS) OF
RP 28-142 IN COMPLEX WITH CALCIUM ION, COFACTOR, SUBUNIT, AND DISULFIDE BONDS.
RC TISSUE=Venom, and Venom gland;
RX PubMed=11286555; DOI=10.1006/jmbi.2001.4550;
RA Singh G., Gourinath S., Sharma S., Paramasivam M., Srinivasan A.,
RA Singh T.P.;
RT "Sequence and crystal structure determination of a basic phospholipase A2
RT from common krait (Bungarus caeruleus) at 2.4 A resolution: identification
RT and characterization of its pharmacological sites.";
RL J. Mol. Biol. 307:1049-1059(2001).
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.
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:0000305|PubMed:11286555};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000305|PubMed:11286555};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11286555}.
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}.
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DR EMBL; AF297663; AAG13412.1; -; mRNA.
DR PDB; 1DPY; X-ray; 2.45 A; A=28-142.
DR PDB; 1FE5; X-ray; 2.45 A; A=28-145.
DR PDB; 1PO8; X-ray; 2.71 A; A=28-145.
DR PDBsum; 1DPY; -.
DR PDBsum; 1FE5; -.
DR PDBsum; 1PO8; -.
DR AlphaFoldDB; Q9DF52; -.
DR SMR; Q9DF52; -.
DR EvolutionaryTrace; Q9DF52; -.
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..19
FT /evidence="ECO:0000255"
FT PROPEP 20..27
FT /evidence="ECO:0000250"
FT /id="PRO_0000022827"
FT CHAIN 28..145
FT /note="Basic phospholipase A2 KPA2"
FT /id="PRO_0000022828"
FT ACT_SITE 73
FT /evidence="ECO:0000305|PubMed:11286555"
FT ACT_SITE 119
FT /evidence="ECO:0000305|PubMed:11286555"
FT BINDING 53
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:11286555,
FT ECO:0007744|PDB:1FE5"
FT BINDING 55
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:11286555,
FT ECO:0007744|PDB:1FE5"
FT BINDING 57
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:11286555,
FT ECO:0007744|PDB:1FE5"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:11286555,
FT ECO:0007744|PDB:1FE5"
FT DISULFID 38..97
FT /evidence="ECO:0000269|PubMed:11286555,
FT ECO:0007744|PDB:1FE5"
FT DISULFID 52..144
FT /evidence="ECO:0000269|PubMed:11286555,
FT ECO:0007744|PDB:1FE5"
FT DISULFID 54..70
FT /evidence="ECO:0000269|PubMed:11286555,
FT ECO:0007744|PDB:1FE5"
FT DISULFID 69..125
FT /evidence="ECO:0000269|PubMed:11286555,
FT ECO:0007744|PDB:1FE5"
FT DISULFID 76..118
FT /evidence="ECO:0000269|PubMed:11286555,
FT ECO:0007744|PDB:1FE5"
FT DISULFID 86..111
FT /evidence="ECO:0000269|PubMed:11286555,
FT ECO:0007744|PDB:1FE5"
FT DISULFID 104..116
FT /evidence="ECO:0000269|PubMed:11286555,
FT ECO:0007744|PDB:1FE5"
FT HELIX 29..39
FT /evidence="ECO:0007829|PDB:1DPY"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:1DPY"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:1DPY"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:1DPY"
FT HELIX 65..80
FT /evidence="ECO:0007829|PDB:1DPY"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:1DPY"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:1DPY"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:1DPY"
FT HELIX 110..128
FT /evidence="ECO:0007829|PDB:1DPY"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:1DPY"
FT TURN 139..142
FT /evidence="ECO:0007829|PDB:1PO8"
SQ SEQUENCE 145 AA; 15765 MW; 4CE49BD226AF3317 CRC64;
MYPAHLLVLV AVCVSLLGAA NIPPQPLNLI QFKNMIQCAG TRPWTAYVNY GCYCGKGGSG
TPVDELDRCC YTHDNCYNEA EKIPGCNPNI KTYSYTCTEP NLTCTDTADT CARFLCDCDR
TAAICFASAP YNSNNVMISS STNCQ
