PA2A1_BUNCE
ID PA2A1_BUNCE Reviewed; 137 AA.
AC Q6SLM2;
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=Acidic phospholipase A2 1;
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], MASS SPECTROMETRY, X-RAY CRYSTALLOGRAPHY (2.7
RP ANGSTROMS) OF 20-137 IN COMPLEX WITH N-TRIDECANOIC ACID, AND DISULFIDE
RP BONDS.
RC TISSUE=Venom, and Venom gland;
RX PubMed=15659372; DOI=10.1110/ps.041115505;
RA Singh G., Jasti J., Saravanan K., Sharma S., Kaur P., Srinivasan A.,
RA Singh T.P.;
RT "Crystal structure of the complex formed between a group I phospholipase A2
RT and a naturally occurring fatty acid at 2.7 A resolution.";
RL Protein Sci. 14:395-400(2005).
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. {ECO:0000250|UniProtKB:P14418};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15659372}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: Mass=13198.1; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:15659372};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR EMBL; AY455754; AAS20530.1; -; mRNA.
DR PDB; 1TC8; X-ray; 2.70 A; A=20-137.
DR PDBsum; 1TC8; -.
DR AlphaFoldDB; Q6SLM2; -.
DR SMR; Q6SLM2; -.
DR PRIDE; Q6SLM2; -.
DR EvolutionaryTrace; Q6SLM2; -.
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 /id="PRO_0000414302"
FT CHAIN 20..137
FT /note="Acidic phospholipase A2 1"
FT /id="PRO_0000414303"
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 49
FT /ligand="tridecanoate"
FT /ligand_id="ChEBI:CHEBI:125832"
FT /evidence="ECO:0000269|PubMed:15659372"
FT BINDING 65
FT /ligand="tridecanoate"
FT /ligand_id="ChEBI:CHEBI:125832"
FT /evidence="ECO:0000269|PubMed:15659372"
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:15659372,
FT ECO:0007744|PDB:1TC8"
FT DISULFID 44..136
FT /evidence="ECO:0000269|PubMed:15659372,
FT ECO:0007744|PDB:1TC8"
FT DISULFID 46..62
FT /evidence="ECO:0000269|PubMed:15659372,
FT ECO:0007744|PDB:1TC8"
FT DISULFID 61..117
FT /evidence="ECO:0000269|PubMed:15659372,
FT ECO:0007744|PDB:1TC8"
FT DISULFID 68..110
FT /evidence="ECO:0000269|PubMed:15659372,
FT ECO:0007744|PDB:1TC8"
FT DISULFID 78..103
FT /evidence="ECO:0000269|PubMed:15659372,
FT ECO:0007744|PDB:1TC8"
FT DISULFID 96..108
FT /evidence="ECO:0000269|PubMed:15659372,
FT ECO:0007744|PDB:1TC8"
FT NON_TER 1
FT HELIX 21..31
FT /evidence="ECO:0007829|PDB:1TC8"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:1TC8"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:1TC8"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:1TC8"
FT HELIX 57..72
FT /evidence="ECO:0007829|PDB:1TC8"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:1TC8"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:1TC8"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:1TC8"
FT HELIX 102..120
FT /evidence="ECO:0007829|PDB:1TC8"
FT TURN 131..134
FT /evidence="ECO:0007829|PDB:1TC8"
SQ SEQUENCE 137 AA; 15058 MW; 83F379CD4BF3D44F CRC64;
LVAVCVSLLG AANIPPQPLN LYQLMNMIQC ANTRTWPSYT NYGCYCGKGG SGTPVDDLDR
CCYTHDHCYN DAKNIDGCNP VTKTYSYTCT EPTITCNDSK DKCARFVCDC DRTAAICFAK
APYNTSNVMI RSTNSCQ
