PA2B_HYDSC
ID PA2B_HYDSC Reviewed; 119 AA.
AC P00610;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Basic phospholipase A2;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Myotoxin;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE AltName: Full=Toxin VI-5;
DE AltName: Full=Toxin VI:5b;
OS Hydrophis schistosus (Beaked sea snake) (Enhydrina schistosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Hydrophiidae; Hydrophis.
OX NCBI_TaxID=8682;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Venom;
RX PubMed=7222079; DOI=10.1016/0041-0101(81)90113-6;
RA Lind P., Eaker D.;
RT "Amino acid sequence of a lethal myotoxic phospholipase A2 from the venom
RT of the common sea snake (Enhydrina schistosa).";
RL Toxicon 19:11-24(1981).
RN [2]
RP FUNCTION.
RX PubMed=3117784; DOI=10.1016/s0021-9258(18)47808-8;
RA Kini R.M., Evans H.J.;
RT "Structure-function relationships of phospholipases. The anticoagulant
RT region of phospholipases A2.";
RL J. Biol. Chem. 262:14402-14407(1987).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that has several
CC activities. It is myotoxic, has weak anticoagulant activity and
CC inhibits neuromuscular transmission by blocking acetylcholine release
CC from the nerve termini. PLA2 catalyzes the calcium-dependent hydrolysis
CC of the 2-acyl groups in 3-sn-phosphoglycerides.
CC {ECO:0000269|PubMed:3117784}.
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 -!- TOXIC DOSE: LD(50) is 0.11 mg/kg by intravenous injection.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR PIR; A00751; PSEYA.
DR AlphaFoldDB; P00610; -.
DR SMR; P00610; -.
DR PRIDE; P00610; -.
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 Blood coagulation cascade inhibiting toxin; Calcium;
KW Direct protein sequencing; Disulfide bond; Hemostasis impairing toxin;
KW Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding; Myotoxin;
KW Neurotoxin; Presynaptic neurotoxin; Secreted; Toxin.
FT CHAIN 1..119
FT /note="Basic phospholipase A2"
FT /id="PRO_0000161644"
FT ACT_SITE 48
FT /evidence="ECO:0000250"
FT ACT_SITE 93
FT /evidence="ECO:0000250"
FT BINDING 28
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 30
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 32
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 11..71
FT /evidence="ECO:0000250"
FT DISULFID 27..118
FT /evidence="ECO:0000250"
FT DISULFID 29..45
FT /evidence="ECO:0000250"
FT DISULFID 44..99
FT /evidence="ECO:0000250"
FT DISULFID 51..92
FT /evidence="ECO:0000250"
FT DISULFID 60..85
FT /evidence="ECO:0000250"
FT DISULFID 78..90
FT /evidence="ECO:0000250"
FT VARIANT 64
FT /note="M -> L (in 50% of the molecules)"
FT VARIANT 98
FT /note="E -> K (in 30% of the molecules)"
SQ SEQUENCE 119 AA; 13446 MW; A79952C182F4D7B4 CRC64;
NLVQFSYVIT CANHNRRSSL DYADYGCYCG AGGSGTPVDE LDRCCKIHDD CYGEAEKQGC
YPKMLMYDYY CGSNGPYCRN VKKKCNRKVC DCDVAAAECF ARNAYNNANY NIDTKKRCK
