PA2B3_NAJMO
ID PA2B3_NAJMO Reviewed; 118 AA.
AC P00604;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Basic phospholipase A2 CM-III;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
OS Naja mossambica (Mozambique spitting cobra).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX NCBI_TaxID=8644;
RN [1]
RP PROTEIN SEQUENCE, AND TOXIC DOSE.
RC TISSUE=Venom;
RX PubMed=880314; DOI=10.1016/0005-2795(77)90275-6;
RA Joubert F.J.;
RT "Naja mossambica mossambica venom. Purification, some properties and the
RT amino acid sequences of three phospholipases A (CM-I, CM-II and CM-III).";
RL Biochim. Biophys. Acta 493:216-227(1977).
RN [2]
RP FUNCTION.
RX PubMed=3615669;
RA Lin W.W., Chang P.L., Lee C.Y., Joubert F.J.;
RT "Pharmacological study on phospholipases A2 isolated from Naja mossambica
RT mossambica venom.";
RL Proc. Natl. Sci. Counc. Repub. China, B, Life Sci. 11:155-163(1987).
RN [3]
RP REVIEW, FUNCTION, AND MOTIF.
RX PubMed=15922780; DOI=10.1016/j.toxicon.2005.02.018;
RA Kini R.M.;
RT "Structure-function relationships and mechanism of anticoagulant
RT phospholipase A2 enzymes from snake venoms.";
RL Toxicon 45:1147-1161(2005).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that shows several
CC activities. It shows strong anticoagulant activity, probably by binding
CC to coagulation factor Xa (F10) and inhibiting the formation of the
CC prothrombinase complex (PubMed:15922780), shows direct hemolytic
CC action, causes neuromuscular blockade with a gradual contracture and a
CC decreased sensitivity to ACh and KCl, abolishes twitches evoked by
CC indirect stimulation earlier than those by direct stimulation (in the
CC mouse phrenic nerve-diaphragm preparation), and causes myonecrosis when
CC injected intramuscularly (PubMed:3615669). PLA2 catalyzes the calcium-
CC dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
CC {ECO:0000269|PubMed:15922780, ECO:0000269|PubMed:3615669}.
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 0.3 mg/kg by injection into mice.
CC {ECO:0000269|PubMed:880314}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR PIR; A00744; PSNJ3M.
DR AlphaFoldDB; P00604; -.
DR SMR; P00604; -.
DR PRIDE; P00604; -.
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:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
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; Cytolysis;
KW Direct protein sequencing; Disulfide bond; Hemolysis;
KW Hemostasis impairing toxin; Hydrolase; Lipid degradation; Lipid metabolism;
KW Metal-binding; Myotoxin; Neurotoxin; Secreted; Toxin.
FT CHAIN 1..118
FT /note="Basic phospholipase A2 CM-III"
FT /id="PRO_0000161668"
FT MOTIF 52..69
FT /note="Coagulation factor Xa binding motif"
FT ACT_SITE 47
FT /evidence="ECO:0000250"
FT ACT_SITE 92
FT /evidence="ECO:0000250"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 11..70
FT /evidence="ECO:0000250"
FT DISULFID 26..117
FT /evidence="ECO:0000250"
FT DISULFID 28..44
FT /evidence="ECO:0000250"
FT DISULFID 43..98
FT /evidence="ECO:0000250"
FT DISULFID 50..91
FT /evidence="ECO:0000250"
FT DISULFID 59..84
FT /evidence="ECO:0000250"
FT DISULFID 77..89
FT /evidence="ECO:0000250"
SQ SEQUENCE 118 AA; 13302 MW; 0CF2A6A2A4C11BC2 CRC64;
NLYQFKNMIH CTVPSRPWWH FADYGCYCGR GGKGTPVDDL DRCCQVHDNC YEKAGKMGCW
PYFTLYKYKC SQGKLTCSGG NSKCGAAVCN CDLVAANCFA GARYIDANYN INFKKRCQ
