PA2B_NAJPA
ID PA2B_NAJPA Reviewed; 118 AA.
AC P14556;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Basic phospholipase A2 nigexine;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
OS Naja pallida (Red 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=8658;
RN [1]
RP PROTEIN SEQUENCE, AND FUNCTION.
RC TISSUE=Venom;
RX PubMed=2753914; DOI=10.1016/s0021-9258(18)51627-6;
RA Chwetzoff S., Tsunasawa S., Sakiyama F., Menez A.;
RT "Nigexine, a phospholipase A2 from cobra venom with cytotoxic properties
RT not related to esterase activity. Purification, amino acid sequence, and
RT biological properties.";
RL J. Biol. Chem. 264:13289-13297(1989).
RN [2]
RP FUNCTION.
RX PubMed=2048150; DOI=10.1016/0041-0101(91)90290-8;
RA Rowan E.G., Harvey A.L., Menez A.;
RT "Neuromuscular effects of nigexine, a basic phospholipase A2 from Naja
RT nigricollis venom.";
RL Toxicon 29:371-374(1991).
RN [3]
RP REVIEW, 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 anticoagulant
CC activity, has cytotoxic activity and affects neuromuscular transmission
CC in vitro. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:2048150,
CC ECO:0000269|PubMed:2753914}.
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 -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
CC -!- CAUTION: The venom of this snake was originally thought to be that of
CC N.nigricollis. {ECO:0000305}.
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DR AlphaFoldDB; P14556; -.
DR SMR; P14556; -.
DR PRIDE; P14556; -.
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; Neurotoxin;
KW Secreted; Toxin.
FT CHAIN 1..118
FT /note="Basic phospholipase A2 nigexine"
FT /id="PRO_0000161672"
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; 13340 MW; FAE66EF8CF2CCA29 CRC64;
NLYQFKNMIH CTVPSRPWWH FADYGCYCGR GGKGTPIDDL DRCCQVHDNC YEKAGKMGCW
PYFTLYKYKC SKGTLTCNGR NGKCAAAVCN CDLVAANCFA GAPYINANYN IDFKKRCQ
