ID   PA2B1_NAJNG             Reviewed;          30 AA.
AC   P0DKU3;
DT   06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2013, sequence version 1.
DT   25-MAY-2022, entry version 21.
DE   RecName: Full=Basic phospholipase A2 CM-I;
DE            Short=svPLA2;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   AltName: Full=Phospholipase A2 isozyme I;
DE   Flags: Fragment;
OS   Naja nigricollis (Black-necked 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=8654;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Venom;
RX   PubMed=7364769; DOI=10.1016/s0021-9258(19)85774-5;
RA   Evans H.J., Franson R., Qureshi G.D., Moo-Penn W.F.;
RT   "Isolation of anticoagulant proteins from cobra venom (Naja nigricollis).
RT   Identity with phospholipases A2.";
RL   J. Biol. Chem. 255:3793-3797(1980).
RN   [2]
RP   FUNCTION.
RX   PubMed=2814939; DOI=10.1016/0049-3848(89)90056-x;
RA   Stefansson S., Kini R.M., Evans H.J.;
RT   "The inhibition of clotting complexes of the extrinsic coagulation cascade
RT   by the phospholipase A2 isoenzymes from Naja nigricollis venom.";
RL   Thromb. Res. 55:481-491(1989).
RN   [3]
RP   FUNCTION.
RX   PubMed=2271532; DOI=10.1021/bi00485a024;
RA   Stefansson S., Kini R.M., Evans H.J.;
RT   "The basic phospholipase A2 from Naja nigricollis venom inhibits the
RT   prothrombinase complex by a novel nonenzymatic mechanism.";
RL   Biochemistry 29:7742-7746(1990).
RN   [4]
RP   FUNCTION.
RX   PubMed=8866616; DOI=10.1016/0041-0101(95)00103-4;
RA   Kini R.M., Evans H.J.;
RT   "The role of enzymatic activity in inhibition of the extrinsic tenase
RT   complex by phospholipase A2 isoenzymes from Naja nigricollis venom.";
RL   Toxicon 33:1585-1590(1995).
RN   [5]
RP   REVIEW.
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 weak
CC       anticoagulant activity. Is more catalytically active than the strong
CC       anticoagulant protein CM-IV found in this venom. Acts by inhibiting the
CC       complex composed of tissue factor (F3) and coagulation factor VIIa (F7)
CC       (TF-VIIa complex) by only enzymatic mechanism (PubMed:8866616). PLA2
CC       catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-
CC       sn-phosphoglycerides. {ECO:0000269|PubMed:2271532,
CC       ECO:0000269|PubMed:2814939, ECO:0000269|PubMed:8866616}.
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   -!- 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       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P0DKU3; -.
DR   SMR; P0DKU3; -.
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   Gene3D; 1.20.90.10; -; 1.
DR   InterPro; IPR001211; PLipase_A2.
DR   InterPro; IPR036444; PLipase_A2_dom_sf.
DR   PRINTS; PR00389; PHPHLIPASEA2.
DR   SUPFAM; SSF48619; SSF48619; 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; Secreted;
KW   Toxin.
FT   CHAIN           1..>30
FT                   /note="Basic phospholipase A2 CM-I"
FT                   /id="PRO_0000420886"
FT   DISULFID        11..?
FT                   /evidence="ECO:0000250"
FT   DISULFID        26..?
FT                   /evidence="ECO:0000250"
FT   DISULFID        28..?
FT                   /evidence="ECO:0000250"
FT   NON_TER         30
SQ   SEQUENCE   30 AA;  3694 MW;  9B97ECBD439F7615 CRC64;
     NLYQFKNMIH CTVPSRPWWH FADYGCYCGR