PA21_CERGO
ID PA21_CERGO Reviewed; 39 AA.
AC P0DQP6;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 02-JUN-2021, sequence version 1.
DT 03-AUG-2022, entry version 5.
DE RecName: Full=Basic phospholipase A2;
DE Short=svPLA2;
DE EC=3.1.1.4 {ECO:0000269|PubMed:1524423};
DE AltName: Full=Myotoxin I {ECO:0000303|PubMed:10698689, ECO:0000303|PubMed:1524423};
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE Flags: Fragment;
OS Cerrophidion godmani (Porthidium godmani) (Bothrops godmani).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Cerrophidion.
OX NCBI_TaxID=44722;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=10698689; DOI=10.1042/bj3460631;
RA Lizano S., Angulo Y., Lomonte B., Fox J.W., Lambeau G., Lazdunski M.,
RA Gutierrez J.M.;
RT "Two phospholipase A2 inhibitors from the plasma of Cerrophidion (Bothrops)
RT godmani which selectively inhibit two different group-II phospholipase A2
RT myotoxins from its own venom: isolation, molecular cloning and biological
RT properties.";
RL Biochem. J. 346:631-639(2000).
RN [2]
RP AMINO-ACID COMPOSITION, FUNCTION, AND CATALYTIC ACTIVITY.
RC TISSUE=Venom;
RX PubMed=1524423; DOI=10.1016/0003-9861(92)90104-5;
RA Diaz C., Gutierrez J.M., Lomonte B.;
RT "Isolation and characterization of basic myotoxic phospholipases A2 from
RT Bothrops godmani (Godman's pit viper) snake venom.";
RL Arch. Biochem. Biophys. 298:135-142(1992).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that shows high myotoxic
CC activities, induces mild edema, and shows cytolytic, and anti-coagulant
CC activities, as well as intracerebral lethal effect (PubMed:10698689,
CC PubMed:1524423). Does not induce lethality at a dose of 5 ug/g, when
CC intravenously injected into mice (PubMed:1524423). PLA2 catalyzes the
CC calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-
CC phosphoglycerides (PubMed:1524423). {ECO:0000269|PubMed:10698689,
CC ECO:0000269|PubMed:1524423}.
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:0000269|PubMed:1524423};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:1524423};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Is selectively inhibited by the gamma-
CC phospholipase A2 inhibitor (PLI) CgMIP-I (AC P0DQP7) but not by the
CC alpha-PLI CgMIP-II (AC P0DQP8). {ECO:0000269|PubMed:10698689}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10698689}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:10698689}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0DQP6; -.
DR SMR; P0DQP6; -.
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; IPR016090; PLipase_A2_dom.
DR InterPro; IPR036444; PLipase_A2_dom_sf.
DR Pfam; PF00068; Phospholip_A2_1; 1.
DR PRINTS; PR00389; PHPHLIPASEA2.
DR SUPFAM; SSF48619; SSF48619; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Lipid degradation; Lipid metabolism; Metal-binding; Myotoxin; Secreted;
KW Toxin.
FT CHAIN 1..>39
FT /note="Basic phospholipase A2"
FT /evidence="ECO:0000269|PubMed:10698689"
FT /id="PRO_0000452707"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT DISULFID 26..?
FT /evidence="ECO:0000305"
FT DISULFID 28..?
FT /evidence="ECO:0000305"
FT NON_TER 39
FT /evidence="ECO:0000305"
SQ SEQUENCE 39 AA; 4403 MW; 596FD5389A3EBDED CRC64;
HLFQFREMIK EMTGKEPVVS YAFYGCYCGK GGRGKPDAT
