PA22_ACASS
ID PA22_ACASS Reviewed; 30 AA.
AC P85060;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Phospholipase A2 acanmyotoxin-2;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE Flags: Fragment;
OS Acanthophis sp. (strain Seram) (Seram death adder).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Acanthophiinae; Acanthophis;
OC unclassified Acanthophis.
OX NCBI_TaxID=412080;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RC TISSUE=Venom {ECO:0000269|PubMed:16242671};
RX PubMed=16242671; DOI=10.1016/j.bcp.2005.09.017;
RA Hart A.J., Smith A.I., Reeve S., Hodgson W.C.;
RT "Isolation and characterisation of acanmyotoxin-2 and acanmyotoxin-3,
RT myotoxins from the venom of the death adder Acanthophis sp. Seram.";
RL Biochem. Pharmacol. 70:1807-1813(2005).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that has myotoxic
CC activity but no significant neurotoxicity. PLA2 catalyzes the calcium-
CC dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
CC {ECO:0000269|PubMed:16242671}.
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, ECO:0000269|PubMed:16242671};
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 {ECO:0000269|PubMed:16242671}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:16242671}.
CC -!- PTM: Contains seven disulfide bonds. {ECO:0000250|UniProtKB:P81236}.
CC -!- MASS SPECTROMETRY: Mass=13082; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:16242671};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC {ECO:0000255}.
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DR AlphaFoldDB; P85060; -.
DR SMR; P85060; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004623; F:phospholipase A2 activity; IDA:UniProtKB.
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 GO; GO:0006937; P:regulation of muscle contraction; IDA:UniProtKB.
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 Calcium; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Lipid degradation; Lipid metabolism; Metal-binding; Myotoxin; Secreted;
KW Toxin.
FT CHAIN 1..>30
FT /note="Phospholipase A2 acanmyotoxin-2"
FT /id="PRO_0000271910"
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 NON_TER 30
FT /evidence="ECO:0000303|PubMed:16242671"
SQ SEQUENCE 30 AA; 3327 MW; B40296DD1B81149D CRC64;
NLYQFGGMIG CANKGTRSWL SYVNYGCYCG
