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PA2B1_ACAAN
ID   PA2B1_ACAAN             Reviewed;         119 AA.
AC   P81236;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Basic phospholipase A2 acanthin-1;
DE            Short=svPLA2;
DE            EC=3.1.1.4;
DE   AltName: Full=Acanthin I;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
OS   Acanthophis antarcticus (Common death adder).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Acanthophiinae; Acanthophis.
OX   NCBI_TaxID=8605;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=9637731; DOI=10.1006/abbi.1998.0685;
RA   Chow G., Subburaju S., Kini R.M.;
RT   "Purification, characterization, and amino acid sequence determination of
RT   acanthins, potent inhibitors of platelet aggregation from Acanthophis
RT   antarcticus (common death adder) venom.";
RL   Arch. Biochem. Biophys. 354:232-238(1998).
CC   -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that potently inhibits
CC       ADP-(IC(50)=10 nM) and collagen-induced (IC(50)=7 nM) platelet
CC       aggregation when tested on human whole blood. PLA2 catalyzes the
CC       calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-
CC       phosphoglycerides. {ECO:0000269|PubMed:9637731}.
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   -!- MASS SPECTROMETRY: Mass=12844.58; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:9637731};
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC       D49 sub-subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P81236; -.
DR   SMR; P81236; -.
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   Calcium; Direct protein sequencing; Disulfide bond;
KW   Hemostasis impairing toxin; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Metal-binding; Platelet aggregation inhibiting toxin; Secreted; Toxin.
FT   CHAIN           1..119
FT                   /note="Basic phospholipase A2 acanthin-1"
FT                   /id="PRO_0000161591"
FT   ACT_SITE        48
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        93
FT                   /evidence="ECO:0000250"
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   BINDING         32
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         49
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   DISULFID        11..71
FT                   /evidence="ECO:0000250"
FT   DISULFID        27..118
FT                   /evidence="ECO:0000250"
FT   DISULFID        29..45
FT                   /evidence="ECO:0000250"
FT   DISULFID        44..99
FT                   /evidence="ECO:0000250"
FT   DISULFID        51..92
FT                   /evidence="ECO:0000250"
FT   DISULFID        60..85
FT                   /evidence="ECO:0000250"
FT   DISULFID        78..90
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   119 AA;  12857 MW;  229241793FA826F7 CRC64;
     DLFQFGGMIG CANKGARSWL SYVNYGCYCG WGGSGTPVDE LDRCCQIHDN CYGEAEKKQC
     GPKMTSYSWK CANDVPVCND SKSACKGFVC DCDAAAAKCF AKAPYNKNNI GIGSKTRCQ
 
 
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