ID   PA2A2_WALAE             Reviewed;         137 AA.
AC   C1IC45;
DT   03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=Acidic phospholipase A2 PL-II;
DE            Short=svPLA2;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   Flags: Precursor; Fragment;
OS   Walterinnesia aegyptia (Desert black snake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Walterinnesia.
OX   NCBI_TaxID=64182;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MASS SPECTROMETRY.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=18405934; DOI=10.1016/j.toxicon.2008.02.012;
RA   Tsai H.-Y., Wang Y.M., Tsai I.-H.;
RT   "Cloning, characterization and phylogenetic analyses of members of three
RT   major venom families from a single specimen of Walterinnesia aegyptia.";
RL   Toxicon 51:1245-1254(2008).
CC   -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that may act in the
CC       hemostasis system of the prey (By similarity). Exhibits hydrolytic
CC       activities, and prefers the anionic micelles (dPPC with deoxycholate)
CC       (54 umol/mg/min) to the zwitterionic micelles (dPPC with Triton X-100)
CC       (15 umol/mg/min). PLA2 catalyzes the calcium-dependent hydrolysis of
CC       the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000250,
CC       ECO:0000269|PubMed:18405934}.
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=13343; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:18405934};
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC       D49 sub-subfamily. {ECO:0000305}.
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DR   EMBL; EU196553; ABX82862.1; -; mRNA.
DR   AlphaFoldDB; C1IC45; -.
DR   SMR; C1IC45; -.
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; Disulfide bond; Hemostasis impairing toxin; Hydrolase;
KW   Lipid degradation; Lipid metabolism; Metal-binding; Secreted; Signal;
KW   Toxin.
FT   SIGNAL          <1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..137
FT                   /note="Acidic phospholipase A2 PL-II"
FT                   /id="PRO_5000456110"
FT   ACT_SITE        65
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        111
FT                   /evidence="ECO:0000250"
FT   BINDING         45
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         47
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   BINDING         66
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   DISULFID        28..89
FT                   /evidence="ECO:0000250"
FT   DISULFID        44..136
FT                   /evidence="ECO:0000250"
FT   DISULFID        46..62
FT                   /evidence="ECO:0000250"
FT   DISULFID        61..117
FT                   /evidence="ECO:0000250"
FT   DISULFID        68..110
FT                   /evidence="ECO:0000250"
FT   DISULFID        78..103
FT                   /evidence="ECO:0000250"
FT   DISULFID        96..108
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   137 AA;  15035 MW;  D025BAE583FEE35B CRC64;
     AVCVSLLGAS SIRPLPLHLG QFNNMIKCTI PGSTPWWDFS DYGCYCGYGG SGTPVDQLDR
     CCQTHDNCYT EAQKFSGCSP YRRKYSYECS EGTLTCKSDN DECAAFVCNC DRLAAICFAG
     APYNSNNVDI DLEARCQ