PA2A1_WALAE
ID PA2A1_WALAE Reviewed; 137 AA.
AC C1IC46;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Acidic phospholipase A2 PL-I;
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 (793 umol/mg/min) to the zwitterionic micelles (dPPC with Triton X-100)
CC (591 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=13342; 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; EU196554; ABX82863.1; -; mRNA.
DR AlphaFoldDB; C1IC46; -.
DR SMR; C1IC46; -.
DR TopDownProteomics; C1IC46; -.
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-I"
FT /id="PRO_5000456111"
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; 15034 MW; 08CF47B383FEE35F CRC64;
AVCVSLLGAS SIRPLPLHLG QFNNMIKCTI PGSTPWWDFS DYGCYCGYGG SGTPVDQLDR
CCQTHDNCYT EAQKFSGCSP YTRKYSYECS EGTLTCKSDN DECAAFVCNC DRSAAICFAR
APYNSNNVDI DLEAHCQ
