PA2BA_PSETE
ID PA2BA_PSETE Reviewed; 145 AA.
AC P23026; C7S7C0;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 3.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Basic phospholipase A2 textilotoxin A chain;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE Flags: Precursor;
OS Pseudonaja textilis (Eastern brown snake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Acanthophiinae; Pseudonaja.
OX NCBI_TaxID=8673;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA St Pierre L.;
RT "Identification of the subunits of textilotoxin from the common brown
RT snake, Pseudonaja textilis.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 28-145, FUNCTION, AND TOXIC DOSE.
RC TISSUE=Venom;
RX PubMed=8431471; DOI=10.1016/0167-4838(93)90217-f;
RA Pearson J.A., Tyler M.I., Retson K.V., Howden M.E.H.;
RT "Studies on the subunit structure of textilotoxin, a potent presynaptic
RT neurotoxin from the venom of the Australian common brown snake (Pseudonaja
RT textilis). 3. The complete amino-acid sequences of all the subunits.";
RL Biochim. Biophys. Acta 1161:223-229(1993).
RN [3]
RP PROTEIN SEQUENCE OF 28-145.
RC TISSUE=Venom;
RX PubMed=3651474; DOI=10.1016/0167-4838(87)90302-5;
RA Tyler M.I., Barnett D., Nicholson P., Spence I., Howden M.E.H.;
RT "Studies on the subunit structure of textilotoxin, a potent neurotoxin from
RT the venom of the Australian common brown snake (Pseudonaja textilis).";
RL Biochim. Biophys. Acta 915:210-216(1987).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=16284125; DOI=10.1074/mcp.m500270-mcp200;
RA Birrell G.W., Earl S., Masci P.P., de Jersey J., Wallis T.P., Gorman J.J.,
RA Lavin M.F.;
RT "Molecular diversity in venom from the Australian Brown snake, Pseudonaja
RT textilis.";
RL Mol. Cell. Proteomics 5:379-389(2006).
RN [5]
RP SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=18951409; DOI=10.1002/prot.22259;
RA Aquilina J.A.;
RT "The major toxin from the Australian common brown snake is a hexamer with
RT unusual gas-phase dissociation properties.";
RL Proteins 75:478-485(2009).
CC -!- FUNCTION: Snake venom oligomeric phospholipase A2 that has potent
CC presynaptic neurotoxicity. Chain A possesses a very low toxicity, but
CC is essential for neurotoxicity. Possesses a low enzymatic activity.
CC PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in
CC 3-sn-phosphoglycerides. {ECO:0000269|PubMed:8431471}.
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 -!- SUBUNIT: Heterohexamer. 2 forms exist: 2 A or 2 B chains, 2 C chains
CC and 2 covalently-linked D chains, and 1 A or 1 B, 1 C, 2 covalently-
CC linked D chains and 2 differentially glycosylated covalently-linked D
CC chains. Textilotoxin was originally described as pentameric
CC (PubMed:8431471). {ECO:0000269|PubMed:18951409,
CC ECO:0000269|PubMed:8431471}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- TOXIC DOSE: Oligomer: LD(50) is 1 ug/kg by intraperitoneal injection
CC into mice. {ECO:0000269|PubMed:8431471}.
CC -!- TOXIC DOSE: Monomer: LD(50) is 4 mg/kg by intravenous injection into
CC mice. {ECO:0000269|PubMed:8431471}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR EMBL; EU523132; ACD36029.1; -; mRNA.
DR PIR; S29651; S29651.
DR AlphaFoldDB; P23026; -.
DR SMR; P23026; -.
DR Proteomes; UP000472273; Unplaced.
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; Hydrolase;
KW Lipid degradation; Lipid metabolism; Metal-binding; Neurotoxin;
KW Presynaptic neurotoxin; Reference proteome; Secreted; Signal; Toxin.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..27
FT /evidence="ECO:0000269|PubMed:3651474,
FT ECO:0000269|PubMed:8431471"
FT /id="PRO_0000420145"
FT CHAIN 28..145
FT /note="Basic phospholipase A2 textilotoxin A chain"
FT /id="PRO_0000161694"
FT ACT_SITE 75
FT /evidence="ECO:0000250"
FT ACT_SITE 119
FT /evidence="ECO:0000250"
FT BINDING 55
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 57
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 38..98
FT /evidence="ECO:0000250"
FT DISULFID 54..144
FT /evidence="ECO:0000250"
FT DISULFID 56..72
FT /evidence="ECO:0000250"
FT DISULFID 71..125
FT /evidence="ECO:0000250"
FT DISULFID 78..118
FT /evidence="ECO:0000250"
FT DISULFID 87..111
FT /evidence="ECO:0000250"
FT DISULFID 105..116
FT /evidence="ECO:0000250"
FT CONFLICT 95
FT /note="Y -> N (in Ref. 2; AA sequence and 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="R -> Q (in Ref. 2; AA sequence and 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 145 AA; 16684 MW; 58418ACC29F521F4 CRC64;
MHPAHLLVLL GVCVSLLGAS DIPPLPLNLV QFSYLIRCAN KYKRPGWHYA NYGCYCGSGG
RGTPVDDVDR CCQAHDKCYE DAEKLGCYPK WTTYYYYCGA NGPYCKTRTK CQRFVCNCDV
VAADCFASYP YNRRYWFYSN KKRCR
