PA2A_TRIGS
ID PA2A_TRIGS Reviewed; 139 AA.
AC A8E2V8;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Acidic phospholipase A2 Tgc-E6;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE Flags: Precursor;
OS Trimeresurus gracilis (Kikuchi habu).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Trimeresurus.
OX NCBI_TaxID=109781;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-46, FUNCTION, SUBUNIT,
RP AND MASS SPECTROMETRY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=22115990; DOI=10.1016/j.toxicon.2011.10.016;
RA Tsai I.-H., Tsai T.-S., Wang Y.-M., Tu M.-C., Chang H.-C.;
RT "Cloning and characterization of Trimeresurus gracilis venom phospholipases
RT A(2): comparison with Ovophis okinavensis venom and the systematic
RT implications.";
RL Toxicon 59:151-157(2012).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits the ADP-
CC (IC(50)=272 nM) and collagen-induced (IC(50)=518 nM) human platelet
CC aggregation in platelet rich plasma. Exhibits very high hydrolytic
CC activities toward the synthetic lecithin, and prefers the anionic
CC micelles (dPPC with deoxycholate) to the zwitterionic micelles (dPPC
CC with Triton X-100). PLA2 catalyzes the calcium-dependent hydrolysis of
CC the 2-acyl groups in 3-sn-phosphoglycerides.
CC {ECO:0000269|PubMed:22115990}.
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: Monomer. {ECO:0000269|PubMed:22115990}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: Mass=13891; Method=MALDI; Note=Oxidized forms with
CC mass increases of 16, 32 and 48 are also detected.;
CC Evidence={ECO:0000269|PubMed:22115990};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR EMBL; AY764141; AAW92121.1; -; mRNA.
DR AlphaFoldDB; A8E2V8; -.
DR SMR; A8E2V8; -.
DR GO; GO:0005576; C:extracellular region; TAS:UniProtKB.
DR GO; GO:0043655; C:host extracellular space; TAS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; NAS:UniProtKB.
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:0044477; P:envenomation resulting in negative regulation of platelet aggregation in another organism; IDA:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IDA:UniProtKB.
DR GO; GO:0006644; P:phospholipid metabolic process; IDA:UniProtKB.
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; Metal-binding;
KW Platelet aggregation inhibiting toxin; Secreted; Signal; Toxin.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:22115990"
FT CHAIN 17..139
FT /note="Acidic phospholipase A2 Tgc-E6"
FT /id="PRO_0000419052"
FT ACT_SITE 63
FT /evidence="ECO:0000250|UniProtKB:P06859"
FT ACT_SITE 105
FT /evidence="ECO:0000250|UniProtKB:P06859"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 42..132
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 44..60
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 59..111
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 65..139
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 66..104
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 73..97
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 91..102
FT /evidence="ECO:0000250|UniProtKB:O42191"
SQ SEQUENCE 139 AA; 15689 MW; 7E0672B83F05D0B4 CRC64;
MRTLWIMAVL LLGVEGSLMQ FEMLIMKLAK SSGMFWYSAY GCYCGWGGQG RPQDATDRCC
FVHDCCYGKA TGCDPKKDVY TYSEENGDIV CGGDDPCRKE VCECDKAAAI CFRDNMDTYN
SKTYWMFPAK NCQEESEPC
