PA2AC_TRIPE
ID PA2AC_TRIPE Reviewed; 122 AA.
AC P0DJP4;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 1.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=Acidic phospholipase A2 Tpu-E6c;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE Flags: Fragments;
OS Trimeresurus puniceus (Flat-nosed pitviper).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Trimeresurus.
OX NCBI_TaxID=197218;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, SUBUNIT, AND MASS SPECTROMETRY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=15955061; DOI=10.1111/j.1742-4658.2005.04715.x;
RA Wang Y.-M., Peng H.-F., Tsai I.-H.;
RT "Unusual venom phospholipases A2 of two primitive tree vipers Trimeresurus
RT puniceus and Trimeresurus borneensis.";
RL FEBS J. 272:3015-3025(2005).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that impairs hemostasis.
CC It weakly inhibits ADP-induced platelet aggregation when tested on
CC platelet rich plasma from human and rabbit blood (15-25% of inhibition
CC at 5-10 ug of enzyme), and dose-dependently inhibits blood coagulation,
CC possibly by inhibiting thrombin activation. Exhibits high hydrolytic
CC activities toward L-dipalmitoyl phosphatidylcholine. PLA2 catalyzes the
CC calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-
CC phosphoglycerides. {ECO:0000269|PubMed:15955061}.
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 -!- 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:15955061}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: Mass=13792.8; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:15955061};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; P0DJP4; -.
DR SMR; P0DJP4; -.
DR PRIDE; P0DJP4; -.
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.
PE 1: Evidence at protein level;
KW Blood coagulation cascade inhibiting toxin; Direct protein sequencing;
KW Disulfide bond; Hemostasis impairing toxin; Hydrolase; Lipid degradation;
KW Lipid metabolism; Metal-binding; Platelet aggregation inhibiting toxin;
KW Secreted; Toxin.
FT CHAIN 1..122
FT /note="Acidic phospholipase A2 Tpu-E6c"
FT /id="PRO_0000419060"
FT ACT_SITE 47
FT /evidence="ECO:0000250"
FT ACT_SITE 89
FT /evidence="ECO:0000250"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 26..115
FT /evidence="ECO:0000250"
FT DISULFID 28..44
FT /evidence="ECO:0000250"
FT DISULFID 43..95
FT /evidence="ECO:0000250"
FT DISULFID 49..122
FT /evidence="ECO:0000250"
FT DISULFID 50..88
FT /evidence="ECO:0000250"
FT DISULFID 57..81
FT /evidence="ECO:0000250"
FT DISULFID 75..86
FT /evidence="ECO:0000250"
FT UNSURE 65..66
FT NON_CONS 23..24
FT /evidence="ECO:0000305"
SQ SEQUENCE 122 AA; 13808 MW; 2F62C295B4CBFA62 CRC64;
NLLQFEMMIL KMAGRSGIRW YSDYGCYCGK GGHGQPQDAT DRCCFVHDCC YGKVSGCDPK
DEFYKYSSDN NDIVCGGNNP CLKEICECDR DAAICFRDNL STYNNKYWNV PSETCQVESE
PC
