PA2AI_TRIST
ID PA2AI_TRIST Reviewed; 122 AA.
AC Q6H3C6;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Acidic phospholipase A2 CTs-A3;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
OS Trimeresurus stejnegeri (Chinese green tree viper) (Viridovipera
OS stejnegeri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Trimeresurus.
OX NCBI_TaxID=39682;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-23, FUNCTION, AND MASS
RP SPECTROMETRY.
RC STRAIN=Chinese; TISSUE=Venom, and Venom gland;
RX PubMed=12959640; DOI=10.1042/bj20030818;
RA Tsai I.-H., Wang Y.-M., Chen Y.-H., Tsai T.-S., Tu M.-C.;
RT "Venom phospholipases A2 of bamboo viper (Trimeresurus stejnegeri):
RT molecular characterization, geographic variations and evidence of multiple
RT ancestries.";
RL Biochem. J. 377:215-223(2004).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that shows a moderate
CC inhibition of ADP-induced human platelet aggregation when tested on
CC platelet rich plasma. Exhibits moderate hydrolytic activities and
CC prefers the anionic micelles (dPPC with deoxycholate) to the
CC zwitterionic micelles (dPPC with Triton X-100). PLA2 catalyzes the
CC calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-
CC phosphoglycerides. {ECO:0000269|PubMed:12959640}.
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=13776; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:12959640};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR EMBL; AY211943; AAP48901.1; -; mRNA.
DR AlphaFoldDB; Q6H3C6; -.
DR SMR; Q6H3C6; -.
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;
KW Hemostasis impairing toxin; Hydrolase; Lipid degradation; Lipid metabolism;
KW Metal-binding; Platelet aggregation inhibiting toxin; Secreted; Toxin.
FT CHAIN 1..122
FT /note="Acidic phospholipase A2 CTs-A3"
FT /id="PRO_0000419073"
FT ACT_SITE 47
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT ACT_SITE 89
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT DISULFID 26..116
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT DISULFID 28..44
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT DISULFID 43..95
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT DISULFID 49..122
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT DISULFID 50..88
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT DISULFID 57..81
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT DISULFID 75..86
FT /evidence="ECO:0000250|UniProtKB:P14418"
SQ SEQUENCE 122 AA; 13790 MW; 698684B6B0FF20D3 CRC64;
SLIQFETLIM KVAKKSGMFS YSAYGCYCGW GGQGQPQDPT DRCCFVHDCC YGKVTGCDPK
MDIYTYSEEN GDIVCGGDDP CRKAVCECDK AAAICFRDNK DTYDWKKYWR FPTKNCQESV
PC
