PA2A5_TRIST
ID PA2A5_TRIST Reviewed; 122 AA.
AC P82896;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Acidic phospholipase A2 5 {ECO:0000305};
DE Short=svPLA2;
DE EC=3.1.1.4 {ECO:0000269|PubMed:25447533};
DE AltName: Full=PA2-Vb {ECO:0000303|PubMed:25447533};
DE AltName: Full=PLA2-V {ECO:0000303|Ref.1};
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 PROTEIN SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RA Li S.-Y., Guo Z.-X., Yang Y.-Y., Wang W.-Y., Xiong Y.-L.;
RT "Isolation and sequencing of five variants of phospholipase A2 from venom
RT of snake Trimeresurus stejnegeri.";
RL J. Hubei Univ. 25:63-68(2003).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS), CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=25447533; DOI=10.1016/j.febslet.2014.10.032;
RA Zeng F., Zhang W., Xue N., Teng M., Li X., Shen B.;
RT "Crystal structure of phospholipase PA2-Vb, a protease-activated receptor
RT agonist from the Trimeresurus stejnegeri snake venom.";
RL FEBS Lett. 588:4604-4612(2014).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits platelet
CC aggregation induced by ADP, arachidonic acid and PAF (Ref.1). Acts in a
CC enzymatic independent manner on a proteinase-activated receptor (PAR1,
CC F2R) to evoke calcium release through the inositol 1,4,5-trisphosphate
CC receptor (ITPR1, IP3R) and induces mouse aorta contraction
CC (PubMed:25447533). PAR1, phospholipase C and IP3R inhibitors suppress
CC PA2-induced aorta contraction (PubMed:25447533). PLA2 catalyzes the
CC calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-
CC phosphoglycerides. {ECO:0000269|PubMed:25447533, ECO:0000269|Ref.1}.
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, ECO:0000269|PubMed:25447533};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Preincubation with heparin slightly increase the
CC enzymatic activity. {ECO:0000269|PubMed:25447533}.
CC -!- SUBUNIT: Monomer (predominant). Non-covalently linked homodimers are
CC also observed. {ECO:0000269|PubMed:25447533}.
CC -!- INTERACTION:
CC P82896; P82896: -; NbExp=2; IntAct=EBI-10105591, EBI-10105591;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25447533,
CC ECO:0000269|Ref.1}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:25447533, ECO:0000305|Ref.1}.
CC -!- MISCELLANEOUS: Hemolytic and neurotoxic activities are not detected.
CC {ECO:0000269|Ref.1}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR PDB; 4RFP; X-ray; 1.60 A; A/B=1-122.
DR PDBsum; 4RFP; -.
DR AlphaFoldDB; P82896; -.
DR SMR; P82896; -.
DR MINT; P82896; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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 3D-structure; 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 5"
FT /id="PRO_0000161711"
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:0007744|PDB:4RFP"
FT DISULFID 28..44
FT /evidence="ECO:0007744|PDB:4RFP"
FT DISULFID 43..95
FT /evidence="ECO:0007744|PDB:4RFP"
FT DISULFID 49..122
FT /evidence="ECO:0007744|PDB:4RFP"
FT DISULFID 50..88
FT /evidence="ECO:0007744|PDB:4RFP"
FT DISULFID 57..81
FT /evidence="ECO:0007744|PDB:4RFP"
FT DISULFID 75..86
FT /evidence="ECO:0007744|PDB:4RFP"
FT HELIX 2..13
FT /evidence="ECO:0007829|PDB:4RFP"
FT HELIX 17..20
FT /evidence="ECO:0007829|PDB:4RFP"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:4RFP"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:4RFP"
FT HELIX 39..52
FT /evidence="ECO:0007829|PDB:4RFP"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:4RFP"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:4RFP"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:4RFP"
FT HELIX 80..98
FT /evidence="ECO:0007829|PDB:4RFP"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:4RFP"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:4RFP"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:4RFP"
SQ SEQUENCE 122 AA; 13880 MW; 8B20A1D3907EB522 CRC64;
NLMQFELLIM KVAGRSGIVW YSDYGCFCGK GGHGRPQDAT DRCCFVHDCC YGKVTECDPK
MDFYRYSSNN GDIVCEANNP CTKEICECDK AAAICFRDNK DTYDNKYWNI PMEGCQEESE
PC
