PA2A_GLOHA
ID PA2A_GLOHA Reviewed; 124 AA.
AC P14418;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Acidic phospholipase A2;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=APLA2;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
OS Gloydius halys (Chinese water mocassin) (Agkistrodon halys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Gloydius.
OX NCBI_TaxID=8714;
RN [1]
RP PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=3617077; DOI=10.1016/0041-0101(87)90073-0;
RA Chen Y.-C., Maraganore J.M., Reardon I., Heinrikson R.L.;
RT "Characterization of the structure and function of three phospholipases A2
RT from the venom of Agkistrodon halys pallas.";
RL Toxicon 25:401-409(1987).
RN [2]
RP PROTEIN SEQUENCE OF 1-114, FUNCTION, BIOASSAY, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=18456297; DOI=10.1016/j.toxicon.2008.01.003;
RA Wang Y., Cui G., Zhao M., Yang J., Wang C., Giese R.W., Peng S.;
RT "Bioassay-directed purification of an acidic phospholipase A(2) from
RT Agkistrodon halys pallas venom.";
RL Toxicon 51:1131-1139(2008).
RN [3] {ECO:0000312|PDB:1PSJ}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH CALCIUM ION,
RP COFACTOR, AND DISULFIDE BONDS.
RC TISSUE=Venom;
RX PubMed=8636969; DOI=10.1006/jmbi.1996.0054;
RA Wang X.-Q., Yang J., Gui L.-L., Lin Z.-J., Chen Y.-C., Zhou Y.-C.;
RT "Crystal structure of an acidic phospholipase A2 from the venom of
RT Agkistrodon halys pallas at 2.0-A resolution.";
RL J. Mol. Biol. 255:669-676(1996).
RN [4] {ECO:0000312|PDB:1BK9}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH CALCIUM ION,
RP COFACTOR, AND DISULFIDE BONDS.
RC TISSUE=Venom;
RX PubMed=9663694; DOI=10.1016/s0041-0101(97)00169-4;
RA Zhao H., Tang L., Wang X., Zhou Y., Lin Z.;
RT "Structure of a snake venom phospholipase A2 modified by p-bromo-phenacyl-
RT bromide.";
RL Toxicon 36:875-886(1998).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that acts in vivo as an
CC anti-thrombotic agent. Inhibits platelet aggregation induced by ADP,
CC arachidonic acid, and thrombin. PLA2 catalyzes the calcium-dependent
CC hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
CC {ECO:0000269|PubMed:18456297}.
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;
CC Evidence={ECO:0000305|PubMed:8636969, ECO:0000305|PubMed:9663694};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000305|PubMed:8636969,
CC ECO:0000305|PubMed:9663694};
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3617077}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:3617077}.
CC -!- MASS SPECTROMETRY: Mass=13962; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:18456297};
CC -!- PHARMACEUTICAL: The venom of this snake has been orally administered to
CC patients in China for about 2000 years, mostly to treat thrombotic
CC diseases.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR PIR; A26535; A26535.
DR PDB; 1BK9; X-ray; 2.00 A; A=1-124.
DR PDB; 1PSJ; X-ray; 2.00 A; A=1-124.
DR PDBsum; 1BK9; -.
DR PDBsum; 1PSJ; -.
DR AlphaFoldDB; P14418; -.
DR SMR; P14418; -.
DR BRENDA; 3.1.1.4; 195.
DR EvolutionaryTrace; P14418; -.
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 3D-structure; Blood coagulation cascade inhibiting toxin; Calcium;
KW Direct protein sequencing; Disulfide bond; Hemostasis impairing toxin;
KW Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding;
KW Pharmaceutical; Platelet aggregation inhibiting toxin; Secreted; Toxin.
FT CHAIN 1..124
FT /note="Acidic phospholipase A2"
FT /evidence="ECO:0000269|PubMed:3617077"
FT /id="PRO_0000161597"
FT ACT_SITE 47
FT /evidence="ECO:0000250|UniProtKB:P06859"
FT ACT_SITE 89
FT /evidence="ECO:0000250|UniProtKB:P06859"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:8636969,
FT ECO:0000269|PubMed:9663694, ECO:0007744|PDB:1BK9,
FT ECO:0007744|PDB:1PSJ"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:8636969,
FT ECO:0000269|PubMed:9663694, ECO:0007744|PDB:1BK9,
FT ECO:0007744|PDB:1PSJ"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:8636969,
FT ECO:0000269|PubMed:9663694, ECO:0007744|PDB:1BK9,
FT ECO:0007744|PDB:1PSJ"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:8636969,
FT ECO:0000269|PubMed:9663694, ECO:0007744|PDB:1BK9,
FT ECO:0007744|PDB:1PSJ"
FT DISULFID 26..116
FT /evidence="ECO:0000269|PubMed:8636969,
FT ECO:0000269|PubMed:9663694, ECO:0007744|PDB:1BK9,
FT ECO:0007744|PDB:1PSJ"
FT DISULFID 28..44
FT /evidence="ECO:0000269|PubMed:8636969,
FT ECO:0000269|PubMed:9663694, ECO:0007744|PDB:1BK9,
FT ECO:0007744|PDB:1PSJ"
FT DISULFID 43..95
FT /evidence="ECO:0000269|PubMed:8636969,
FT ECO:0000269|PubMed:9663694, ECO:0007744|PDB:1BK9,
FT ECO:0007744|PDB:1PSJ"
FT DISULFID 49..124
FT /evidence="ECO:0000269|PubMed:8636969,
FT ECO:0000269|PubMed:9663694, ECO:0007744|PDB:1BK9,
FT ECO:0007744|PDB:1PSJ"
FT DISULFID 50..88
FT /evidence="ECO:0000269|PubMed:8636969,
FT ECO:0000269|PubMed:9663694, ECO:0007744|PDB:1BK9,
FT ECO:0007744|PDB:1PSJ"
FT DISULFID 57..81
FT /evidence="ECO:0000269|PubMed:8636969,
FT ECO:0000269|PubMed:9663694, ECO:0007744|PDB:1BK9,
FT ECO:0007744|PDB:1PSJ"
FT DISULFID 75..86
FT /evidence="ECO:0000269|PubMed:8636969,
FT ECO:0000269|PubMed:9663694, ECO:0007744|PDB:1BK9,
FT ECO:0007744|PDB:1PSJ"
FT CONFLICT 101..102
FT /note="TL -> NT (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 2..13
FT /evidence="ECO:0007829|PDB:1BK9"
FT HELIX 17..20
FT /evidence="ECO:0007829|PDB:1BK9"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:1BK9"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:1BK9"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:1BK9"
FT HELIX 39..52
FT /evidence="ECO:0007829|PDB:1BK9"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:1BK9"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:1BK9"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:1BK9"
FT HELIX 80..98
FT /evidence="ECO:0007829|PDB:1BK9"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:1BK9"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:1BK9"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:1BK9"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:1BK9"
SQ SEQUENCE 124 AA; 13974 MW; 34BE769D31A45D26 CRC64;
SLIQFETLIM KVAKKSGMFW YSNYGCYCGW GGQGRPQDAT DRCCFVHDCC YGKVTGCDPK
MDVYSFSEEN GDIVCGGDDP CKKEICECDR AAAICFRDNL TLYNDKKYWA FGAKNCPQEE
SEPC
