PA2A_DEIAC
ID PA2A_DEIAC Reviewed; 123 AA.
AC Q7SID6; Q1ZY04;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Acidic phospholipase A2;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
OS Deinagkistrodon acutus (Hundred-pace snake) (Agkistrodon acutus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Deinagkistrodon.
OX NCBI_TaxID=36307;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND VARIANTS PRO-39 AND SER-56.
RC TISSUE=Venom gland {ECO:0000269|PubMed:8931260};
RX PubMed=8931260; DOI=10.1016/0041-0101(96)00067-0;
RA Wang Y.-M., Wang J.-H., Tsai I.-H.;
RT "Molecular cloning and deduced primary structures of acidic and basic
RT phospholipases A2 from the venom of Deinagkistrodon acutus.";
RL Toxicon 34:1191-1196(1996).
RN [2] {ECO:0000312|PDB:1IJL}
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-112 IN COMPLEX WITH CALCIUM ION,
RP COFACTOR, SUBUNIT, AND DISULFIDE BONDS.
RC TISSUE=Venom;
RX PubMed=11752784; DOI=10.1107/s0907444901018170;
RA Gu L., Zhang H., Song S., Zhou Y., Lin Z.;
RT "Structure of an acidic phospholipase A2 from the venom of Deinagkistrodon
RT acutus.";
RL Acta Crystallogr. D 58:104-110(2002).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits ADP-induced
CC platelet aggregation. PLA2 catalyzes the calcium-dependent hydrolysis
CC of the 2-acyl groups in 3-sn-phosphoglycerides.
CC {ECO:0000269|PubMed:8931260}.
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:0000250|UniProtKB:P00593, ECO:0000255|PROSITE-
CC ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:11752784};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:11752784};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11752784}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8931260}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:8931260}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR EMBL; X77648; CAJ85790.1; -; mRNA.
DR PDB; 1IJL; X-ray; 2.60 A; A/B=1-123.
DR PDBsum; 1IJL; -.
DR AlphaFoldDB; Q7SID6; -.
DR SMR; Q7SID6; -.
DR EvolutionaryTrace; Q7SID6; -.
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; Calcium; Disulfide bond; Hemostasis impairing toxin;
KW Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding;
KW Platelet aggregation inhibiting toxin; Secreted; Toxin.
FT CHAIN 1..123
FT /note="Acidic phospholipase A2"
FT /id="PRO_0000235854"
FT ACT_SITE 47
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT ACT_SITE 89
FT /evidence="ECO:0000250|UniProtKB:P00593"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:11752784,
FT ECO:0007744|PDB:1IJL"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:11752784,
FT ECO:0007744|PDB:1IJL"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:11752784,
FT ECO:0007744|PDB:1IJL"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:11752784"
FT DISULFID 26..116
FT /evidence="ECO:0000305|PubMed:11752784"
FT DISULFID 28..44
FT /evidence="ECO:0000269|PubMed:11752784"
FT DISULFID 43..95
FT /evidence="ECO:0000269|PubMed:11752784"
FT DISULFID 49..123
FT /evidence="ECO:0000305|PubMed:11752784"
FT DISULFID 50..88
FT /evidence="ECO:0000269|PubMed:11752784"
FT DISULFID 57..81
FT /evidence="ECO:0000269|PubMed:11752784"
FT DISULFID 75..86
FT /evidence="ECO:0000269|PubMed:11752784"
FT VARIANT 39
FT /note="A -> P"
FT /evidence="ECO:0000269|PubMed:8931260"
FT VARIANT 56
FT /note="G -> S"
FT /evidence="ECO:0000269|PubMed:8931260"
FT HELIX 2..12
FT /evidence="ECO:0007829|PDB:1IJL"
FT HELIX 17..20
FT /evidence="ECO:0007829|PDB:1IJL"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:1IJL"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:1IJL"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:1IJL"
FT HELIX 39..51
FT /evidence="ECO:0007829|PDB:1IJL"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:1IJL"
FT STRAND 66..75
FT /evidence="ECO:0007829|PDB:1IJL"
FT HELIX 80..98
FT /evidence="ECO:0007829|PDB:1IJL"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:1IJL"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:1IJL"
FT HELIX 113..116
FT /evidence="ECO:0007829|PDB:1IJL"
SQ SEQUENCE 123 AA; 14032 MW; 4A0FA52268E7ACAD CRC64;
SLIQFETLIM KVVKKSGMFW YSAYGCYCGW GGHGRPQDAT DRCCFVHDCC YGKVTGCDPK
MDSYTYSEEN GDIVCGGDDP CKREICECDR VAAVCFRDNL DTYNSDTYWR YPTKNCQEEP
DPC
