PA2A1_OPHHA
ID PA2A1_OPHHA Reviewed; 151 AA.
AC P80966; Q9DF32;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Acidic phospholipase A2 1;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=APLA2-1;
DE AltName: Full=OHV A-PLA2;
DE Short=OHV-APLA2;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE Flags: Precursor;
OS Ophiophagus hannah (King cobra) (Naja hannah).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX NCBI_TaxID=8665;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Wang Q.Y., Shu Y.Y.;
RT "Cloning and characterization of cDNAs encoding two acidic isoforms of
RT phospholipase A2 in Guangxi king cobra (Ophiophagus hannah).";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 28-151, FUNCTION, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=9028866; DOI=10.1006/abbi.1996.9814;
RA Huang M.Z., Gopalakrishnakone P., Chung M.C.M., Kini R.M.;
RT "Complete amino acid sequence of an acidic, cardiotoxic phospholipase A2
RT from the venom of Ophiophagus hannah (King Cobra): a novel cobra venom
RT enzyme with 'pancreatic loop'.";
RL Arch. Biochem. Biophys. 338:150-156(1997).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH CALCIUM ION,
RP COFACTOR, AND DISULFIDE BONDS.
RX PubMed=12217659; DOI=10.1016/s1047-8477(02)00022-9;
RA Zhang H.L., Xu S.J., Wang Q.Y., Song S.Y., Shu Y.Y., Lin Z.J.;
RT "Structure of a cardiotoxic phospholipase A(2) from Ophiophagus hannah with
RT the 'pancreatic loop'.";
RL J. Struct. Biol. 138:207-215(2002).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that may exhibit
CC cardiotoxicity, myotoxicity, antiplatelet activity, and edema-inducing
CC activity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:9028866}.
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:0000269|PubMed:12217659};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000269|PubMed:12217659};
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: Mass=13720.47; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:9028866};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR EMBL; AF302908; AAG23964.1; -; mRNA.
DR PDB; 1GP7; X-ray; 2.60 A; A/B/C=1-151.
DR PDBsum; 1GP7; -.
DR AlphaFoldDB; P80966; -.
DR SMR; P80966; -.
DR PRIDE; P80966; -.
DR EvolutionaryTrace; P80966; -.
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; Cardiotoxin; Direct protein sequencing;
KW Disulfide bond; Hemostasis impairing toxin; Hydrolase; Lipid degradation;
KW Lipid metabolism; Metal-binding; Myotoxin;
KW Platelet aggregation inhibiting toxin; Secreted; Signal; Toxin.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..27
FT /evidence="ECO:0000269|PubMed:9028866"
FT /id="PRO_0000022942"
FT CHAIN 28..151
FT /note="Acidic phospholipase A2 1"
FT /id="PRO_0000022943"
FT ACT_SITE 75
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT ACT_SITE 126
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT BINDING 55
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12217659,
FT ECO:0007744|PDB:1GP7"
FT BINDING 57
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12217659,
FT ECO:0007744|PDB:1GP7"
FT BINDING 59
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12217659,
FT ECO:0007744|PDB:1GP7"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12217659,
FT ECO:0007744|PDB:1GP7"
FT DISULFID 38..104
FT /evidence="ECO:0000269|PubMed:12217659,
FT ECO:0007744|PDB:1GP7"
FT DISULFID 54..151
FT /evidence="ECO:0000269|PubMed:12217659,
FT ECO:0007744|PDB:1GP7"
FT DISULFID 56..72
FT /evidence="ECO:0000269|PubMed:12217659,
FT ECO:0007744|PDB:1GP7"
FT DISULFID 71..132
FT /evidence="ECO:0000269|PubMed:12217659,
FT ECO:0007744|PDB:1GP7"
FT DISULFID 78..125
FT /evidence="ECO:0000269|PubMed:12217659,
FT ECO:0007744|PDB:1GP7"
FT DISULFID 88..118
FT /evidence="ECO:0000269|PubMed:12217659,
FT ECO:0007744|PDB:1GP7"
FT DISULFID 111..123
FT /evidence="ECO:0000269|PubMed:12217659,
FT ECO:0007744|PDB:1GP7"
FT HELIX 29..39
FT /evidence="ECO:0007829|PDB:1GP7"
FT HELIX 46..49
FT /evidence="ECO:0007829|PDB:1GP7"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:1GP7"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:1GP7"
FT HELIX 67..84
FT /evidence="ECO:0007829|PDB:1GP7"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:1GP7"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:1GP7"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:1GP7"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:1GP7"
FT HELIX 117..134
FT /evidence="ECO:0007829|PDB:1GP7"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:1GP7"
FT HELIX 147..150
FT /evidence="ECO:0007829|PDB:1GP7"
SQ SEQUENCE 151 AA; 16444 MW; F1E021B886BC4BEB CRC64;
MNPAHLLVLS AVCVSLLGAS SIPPQPLHLI QFGNMIQCTV PGFLSWIKYA DYGCYCGAGG
SGTPVDKLDR CCQVHDNCYT QAQKLPACSS IMDSPYVKIY SYDCSERTVT CKADNDECAA
FICNCDRVAA HCFAASPYNN NNYNIDTTTR C
