ID PA2A2_OPHHA Reviewed; 146 AA. AC Q9DF33; DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 02-SEP-2026, entry version 112. DE RecName: Full=Acidic phospholipase A2 2; DE Short=svPLA2; DE EC=3.1.1.4; DE AltName: Full=APLA2-2; 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 IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Venom; RX PubMed=24297900; DOI=10.1073/pnas.1314702110; RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J., RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J., RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A., RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C., RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M., RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P., RA Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.; RT "The king cobra genome reveals dynamic gene evolution and adaptation in the RT snake venom system."; RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 28-146 IN COMPLEX WITH CALCIUM RP ION, COFACTOR, AND DISULFIDE BONDS. RX PubMed=12925787; DOI=10.1107/s0907444903014598; RA Xu S., Gu L., Wang Q., Shu Y., Song S., Lin Z.; RT "Structure of a king cobra phospholipase A2 determined from a hemihedrally RT twinned crystal."; RL Acta Crystallogr. D 59:1574-1581(2003). CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that displays edema- CC inducing and moderate anticoagulant activities. PLA2 catalyzes the CC calcium-dependent hydrolysis of the 2-acyl groups in 3-sn- CC phosphoglycerides. 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:12925787}; CC Note=Binds 1 Ca(2+) ion. {ECO:0000305|PubMed:12925787}; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily. CC D49 sub-subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF302907; AAG23963.1; -; mRNA. DR PDB; 1M8T; X-ray; 2.10 A; A/B/C/D/E/F=28-146. DR AlphaFoldDB; Q9DF33; -. DR SMR; Q9DF33; -. DR TopDownProteomics; Q9DF33; -. DR EvolutionaryTrace; Q9DF33; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0004623; F:A2-type glycerophospholipase activity; IEA:UniProtKB-EC. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0005543; F:phospholipid binding; IEA:TreeGrafter. DR GO; GO:0005102; F:signaling receptor binding; IEA:TreeGrafter. DR GO; GO:0050482; P:arachidonate secretion; IEA:InterPro. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:TreeGrafter. DR GO; GO:0016042; P:lipid catabolic process; IEA:InterPro. DR GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro. DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:TreeGrafter. DR CDD; cd00125; PLA2c; 1. DR FunFam; 1.20.90.10:FF:000007; Acidic phospholipase A2; 1. DR Gene3D; 1.20.90.10; Phospholipase A2 domain; 1. DR InterPro; IPR001211; PLA2. DR InterPro; IPR016090; PLA2-like_dom. DR InterPro; IPR033112; PLA2_Asp_AS. DR InterPro; IPR033113; PLA2_histidine. DR InterPro; IPR036444; PLipase_A2_dom_sf. DR PANTHER; PTHR11716:SF94; PHOSPHOLIPASE A2; 1. DR PANTHER; PTHR11716; PHOSPHOLIPASE A2 FAMILY MEMBER; 1. DR Pfam; PF00068; Phospholip_A2_1; 1. DR PRINTS; PR00389; PHPHLIPASEA2. DR SMART; SM00085; PA2c; 1. DR SUPFAM; SSF48619; Phospholipase A2, PLA2; 1. DR PROSITE; PS00119; PA2_ASP; 1. DR PROSITE; PS00118; PA2_HIS; 1. DR PDBsum; 1M8T; -. PE 1: Evidence at protein level; KW 3D-structure; Blood coagulation cascade inhibiting toxin; Calcium; KW Disulfide bond; Hemostasis impairing toxin; Hydrolase; Lipid degradation; KW Lipid metabolism; Metal-binding; Secreted; Signal; Toxin. FT SIGNAL 1..21 FT /evidence="ECO:0000255" FT PROPEP 22..27 FT /evidence="ECO:0000255" FT /id="PRO_0000022944" FT CHAIN 28..146 FT /note="Acidic phospholipase A2 2" FT /id="PRO_0000022945" FT ACT_SITE 75 FT /evidence="ECO:0000250|UniProtKB:P14418" FT ACT_SITE 121 FT /evidence="ECO:0000250|UniProtKB:P14418" FT BINDING 55 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:12925787, FT ECO:0007744|PDB:1M8T" FT BINDING 57 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:12925787, FT ECO:0007744|PDB:1M8T" FT BINDING 59 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:12925787, FT ECO:0007744|PDB:1M8T" FT BINDING 76 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:12925787, FT ECO:0007744|PDB:1M8T" FT DISULFID 38..99 FT /evidence="ECO:0000269|PubMed:12925787, FT ECO:0007744|PDB:1M8T" FT DISULFID 54..146 FT /evidence="ECO:0000269|PubMed:12925787, FT ECO:0007744|PDB:1M8T" FT DISULFID 56..72 FT /evidence="ECO:0000269|PubMed:12925787, FT ECO:0007744|PDB:1M8T" FT DISULFID 71..127 FT /evidence="ECO:0000269|PubMed:12925787, FT ECO:0007744|PDB:1M8T" FT DISULFID 78..120 FT /evidence="ECO:0000269|PubMed:12925787, FT ECO:0007744|PDB:1M8T" FT DISULFID 88..113 FT /evidence="ECO:0000269|PubMed:12925787, FT ECO:0007744|PDB:1M8T" FT DISULFID 106..118 FT /evidence="ECO:0000269|PubMed:12925787, FT ECO:0007744|PDB:1M8T" FT HELIX 29..39 FT /evidence="ECO:0007829|PDB:1M8T" FT HELIX 45..48 FT /evidence="ECO:0007829|PDB:1M8T" FT STRAND 49..52 FT /evidence="ECO:0007829|PDB:1M8T" FT TURN 53..55 FT /evidence="ECO:0007829|PDB:1M8T" FT STRAND 56..59 FT /evidence="ECO:0007829|PDB:1M8T" FT HELIX 67..81 FT /evidence="ECO:0007829|PDB:1M8T" FT TURN 90..92 FT /evidence="ECO:0007829|PDB:1M8T" FT STRAND 97..99 FT /evidence="ECO:0007829|PDB:1M8T" FT STRAND 104..106 FT /evidence="ECO:0007829|PDB:1M8T" FT HELIX 112..130 FT /evidence="ECO:0007829|PDB:1M8T" FT HELIX 135..137 FT /evidence="ECO:0007829|PDB:1M8T" FT HELIX 142..145 FT /evidence="ECO:0007829|PDB:1M8T" SQ SEQUENCE 146 AA; 15901 MW; 354F45F6B67690A7 CRC64; MNPAHLLVLS AVCVSLLGAS SIPPQPLHLV QFNGMIRCTI PGSIPWWDYS DYGCYCGSGG SGTPVDELDR CCQVHDNCYT QAQQLTECSP YSKRYSYDCS EGTLTCKADN DECAAFVCDC DRVAAICFAG APYNKENINI DTTTRC //