ID PA23_NOTSC Reviewed; 119 AA. AC P00609; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 15-JAN-2008, entry version 62. DE Phospholipase A2 (EC 3.1.1.4) (Notechis II-5) (Phosphatidylcholine 2- DE acylhydrolase). OS Notechis scutatus scutatus (Mainland tiger snake) (Common tiger OS snake). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea; OC Elapidae; Acanthophiinae; Notechis. OX NCBI_TaxID=70142; RN [1] RP PROTEIN SEQUENCE. RC TISSUE=Venom; RX MEDLINE=77071450; PubMed=1002692; RA Halpert J., Eaker D.; RT "Isolation and amino acid sequence of a neurotoxic phospholipase A RT from the venom of the Australian tiger snake Notechis scutatus RT scutatus."; RL J. Biol. Chem. 251:7343-7347(1976). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). RC TISSUE=Venom; RX MEDLINE=98267643; PubMed=9604284; DOI=10.1016/S0041-0101(97)00051-2; RA Carredano E., Westerlund B., Persson B., Saarinen M., Ramaswamy S., RA Eaker D., Eklund H.; RT "The three-dimensional structures of two toxins from snake venom throw RT light on the anticoagulant and neurotoxic sites of phospholipase A2."; RL Toxicon 36:75-92(1998). CC -!- FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2- CC acyl groups in 3-sn-phosphoglycerides. Inhibits neuromuscular CC transmission by blocking acetylcholine release from the nerve CC termini. Acts presynaptically. Notechis II-5 is less toxic than CC Notexin but has a higher specific phospholipase activity. CC -!- CATALYTIC ACTIVITY: Phosphatidylcholine + H(2)O = 1- CC acylglycerophosphocholine + a carboxylate. CC -!- COFACTOR: Binds 1 calcium ion per subunit. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TOXIC DOSE: LD(50) is 0.045 mg/kg by intravenous injection. CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I CC subfamily. 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 PIR; A00750; PSNOA5. DR PDB; 2NOT; X-ray; 3.00 A; A/B=1-119. DR PDBsum; 2NOT; -. DR LinkHub; P00609; -. DR InterPro; IPR013090; Phospholip_A2_AS. DR InterPro; IPR001211; Phospholipase_A2. DR Gene3D; G3DSA:1.20.90.10; Phospholipase_A2; 1. DR PANTHER; PTHR11716; Phospholipase_A2; 1. DR Pfam; PF00068; Phospholip_A2_1; 1. DR PRINTS; PR00389; PHPHLIPASEA2. DR ProDom; PD000303; PhospholipaseA2; 1. DR SMART; SM00085; PA2c; 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; Hydrolase; KW Lipid degradation; Metal-binding; Neurotoxin; Presynaptic neurotoxin; KW Secreted; Toxin. FT CHAIN 1 119 Phospholipase A2. FT /FTId=PRO_0000161676. FT ACT_SITE 48 48 FT ACT_SITE 93 93 FT METAL 28 28 Calcium (via carbonyl oxygen). FT METAL 30 30 Calcium (via carbonyl oxygen). FT METAL 32 32 Calcium (via carbonyl oxygen). FT METAL 49 49 Calcium. FT DISULFID 11 71 FT DISULFID 27 118 FT DISULFID 29 45 FT DISULFID 44 99 FT DISULFID 51 92 FT DISULFID 60 85 FT DISULFID 78 90 FT HELIX 2 13 FT HELIX 19 22 FT TURN 26 30 FT HELIX 40 57 FT TURN 62 64 FT STRAND 69 72 FT STRAND 75 78 FT STRAND 81 83 FT HELIX 84 102 FT HELIX 107 109 FT HELIX 114 117 SQ SEQUENCE 119 AA; 13676 MW; 032C9EEBF62BEE26 CRC64; NLVQFSYLIQ CANHGRRPTR HYMDYGCYCG WGGSGTPVDE LDRCCKIHDD CYSDAEKKGC SPKMSAYDYY CGENGPYCRN IKKKCLRFVC DCDVEAAFCF AKAPYNNANW NIDTKKRCQ //