ID PA23_NOTSC STANDARD; PRT; 119 AA. AC P00609; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 15-JUN-2002 (Rel. 41, Last annotation update) DE Phospholipase A2 (EC 3.1.1.4) (Notechis II-5) (Phosphatidylcholine DE 2-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 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; 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 RT throw light on the anticoagulant and neurotoxic sites of RT 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. ACT 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 fatty acid anion. CC -!- COFACTOR: Binds 1 calcium ion per subunit. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- MISCELLANEOUS: 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; 16-JUN-97. DR InterPro; IPR001211; PhospholipaseA2. DR Pfam; PF00068; phoslip; 1. DR PRINTS; PR00389; PHPHLIPASEA2. DR ProDom; PD000303; PhospholipaseA2; 1. DR SMART; SM00085; PA2c; 1. DR PROSITE; PS00118; PA2_HIS; 1. DR PROSITE; PS00119; PA2_ASP; 1. KW Hydrolase; Lipid degradation; Calcium; Presynaptic neurotoxin; Venom; KW Multigene family; 3D-structure. FT ACT_SITE 48 48 FT ACT_SITE 93 93 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 CA_BIND 28 28 VIA CARBONYL OXYGEN. FT CA_BIND 30 30 VIA CARBONYL OXYGEN. FT CA_BIND 32 32 VIA CARBONYL OXYGEN. FT CA_BIND 49 49 SQ SEQUENCE 119 AA; 13676 MW; 032C9EEBF62BEE26 CRC64; NLVQFSYLIQ CANHGRRPTR HYMDYGCYCG WGGSGTPVDE LDRCCKIHDD CYSDAEKKGC SPKMSAYDYY CGENGPYCRN IKKKCLRFVC DCDVEAAFCF AKAPYNNANW NIDTKKRCQ //