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 01-NOV-1997 (REL. 35, 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; VERTEBRATA; TETRAPODA; REPTILIA; OC LEPIDOSAURIA; SERPENTES. RN [1] RP SEQUENCE. RC TISSUE=VENOM; RX MEDLINE; 77071450. RA HALPERT J., EAKER D.; RL J. BIOL. CHEM. 251:7343-7347(1976). CC -!- FUNCTION: PA2 CATALYZES THE CALCIUM-DEPENDENT HYDROLYSIS OF THE CC 2-ACYL GROUPS IN 3-SN-PHOSPHOGLYCERIDES. CC -!- FUNCTION: INHIBITS NEUROMUSCULAR TRANSMISSION BY BLOCKING CC ACETYLCHOLINE RELEASE FROM THE NERVE TERMINI. ACT PRESYNAPTICALLY. CC -!- CATALYTIC ACTIVITY: PHOSPHATIDYLCHOLINE + H(2)O = 1-ACYLGLYCERYL- CC PHOSPHOCHOLINE + A FATTY ACID ANION. CC -!- LD(50) IS 0.045 MG/KG BY INTRAVENOUS INJECTION. CC -!- NOTECHIS II-5 IS LESS TOXIC THAN NOTEXIN BUT HAS A HIGHER SPECIFIC CC PHOSPHOLIPASE ACTIVITY. 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 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 49 49 SQ SEQUENCE 119 AA; 13676 MW; 4A627591 CRC32; NLVQFSYLIQ CANHGRRPTR HYMDYGCYCG WGGSGTPVDE LDRCCKIHDD CYSDAEKKGC SPKMSAYDYY CGENGPYCRN IKKKCLRFVC DCDVEAAFCF AKAPYNNANW NIDTKKRCQ //