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-JAN-1990 (REL. 13, LAST ANNOTATION UPDATE) DE PHOSPHOLIPASE A2 (EC 3.1.1.4) (NOTECHIS 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; RC MEDLINE=77071450; RA HALPERT J., EAKER D.; RL J. BIOL. CHEM. 251:7343-7347(1976). CC -!- FUNCTION: PA2 CATALYZE THE CALCIUM-DEPENDENT HYDROLYSIS OF THE CC 2-ACYL GROUPS IN 3-SN-PHOSPHOGLYCERIDES. CC -!- CATALYTIC ACTIVITY: PHOSPHATIDYLCHOLINE + H(2)O = 1-ACYLGLYCERYL- CC PHOSPHOCHOLINE + A FATTY ACID ANION. CC -!- NOTECHIS 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 PROSITE; PS00118; PA2_HIS. DR PROSITE; PS00119; PA2_ASP. KW HYDROLASE; LIPID DEGRADATION; CALCIUM; PRESYNAPTIC NEUROTOXIN. FT ACT_SITE 48 48 BY SIMILARITY. FT ACT_SITE 93 93 BY SIMILARITY. SQ SEQUENCE 119 AA; 13676 MW; 63242 CN; NLVQFSYLIQ CANHGRRPTR HYMDYGCYCG WGGSGTPVDE LDRCCKIHDD CYSDAEKKGC SPKMSAYDYY CGENGPYCRN IKKKCLRFVC DCDVEAAFCF AKAPYNNANW NIDTKKRCQ //