ID PA2B5_NOTSC Reviewed; 119 AA. AC P00609; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 22-JUL-2015, entry version 95. DE RecName: Full=Basic phospholipase A2 notechis II-5; DE Short=svPLA2; DE EC=3.1.1.4; DE AltName: Full=Phosphatidylcholine 2-acylhydrolase; OS Notechis scutatus scutatus (Mainland tiger snake) (Common tiger OS snake). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; OC Toxicofera; Serpentes; Colubroidea; Elapidae; Acanthophiinae; OC Notechis. OX NCBI_TaxID=70142; RN [1] RP PROTEIN SEQUENCE. RC TISSUE=Venom; RX 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 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: Snake venom phospholipase A2 (PLA2) that inhibits CC neuromuscular transmission by blocking acetylcholine release from CC the nerve termini. Notechis II-5 is less toxic than notexin but CC has a higher specific phospholipase activity. PLA2 catalyzes the CC calcium-dependent hydrolysis of the 2-acyl groups in 3-sn- CC phosphoglycerides. CC -!- CATALYTIC ACTIVITY: Phosphatidylcholine + H(2)O = 1- CC acylglycerophosphocholine + a carboxylate. {ECO:0000255|PROSITE- CC ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036}. CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Note=Binds 1 Ca(2+) ion.; CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. 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. 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 PIR; A00750; PSNOA5. DR PDB; 2NOT; X-ray; 3.00 A; A/B=1-119. DR PDBsum; 2NOT; -. DR ProteinModelPortal; P00609; -. DR SMR; P00609; 1-119. DR HOVERGEN; HBG008137; -. DR EvolutionaryTrace; P00609; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0072556; C:other organism presynaptic membrane; IEA:UniProtKB-KW. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC. DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW. DR GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro. DR Gene3D; 1.20.90.10; -; 1. DR InterPro; IPR001211; PLipase_A2. DR InterPro; IPR013090; PLipase_A2_AS. DR InterPro; IPR016090; PLipase_A2_dom. DR PANTHER; PTHR11716; PTHR11716; 1. DR Pfam; PF00068; Phospholip_A2_1; 1. DR PRINTS; PR00389; PHPHLIPASEA2. DR SMART; SM00085; PA2c; 1. DR SUPFAM; SSF48619; SSF48619; 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; Disulfide bond; KW Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding; KW Neurotoxin; Presynaptic neurotoxin; Secreted; Toxin. FT CHAIN 1 119 Basic phospholipase A2 notechis II-5. 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 {ECO:0000244|PDB:2NOT}. FT HELIX 19 22 {ECO:0000244|PDB:2NOT}. FT TURN 26 30 {ECO:0000244|PDB:2NOT}. FT HELIX 40 57 {ECO:0000244|PDB:2NOT}. FT TURN 62 64 {ECO:0000244|PDB:2NOT}. FT STRAND 69 72 {ECO:0000244|PDB:2NOT}. FT STRAND 75 78 {ECO:0000244|PDB:2NOT}. FT STRAND 81 83 {ECO:0000244|PDB:2NOT}. FT HELIX 84 102 {ECO:0000244|PDB:2NOT}. FT HELIX 107 109 {ECO:0000244|PDB:2NOT}. FT HELIX 114 117 {ECO:0000244|PDB:2NOT}. SQ SEQUENCE 119 AA; 13676 MW; 032C9EEBF62BEE26 CRC64; NLVQFSYLIQ CANHGRRPTR HYMDYGCYCG WGGSGTPVDE LDRCCKIHDD CYSDAEKKGC SPKMSAYDYY CGENGPYCRN IKKKCLRFVC DCDVEAAFCF AKAPYNNANW NIDTKKRCQ //