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 18-SEP-2019, entry version 112. 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: CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1- CC acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); CC Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; CC EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, CC ECO:0000255|PROSITE-ProRule:PRU10036}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000250|UniProtKB:P60043}; CC Note=Binds 1 Ca(2+) ion. {ECO:0000250|UniProtKB:P60043}; 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 SMR; P00609; -. DR EvolutionaryTrace; P00609; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC. DR GO; GO:0102567; F:phospholipase A2 activity (consuming 1,2-dipalmitoylphosphatidylcholine); IEA:UniProtKB-EC. DR GO; GO:0102568; F:phospholipase A2 activity consuming 1,2-dioleoylphosphatidylethanolamine); IEA:UniProtKB-EC. DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW. DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro. DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW. DR GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro. DR CDD; cd00125; PLA2c; 1. DR Gene3D; 1.20.90.10; -; 1. DR InterPro; IPR001211; PLipase_A2. DR InterPro; IPR033112; PLipase_A2_Asp_AS. DR InterPro; IPR016090; PLipase_A2_dom. DR InterPro; IPR036444; PLipase_A2_dom_sf. DR InterPro; IPR033113; PLipase_A2_His_AS. 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 {ECO:0000250|UniProtKB:P00608}. FT ACT_SITE 93 93 {ECO:0000250|UniProtKB:P00608}. FT METAL 28 28 Calcium; via carbonyl oxygen. FT {ECO:0000250|UniProtKB:P60043}. FT METAL 30 30 Calcium; via carbonyl oxygen. FT {ECO:0000250|UniProtKB:P60043}. FT METAL 32 32 Calcium; via carbonyl oxygen. FT {ECO:0000250|UniProtKB:P60043}. FT METAL 49 49 Calcium. {ECO:0000250|UniProtKB:P60043}. FT DISULFID 11 71 {ECO:0000244|PDB:2NOT, FT ECO:0000269|PubMed:9604284}. FT DISULFID 27 118 {ECO:0000244|PDB:2NOT, FT ECO:0000269|PubMed:9604284}. FT DISULFID 29 45 {ECO:0000244|PDB:2NOT, FT ECO:0000269|PubMed:9604284}. FT DISULFID 44 99 {ECO:0000244|PDB:2NOT, FT ECO:0000269|PubMed:9604284}. FT DISULFID 51 92 {ECO:0000244|PDB:2NOT, FT ECO:0000269|PubMed:9604284}. FT DISULFID 60 85 {ECO:0000244|PDB:2NOT, FT ECO:0000269|PubMed:9604284}. FT DISULFID 78 90 {ECO:0000244|PDB:2NOT, FT ECO:0000269|PubMed:9604284}. 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 //