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 14-DEC-2022, entry version 121. 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 snake). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera; OC Serpentes; Colubroidea; Elapidae; Acanthophiinae; Notechis. OX NCBI_TaxID=70142; RN [1] RP PROTEIN SEQUENCE. RC TISSUE=Venom; RX PubMed=1002692; DOI=10.1016/s0021-9258(17)32855-7; RA Halpert J., Eaker D.; RT "Isolation and amino acid sequence of a neurotoxic phospholipase A from the RT venom of the Australian tiger snake Notechis scutatus 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 the CC nerve termini. Notechis II-5 is less toxic than notexin but has a CC higher specific phospholipase activity. PLA2 catalyzes the calcium- CC dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn- CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE- CC 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 subfamily. CC 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 AlphaFoldDB; P00609; -. 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: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; PHOSPHOLIPASE A2 FAMILY MEMBER; 1. DR Pfam; PF00068; Phospholip_A2_1; 1. DR PRINTS; PR00389; PHPHLIPASEA2. DR SMART; SM00085; PA2c; 1. DR SUPFAM; SSF48619; Phospholipase A2, PLA2; 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; Neurotoxin; KW Presynaptic neurotoxin; Secreted; Toxin. FT CHAIN 1..119 FT /note="Basic phospholipase A2 notechis II-5" FT /id="PRO_0000161676" FT ACT_SITE 48 FT /evidence="ECO:0000250|UniProtKB:P00608" FT ACT_SITE 93 FT /evidence="ECO:0000250|UniProtKB:P00608" FT BINDING 28 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P60043" FT BINDING 30 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P60043" FT BINDING 32 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P60043" FT BINDING 49 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P60043" FT DISULFID 11..71 FT /evidence="ECO:0000269|PubMed:9604284, FT ECO:0007744|PDB:2NOT" FT DISULFID 27..118 FT /evidence="ECO:0000269|PubMed:9604284, FT ECO:0007744|PDB:2NOT" FT DISULFID 29..45 FT /evidence="ECO:0000269|PubMed:9604284, FT ECO:0007744|PDB:2NOT" FT DISULFID 44..99 FT /evidence="ECO:0000269|PubMed:9604284, FT ECO:0007744|PDB:2NOT" FT DISULFID 51..92 FT /evidence="ECO:0000269|PubMed:9604284, FT ECO:0007744|PDB:2NOT" FT DISULFID 60..85 FT /evidence="ECO:0000269|PubMed:9604284, FT ECO:0007744|PDB:2NOT" FT DISULFID 78..90 FT /evidence="ECO:0000269|PubMed:9604284, FT ECO:0007744|PDB:2NOT" FT HELIX 2..13 FT /evidence="ECO:0007829|PDB:2NOT" FT HELIX 19..22 FT /evidence="ECO:0007829|PDB:2NOT" FT TURN 26..30 FT /evidence="ECO:0007829|PDB:2NOT" FT HELIX 40..57 FT /evidence="ECO:0007829|PDB:2NOT" FT TURN 62..64 FT /evidence="ECO:0007829|PDB:2NOT" FT STRAND 69..72 FT /evidence="ECO:0007829|PDB:2NOT" FT STRAND 75..78 FT /evidence="ECO:0007829|PDB:2NOT" FT STRAND 81..83 FT /evidence="ECO:0007829|PDB:2NOT" FT HELIX 84..102 FT /evidence="ECO:0007829|PDB:2NOT" FT HELIX 107..109 FT /evidence="ECO:0007829|PDB:2NOT" FT HELIX 114..117 FT /evidence="ECO:0007829|PDB:2NOT" SQ SEQUENCE 119 AA; 13676 MW; 032C9EEBF62BEE26 CRC64; NLVQFSYLIQ CANHGRRPTR HYMDYGCYCG WGGSGTPVDE LDRCCKIHDD CYSDAEKKGC SPKMSAYDYY CGENGPYCRN IKKKCLRFVC DCDVEAAFCF AKAPYNNANW NIDTKKRCQ //