PA2B5_NOTSC
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 03-AUG-2022, entry version 119.
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}.
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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 PRIDE; 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; 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; 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
