PA2BB_PSEAU
ID PA2BB_PSEAU Reviewed; 118 AA.
AC P04056;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1986, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Basic phospholipase A2 PA-11;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
OS Pseudechis australis (Mulga snake) (King brown snake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Acanthophiinae; Pseudechis.
OX NCBI_TaxID=8670;
RN [1]
RP PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=3887651; DOI=10.1016/0041-0101(85)90112-6;
RA Nishida S., Terashima M., Tamiya N.;
RT "Amino acid sequences of phospholipases A2 from the venom of an Australian
RT elapid snake (king brown snake, Pseudechis australis).";
RL Toxicon 23:87-104(1985).
CC -!- FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC 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; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3887651}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:3887651}.
CC -!- TOXIC DOSE: LD(50) is 0.24 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; A00747; PSSNK1.
DR PDB; 3V9M; X-ray; 1.56 A; A/B=1-118.
DR PDBsum; 3V9M; -.
DR AlphaFoldDB; P04056; -.
DR SMR; P04056; -.
DR BRENDA; 3.1.1.4; 7400.
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: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; Secreted.
FT CHAIN 1..118
FT /note="Basic phospholipase A2 PA-11"
FT /id="PRO_0000161686"
FT ACT_SITE 48
FT /evidence="ECO:0000250"
FT ACT_SITE 92
FT /evidence="ECO:0000250"
FT BINDING 28
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007744|PDB:3V9M"
FT BINDING 30
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007744|PDB:3V9M"
FT BINDING 32
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007744|PDB:3V9M"
FT BINDING 49
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007744|PDB:3V9M"
FT DISULFID 11..71
FT /evidence="ECO:0007744|PDB:3V9M"
FT DISULFID 27..117
FT /evidence="ECO:0007744|PDB:3V9M"
FT DISULFID 29..45
FT /evidence="ECO:0007744|PDB:3V9M"
FT DISULFID 44..98
FT /evidence="ECO:0007744|PDB:3V9M"
FT DISULFID 51..91
FT /evidence="ECO:0007744|PDB:3V9M"
FT DISULFID 60..84
FT /evidence="ECO:0007744|PDB:3V9M"
FT DISULFID 78..89
FT /evidence="ECO:0007744|PDB:3V9M"
FT HELIX 2..12
FT /evidence="ECO:0007829|PDB:3V9M"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:3V9M"
FT HELIX 19..22
FT /evidence="ECO:0007829|PDB:3V9M"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:3V9M"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:3V9M"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:3V9M"
FT HELIX 40..57
FT /evidence="ECO:0007829|PDB:3V9M"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:3V9M"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:3V9M"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:3V9M"
FT HELIX 83..101
FT /evidence="ECO:0007829|PDB:3V9M"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:3V9M"
FT HELIX 113..116
FT /evidence="ECO:0007829|PDB:3V9M"
SQ SEQUENCE 118 AA; 12966 MW; F7C90529BB12D5A1 CRC64;
NLIQFGNMIQ CANKGSRPSL DYADYGCYCG WGGSGTPVDE LDRCCQVHDN CYEQAGKKGC
FPKLTLYSWK CTGNVPTCNS KPGCKSFVCA CDAAAAKCFA KAPYKKENYN IDTKKRCK
