PA2B2_NOTSC
ID PA2B2_NOTSC Reviewed; 145 AA.
AC P08873;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Basic phospholipase A2 notechis 11'2;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE Flags: Precursor;
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 NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=3174443; DOI=10.1093/nar/16.18.9049;
RA Ducancel F., Guignery Frelat G., Menez A., Boulain J.-C., Bouchier C.;
RT "Complete amino acid sequence of a PLA2 from the tiger snake Notechis
RT scutatus scutatus as deduced from a complementary DNA.";
RL Nucleic Acids Res. 16:9049-9049(1988).
RN [2]
RP PROTEIN SEQUENCE OF 28-145.
RC TISSUE=Venom;
RX PubMed=1761049; DOI=10.1111/j.1432-1033.1991.tb16399.x;
RA Bouchier C., Boyot P., Tesson F., Tremeau O., Bouet F., Hodgson D.,
RA Boulain J.-C., Menez A.;
RT "Notechis 11'2, a non-toxic phospholipase A2 from the venom of Notechis
RT scutatus scutatus.";
RL Eur. J. Biochem. 202:493-500(1991).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that has no lethal
CC activity. 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.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR EMBL; X12605; CAA31125.1; -; mRNA.
DR PIR; S01390; S01390.
DR AlphaFoldDB; P08873; -.
DR SMR; P08873; -.
DR PRIDE; P08873; -.
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 Calcium; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Lipid degradation; Lipid metabolism; Metal-binding; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..27
FT /evidence="ECO:0000269|PubMed:1761049"
FT /id="PRO_0000022938"
FT CHAIN 28..145
FT /note="Basic phospholipase A2 notechis 11'2"
FT /id="PRO_0000022939"
FT ACT_SITE 75
FT /evidence="ECO:0000250"
FT ACT_SITE 119
FT /evidence="ECO:0000250"
FT BINDING 55
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 57
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 38..98
FT /evidence="ECO:0000250"
FT DISULFID 54..144
FT /evidence="ECO:0000250"
FT DISULFID 56..72
FT /evidence="ECO:0000250"
FT DISULFID 71..125
FT /evidence="ECO:0000250"
FT DISULFID 78..118
FT /evidence="ECO:0000250"
FT DISULFID 87..111
FT /evidence="ECO:0000250"
FT DISULFID 105..116
FT /evidence="ECO:0000250"
SQ SEQUENCE 145 AA; 15903 MW; 3F508029C6E0F001 CRC64;
MYPAHLLVLL TVCVSLLEAS SIPARPLNLY QFGNMIQCAN HGRRPTLAYA DYGCYCGAGG
SGTPVDELDR CCKAHDDCYG EAGKKGCYPT LTLYSWQCIE KTPTCNSKTG CERSVCDCDA
TAAKCFAKAP YNKKNYNIDT EKRCQ
