PA2B2_LACMU
ID PA2B2_LACMU Reviewed; 122 AA.
AC P0C943;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Basic phospholipase A2 LmTX-II;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
OS Lachesis muta muta (Bushmaster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Lachesis.
OX NCBI_TaxID=8753;
RN [1]
RP PROTEIN SEQUENCE, MASS SPECTROMETRY, AND SUBUNIT.
RC TISSUE=Venom;
RX PubMed=16005152; DOI=10.1016/j.bbagen.2005.05.022;
RA Damico D.C.S., Lilla S., de Nucci G., Ponce-Soto L.A., Winck F.V.,
RA Novello J.C., Marangoni S.;
RT "Biochemical and enzymatic characterization of two basic Asp49
RT phospholipase A2 isoforms from Lachesis muta muta (Surucucu) venom.";
RL Biochim. Biophys. Acta 1726:75-86(2005).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that may display
CC neurotoxic and myotoxic activities. May induce inflammatory edema by
CC mechanisms involving mast cell activation and arachidonic acid
CC metabolites. May increase plasma creatine kinase activity. PLA2
CC catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-
CC 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 -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: Mass=14186.2; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:16005152};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR Allergome; 6323; Lac mu 1.
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 Calcium; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Lipid degradation; Lipid metabolism; Metal-binding; Myotoxin; Neurotoxin;
KW Presynaptic neurotoxin; Secreted; Toxin.
FT CHAIN 1..122
FT /note="Basic phospholipase A2 LmTX-II"
FT /id="PRO_0000371714"
FT ACT_SITE 47
FT /evidence="ECO:0000250"
FT ACT_SITE 89
FT /evidence="ECO:0000250"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 26..115
FT /evidence="ECO:0000250"
FT DISULFID 28..44
FT /evidence="ECO:0000250"
FT DISULFID 43..95
FT /evidence="ECO:0000250"
FT DISULFID 49..122
FT /evidence="ECO:0000250"
FT DISULFID 50..88
FT /evidence="ECO:0000250"
FT DISULFID 75..86
FT /evidence="ECO:0000250"
FT UNSURE 2
FT /note="L or I"
FT UNSURE 3
FT /note="L or I"
FT UNSURE 4
FT /note="K or Q"
FT UNSURE 9
FT /note="I or L"
FT UNSURE 18
FT /note="I or L"
FT UNSURE 63
FT /note="L or I"
FT UNSURE 73
FT /note="L or I"
FT UNSURE 84
FT /note="Q or K"
FT UNSURE 85
FT /note="I or L"
FT UNSURE 96
FT /note="L or I"
FT UNSURE 100
FT /note="L or I"
SQ SEQUENCE 122 AA; 14230 MW; 0B4CEB0BC527B0D9 CRC64;
HLLKFNKMIK FETRKNAIPF YAFYGCYCGW GGRXXXXXXX XXCCFVHDCC YGKXXXXXXX
WDLYPYXXXS GYLTCGKGTW CEEQICECDR VAAECLRRSL STYKYGYMFY PDSRCRGPSE
TC
