PA2B1_LACMU
ID PA2B1_LACMU Reviewed; 122 AA.
AC P0C942;
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-I;
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, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, 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).
RN [2]
RP FUNCTION.
RC TISSUE=Venom;
RX PubMed=16626776; DOI=10.1016/j.toxicon.2006.02.007;
RA Damico D.C.S., Bueno L.G.F., Rodrigues-Simioni L., Marangoni S.,
RA da Cruz-Hofling M.A., Novello J.C.;
RT "Functional characterization of a basic D49 phospholipase A2 (LmTX-I) from
RT the venom of the snake Lachesis muta muta (bushmaster).";
RL Toxicon 47:759-765(2006).
RN [3]
RP FUNCTION.
RC TISSUE=Venom;
RX PubMed=17208264; DOI=10.1016/j.toxicon.2006.11.014;
RA Damico D.C.S., Nascimento J.M., Lomonte B., Ponce-Soto L.A., Joazeiro P.P.,
RA Novello J.C., Marangoni S., Collares-Buzato C.B.;
RT "Cytotoxicity of Lachesis muta muta snake (bushmaster) venom and its
RT purified basic phospholipase A2 (LmTX-I) in cultured cells.";
RL Toxicon 49:678-692(2007).
RN [4]
RP FUNCTION.
RC TISSUE=Venom;
RX PubMed=18766430; DOI=10.1007/s10930-008-9148-x;
RA Damico D.C.S., da Cruz-Hofling M.A., Cintra M., Leonardo M.B.,
RA Calgarotto A.K., da Silva S.L., Marangoni S.;
RT "Pharmacological study of edema and myonecrosis in mice induced by venom of
RT the bushmaster snake (Lachesis muta muta) and its basic Asp49 phospholipase
RT A(2) (LmTX-I).";
RL Protein J. 27:384-391(2008).
RN [5]
RP FUNCTION.
RC TISSUE=Venom;
RX PubMed=18996140; DOI=10.1016/j.toxicon.2008.10.016;
RA Ferreira T., Camargo E.A., Ribela M.T.C.P., Damico D.C.S., Marangoni S.,
RA Antunes E., De Nucci G., Landucci E.C.T.;
RT "Inflammatory oedema induced by Lachesis muta muta (Surucucu) venom and
RT LmTX-I in the rat paw and dorsal skin.";
RL Toxicon 53:69-77(2009).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that displays neurotoxic
CC and myotoxic activities. Induces inflammatory edema by mechanisms
CC involving mast cell activation and arachidonic acid metabolites.
CC Increases plasma creatine kinase activity. PLA2 catalyzes the calcium-
CC dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
CC {ECO:0000269|PubMed:16626776, ECO:0000269|PubMed:17208264,
CC ECO:0000269|PubMed:18766430, ECO:0000269|PubMed:18996140}.
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:0000269|PubMed:16005152};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000269|PubMed:16005152};
CC -!- ACTIVITY REGULATION: Inhibited by Mn(2+), Mg(2+), Zn(2+) and Cu(2+).
CC {ECO:0000269|PubMed:16005152}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:16005152};
CC Temperature dependence:
CC Optimum temperature is 35-45 degrees Celsius.
CC {ECO:0000269|PubMed:16005152};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16005152}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: Mass=14245.5; 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 Secreted; Toxin.
FT CHAIN 1..122
FT /note="Basic phospholipase A2 LmTX-I"
FT /id="PRO_0000371713"
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 68
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; 14284 MW; A349F600C73B8D78 CRC64;
HLLKFNKMIK FETRKNAIPF YAFYGCYCGW GGRXXXXXXX XXCCFVHDCC YGKXXXXXXX
WDLYRYSLKS GYLTCGKGTW CEEQICECDR VAAECLRRSL STYKYGYMFY PDSRCRGPSE
TC
