PA2A1_BOTBZ
ID PA2A1_BOTBZ Reviewed; 107 AA.
AC P0DUN3;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 02-JUN-2021, sequence version 1.
DT 03-AUG-2022, entry version 4.
DE RecName: Full=Acidic phospholipase A2 braziliase-I {ECO:0000303|PubMed:28951306};
DE Short=svPLA2;
DE EC=3.1.1.4 {ECO:0000269|PubMed:28951306};
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE Flags: Fragments;
OS Bothrops brazili (Brazil's lancehead).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=157546;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT,
RP SUBCELLULAR LOCATION, MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP 3D-STRUCTURE MODELING.
RC TISSUE=Venom;
RX PubMed=28951306; DOI=10.1016/j.ijbiomac.2017.09.069;
RA Sobrinho J.C., Kayano A.M., Simoes-Silva R., Alfonso J.J., Gomez A.F.,
RA Gomez M.C.V., Zanchi F.B., Moura L.A., Souza V.R., Fuly A.L.,
RA de Oliveira E., da Silva S.L., Almeida J.R., Zuliani J.P., Soares A.M.;
RT "Anti-platelet aggregation activity of two novel acidic Asp49-
RT phospholipases A2 from Bothrops brazili snake venom.";
RL Int. J. Biol. Macromol. 107:1014-1022(2018).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that induces significant
CC edematogenic activity. Shows mild cytotoxicity on Trypanosoma cruzi and
CC Leishmania infantum. Also inhibits ADP- and collagen-induced platelet
CC aggregation. Does not show myotoxic activity.
CC {ECO:0000269|PubMed:28951306}.
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:0000269|PubMed:28951306};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:28951306};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.5-8.5. {ECO:0000269|PubMed:28951306};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:28951306}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28951306}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:28951306}.
CC -!- MASS SPECTROMETRY: Mass=13894; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:28951306};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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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.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond;
KW Hemostasis impairing toxin; Hydrolase; Lipid degradation; Lipid metabolism;
KW Metal-binding; Platelet aggregation inhibiting toxin; Secreted; Toxin.
FT CHAIN 1..107
FT /note="Acidic phospholipase A2 braziliase-I"
FT /evidence="ECO:0000269|PubMed:28951306"
FT /id="PRO_0000452894"
FT ACT_SITE 47
FT /evidence="ECO:0000250|UniProtKB:P06859"
FT ACT_SITE 80
FT /evidence="ECO:0000250|UniProtKB:P06859"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 26..100
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 28..44
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 43..86
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 49..107
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 50..79
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 57..72
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 66..77
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT NON_CONS 61..62
FT /evidence="ECO:0000305|PubMed:28951306"
FT NON_CONS 89..90
FT /evidence="ECO:0000305|PubMed:28951306"
SQ SEQUENCE 107 AA; 12108 MW; 3E7FE7ECBD6A14A2 CRC64;
NLWQFEMLIM KIALTSGFMF YSSYGCYCGW GGHGRPKDAS DRCCFVHDCC YGKVTTCNPK
FGVVVCGGDD PCKKQICECD RVAATCFRDN KYWFYGAKXC QEESDPC
