PA2A_BOTER
ID PA2A_BOTER Reviewed; 138 AA.
AC Q2HZ28;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Acidic phospholipase A2 BE-I-PLA2;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE Flags: Precursor;
OS Bothrops erythromelas (Caatinga lance head).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=44710;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-37; 78-91; 99-109 AND
RP 122-131, FUNCTION, AND MASS SPECTROMETRY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=16750518; DOI=10.1016/j.bcp.2006.04.032;
RA de Albuquerque Modesto J.C., Spencer P.J., Fritzen M., Valenca R.C.,
RA Oliva M.L., da Silva M.B., Chudzinski-Tavassi A.M., Guarnieri M.C.;
RT "BE-I-PLA2, a novel acidic phospholipase A2 from Bothrops erythromelas
RT venom: isolation, cloning and characterization as potent anti-platelet and
RT inductor of prostaglandin I2 release by endothelial cells.";
RL Biochem. Pharmacol. 72:377-384(2006).
CC -!- FUNCTION: Snake venom phospholipase A2 that shows a potent inhibition
CC of human platelet aggregation. This inhibition is concentration-
CC dependent when aggregation is induced by collagen, and concentration-
CC independent when aggregation is induced by arachidonic acid. In human
CC umbilical-cord vein endothelial cells, this toxin stimulates
CC endothelial cells to release prostaglandin I(2), suggesting an increase
CC of its potential anti-platelet activity in vivo. PLA2 catalyzes the
CC calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-
CC phosphoglycerides. {ECO:0000269|PubMed:16750518}.
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 -!- MASS SPECTROMETRY: Mass=13649.57; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16750518};
CC -!- MISCELLANEOUS: Does not inhibit platelet aggregation when aggregation
CC is induced by ADP, and does not induce aggregation of washed platelets.
CC Does not induce changes on the principal platelet receptors (ITGA2,
CC ITGA2B, GPIBA, SELP). In human umbilical-cord vein endothelial cells,
CC does not induce detachment, does not interfere on nitric oxide release,
CC and is neither apoptotic nor proliferative (PubMed:16750518).
CC {ECO:0000305|PubMed:16750518}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR EMBL; DQ359953; ABC96692.1; -; mRNA.
DR AlphaFoldDB; Q2HZ28; -.
DR SMR; Q2HZ28; -.
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;
KW Hemostasis impairing toxin; Hydrolase; Lipid degradation; Lipid metabolism;
KW Metal-binding; Platelet aggregation inhibiting toxin; Secreted; Signal;
KW Toxin.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:16750518"
FT CHAIN 17..138
FT /note="Acidic phospholipase A2 BE-I-PLA2"
FT /id="PRO_5000141191"
FT ACT_SITE 63
FT /evidence="ECO:0000250|UniProtKB:P06859"
FT ACT_SITE 105
FT /evidence="ECO:0000250|UniProtKB:P06859"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 42..131
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 44..60
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 59..111
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 65..138
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 66..104
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 73..97
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 91..102
FT /evidence="ECO:0000250|UniProtKB:O42191"
SQ SEQUENCE 138 AA; 15435 MW; 760A7A10AE6943C8 CRC64;
MRTLWIMAVL LVGVEGSLVQ FETLIMKIAG RSGVWYYGSY GCYCGSGGQG RPQDASDRCC
FVHDCCYGKV TDCDPKADVY TYSEENGVVV CGGDDPCKKQ ICECDRVAAT CFRDNKDTYD
NKYWFFPAKN CQEESEPC
