PA2_LACMR
ID PA2_LACMR Reviewed; 60 AA.
AC B3EWP6;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 24.
DE RecName: Full=Phospholipase A2 {ECO:0000303|PubMed:26145564};
DE Short=Lmr-PLA2 {ECO:0000303|PubMed:26145564};
DE EC=3.1.1.4 {ECO:0000269|PubMed:26145564};
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase {ECO:0000250|UniProtKB:P20249};
DE Flags: Fragment;
OS Lachesis muta rhombeata (Bushmaster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Lachesis.
OX NCBI_TaxID=60219;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MASS SPECTROMETRY.
RC TISSUE=Venom {ECO:0000303|PubMed:26145564};
RX PubMed=26145564; DOI=10.2174/0929866522666150706112431;
RA Cordeiro F.A., Perini T.G., Bregge-Silva C., Cremonez C.M., Rodrigues R.S.,
RA Boldrini-Franca J., Bordon K., De Souza D.L., Ache D.C., de M Rodrigues V.,
RA Dos Santos W.F., Rosa J.C., Arantesa E.C.;
RT "A New Phospholipase A(2) from Lachesis muta rhombeata: Purification,
RT Biochemical and Comparative Characterization with Crotoxin B.";
RL Protein Pept. Lett. 22:816-827(2015).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that displays mild but
CC significant inhibition of mouse platelet aggregation induced by ADP and
CC collagen (PubMed:26145564). Induces edema in the foot pads and
CC gastrocnemius muscles of mice but shows no myonecrotic or myotoxic
CC activity (PubMed:26145564). PA2 catalyzes the calcium-dependent
CC hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides
CC (PubMed:26145564). {ECO:0000269|PubMed:26145564}.
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:26145564};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P20249};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P20249};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.404 mM for 4-nitro-3-(octanoyloxy) benzoic acid
CC {ECO:0000269|PubMed:26145564};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26145564}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:26145564}.
CC -!- MASS SPECTROMETRY: Mass=13975.18; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:26145564};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; B3EWP6; -.
DR SMR; B3EWP6; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004623; F:phospholipase A2 activity; IDA:UniProtKB.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR GO; GO:0044398; P:envenomation resulting in induction of edema in another organism; IDA:UniProtKB.
DR GO; GO:0044478; P:envenomation resulting in positive regulation of platelet aggregation in another organism; IDA:UniProtKB.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR Gene3D; 1.20.90.10; -; 1.
DR InterPro; IPR001211; PLipase_A2.
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; PS00118; PA2_HIS; 1.
PE 1: Evidence at protein level;
KW Calcium; Cytolysis; Direct protein sequencing; Disulfide bond; Hemolysis;
KW Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding; Secreted.
FT CHAIN 1..>60
FT /note="Phospholipase A2"
FT /id="PRO_0000419335"
FT ACT_SITE 47
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10035"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P20249"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P20249"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P20249"
FT DISULFID 28..44
FT /evidence="ECO:0000250|UniProtKB:P20249"
FT NON_TER 60
FT /evidence="ECO:0000303|PubMed:26145564"
SQ SEQUENCE 60 AA; 6740 MW; E0BFAA2AF664CCDC CRC64;
HLLQFGDLIN KIARRNGILY YSFYGCYCGL GGRGRPQDAT DRCCFVHDCC YGKVTGCDPK
