PA2_BOTLA
ID PA2_BOTLA Reviewed; 122 AA.
AC C0HJC1;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 1.
DT 03-AUG-2022, entry version 19.
DE RecName: Full=Acidic phospholipase A2 BlatPLA2;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
OS Bothriechis lateralis (Side-striped palm pitviper).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothriechis.
OX NCBI_TaxID=44727;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=23872034; DOI=10.1016/j.toxicon.2013.07.008;
RA Van der Laat M., Fernandez J., Durban J., Villalobos E., Camacho E.,
RA Calvete J.J., Lomonte B.;
RT "Amino acid sequence and biological characterization of BlatPLA(2), a non-
RT toxic acidic phospholipase A(2) from the venom of the arboreal snake
RT Bothriechis lateralis from Costa Rica.";
RL Toxicon 73:71-80(2013).
CC -!- FUNCTION: Acidic phospholipase A2 (PLA2) that only causes a mild edema,
CC when subcutaneously injected in the mice foot. PLA2 catalyzes the
CC calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-
CC phosphoglycerides. {ECO:0000269|PubMed:23872034}.
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, ECO:0000269|PubMed:23872034};
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:0000269|PubMed:23872034}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23872034}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:23872034}.
CC -!- MASS SPECTROMETRY: Mass=13916.7; Mass_error=0.4; Method=MALDI;
CC Note=Average mass, the difference between the calculated and the
CC experimental values corresponds to a potassium adduct.;
CC Evidence={ECO:0000269|PubMed:23872034};
CC -!- MISCELLANEOUS: Is not myotoxic or lethal. Lacks anti-coagulant,
CC platelet aggregating or anti-aggregating activities (PubMed:23872034).
CC {ECO:0000305|PubMed:23872034}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR AlphaFoldDB; C0HJC1; -.
DR SMR; C0HJC1; -.
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: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; Secreted.
FT CHAIN 1..122
FT /note="Acidic phospholipase A2 BlatPLA2"
FT /id="PRO_0000429743"
FT ACT_SITE 47
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT ACT_SITE 89
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT DISULFID 26..115
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT DISULFID 28..44
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT DISULFID 43..95
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT DISULFID 49..122
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT DISULFID 50..88
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT DISULFID 57..81
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT DISULFID 75..86
FT /evidence="ECO:0000250|UniProtKB:O42187"
SQ SEQUENCE 122 AA; 13891 MW; 59CA9D141806AEE1 CRC64;
SLLQFREMIT KMTGKEPIFF YAFYGCYCGL GGRGKPQDAT DRCCFVHDCC YGKVTGCDPK
KDIYTYSEEN GAFVCGGDDP CKKEICECDK NAAICFRNDL DTYDYKYLLY SPENCQEESE
PC
