PA2A_BOTAM
ID PA2A_BOTAM Reviewed; 122 AA.
AC P86907;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 03-SEP-2014, sequence version 1.
DT 03-AUG-2022, entry version 19.
DE RecName: Full=Acidic phospholipase A2 {ECO:0000303|PubMed:22975267, ECO:0000305|PubMed:22975267};
DE Short=svPLA2 {ECO:0000250|UniProtKB:P20249};
DE EC=3.1.1.4 {ECO:0000269|PubMed:22975267};
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase {ECO:0000250|UniProtKB:P20249};
OS Bothrops ammodytoides (Yararanata) (Patagonian lancehead).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=169857;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION,
RP DISULFIDE BONDS, MASS SPECTROMETRY, AND TOXIC DOSE.
RC TISSUE=Venom {ECO:0000269|PubMed:22975267};
RX PubMed=22975267; DOI=10.1016/j.toxicon.2012.08.019;
RA Clement H., Costa de Oliveira V., Zamudio F.Z., Lago N.R.,
RA Valdez-Cruz N.A., Bernard Valle M., Hajos S.E., Alagon A., Possani L.D.,
RA de Roodt A.R.;
RT "Isolation, amino acid sequence and biological characterization of an
RT 'aspartic-49' phospholipase A(2) from Bothrops (Rhinocerophis) ammodytoides
RT venom.";
RL Toxicon 60:1314-1323(2012).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that displays low
CC systemic toxicity and causes severe symptoms only at very high
CC concentrations (15 mg/kg). Has neither coagulant nor anticoagulant
CC activity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:22975267}.
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:22975267};
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22975267}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:22975267}.
CC -!- PTM: Contains 7 disulfide bonds. {ECO:0000269|PubMed:22975267}.
CC -!- MASS SPECTROMETRY: Mass=13853.65; Method=Unknown;
CC Evidence={ECO:0000269|PubMed:22975267};
CC -!- TOXIC DOSE: LD(50) is 292.5 ug/kg by intravenous injection into mice.
CC {ECO:0000269|PubMed:22975267}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000255}.
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DR AlphaFoldDB; P86907; -.
DR SMR; P86907; -.
DR PRIDE; P86907; -.
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; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0006644; P:phospholipid metabolic process; IDA:UniProtKB.
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; Toxin.
FT CHAIN 1..122
FT /note="Acidic phospholipase A2"
FT /id="PRO_0000430167"
FT ACT_SITE 47
FT /evidence="ECO:0000250|UniProtKB:P06859"
FT ACT_SITE 89
FT /evidence="ECO:0000250|UniProtKB:P06859"
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:P20249"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P20249"
FT DISULFID 26..115
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 28..44
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 43..95
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 49..122
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 50..88
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 57..81
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 75..86
FT /evidence="ECO:0000250|UniProtKB:O42191"
SQ SEQUENCE 122 AA; 13868 MW; 121F76761E39A59F CRC64;
HLMQFETLIK KIAGRSGVWF YGFYGCYCGS GGRGKPKDAT DRCCFVHDCC YGKVTGCDPK
MDFYTYSEEN GVVVCGGDDP CKKQICECDR VAATCFRDNK TYDNNKYWFY PAKNCQEESE
PC
