PA2A2_BOTAS
ID PA2A2_BOTAS Reviewed; 124 AA.
AC P86389;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 28.
DE RecName: Full=Acidic phospholipase A2 2;
DE Short=BaspPLA2-II {ECO:0000303|PubMed:20026168};
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase {ECO:0000250|UniProtKB:P14418};
OS Bothrops asper (Terciopelo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=8722;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE OF 1-103 AND 109-124, NUCLEOTIDE SEQUENCE [MRNA] OF 3-124,
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP MASS SPECTROMETRY.
RC TISSUE=Venom {ECO:0000269|PubMed:20026168}, and
RC Venom gland {ECO:0000269|PubMed:20026168};
RX PubMed=20026168; DOI=10.1016/j.biochi.2009.12.006;
RA Fernandez J., Gutierrez J.M., Angulo Y., Sanz L., Juarez P., Calvete J.J.,
RA Lomonte B.;
RT "Isolation of an acidic phospholipase A(2) from the venom of the snake
RT Bothrops asper of Costa Rica: Biochemical and toxicological
RT characterization.";
RL Biochimie 92:273-283(2010).
CC -!- FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:20026168}.
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:20026168};
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 {ECO:0000269|PubMed:20026168}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:20026168}.
CC -!- MASS SPECTROMETRY: Mass=14212; Mass_error=6; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:20026168};
CC -!- MISCELLANEOUS: Does not have myotoxic, cytotoxic, anticoagulant,
CC hypotensive or anti-platelet aggregation activities. Is not lethal to
CC mice (PubMed:20026168). {ECO:0000305|PubMed:20026168}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P86389; -.
DR SMR; P86389; -.
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..124
FT /note="Acidic phospholipase A2 2"
FT /id="PRO_0000392466"
FT ACT_SITE 47
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT ACT_SITE 91
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14418"
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:P14418"
FT DISULFID 26..117
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT DISULFID 28..44
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT DISULFID 43..97
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT DISULFID 49..124
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT DISULFID 50..90
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT DISULFID 57..83
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT DISULFID 77..88
FT /evidence="ECO:0000250|UniProtKB:P14418"
SQ SEQUENCE 124 AA; 14194 MW; D6E4A704E94CEAA0 CRC64;
NLWQFGQMMS DVMRKNVVFK YLSYGCYCGW GGIGQPKDAT DRCCFVHDCC YGKVTGCDPK
MDIYTYTYSK ENGDVVCGGD DPCKKQICEC DRVAAICFRD NKDTYDSKYW FYGAKNCQED
SEPC
