PA2A2_BOTIN
ID PA2A2_BOTIN Reviewed; 107 AA.
AC P84397;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Acidic phospholipase A2 2;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=BinTX-II;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE Flags: Fragments;
OS Bothrops insularis (Golden lancehead) (Lachesis insularis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=8723;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MASS
RP SPECTROMETRY.
RC TISSUE=Venom {ECO:0000269|PubMed:17140721};
RX PubMed=17140721; DOI=10.1016/j.biochi.2006.10.006;
RA Cogo J.C., Lilla S., Souza G.H.M.F., Hyslop S., de Nucci G.;
RT "Purification, sequencing and structural analysis of two acidic
RT phospholipases A2 from the venom of Bothrops insularis (jararaca ilhoa).";
RL Biochimie 88:1947-1959(2006).
CC -!- FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC groups in 3-sn-phosphoglycerides. {ECO:0000250}.
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:0000250|UniProtKB:O42191, ECO:0000255|PROSITE-
CC ProRule:PRU10035, ECO:0000255|PROSITE-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 {ECO:0000269|PubMed:17140721}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:17140721}.
CC -!- MASS SPECTROMETRY: Mass=13788; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:17140721};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P84397; -.
DR SMR; P84397; -.
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 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 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..107
FT /note="Acidic phospholipase A2 2"
FT /id="PRO_0000161620"
FT ACT_SITE 41
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT ACT_SITE 76
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 42
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT DISULFID 26..100
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT DISULFID 28..38
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT DISULFID 37..82
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT DISULFID 43..107
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT DISULFID 44..75
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT DISULFID 62..73
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT DISULFID ?..68
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT UNSURE 2
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:17140721"
FT UNSURE 4
FT /note="Q or K"
FT /evidence="ECO:0000269|PubMed:17140721"
FT UNSURE 10
FT /note="Q or K"
FT /evidence="ECO:0000269|PubMed:17140721"
FT UNSURE 15
FT /note="Q or K"
FT /evidence="ECO:0000269|PubMed:17140721"
FT UNSURE 17
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:17140721"
FT UNSURE 22
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:17140721"
FT UNSURE 33
FT /note="I or L"
FT /evidence="ECO:0000269|PubMed:17140721"
FT UNSURE 48
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:17140721"
FT UNSURE 50
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:17140721"
FT UNSURE 60
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:17140721"
FT UNSURE 69
FT /note="Q or K"
FT /evidence="ECO:0000269|PubMed:17140721"
FT UNSURE 71
FT /note="Q or K"
FT /evidence="ECO:0000269|PubMed:17140721"
FT UNSURE 72
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:17140721"
FT UNSURE 81
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:17140721"
FT UNSURE 84
FT /note="Q or K"
FT /evidence="ECO:0000269|PubMed:17140721"
FT UNSURE 92
FT /note="Q or K"
FT /evidence="ECO:0000269|PubMed:17140721"
FT UNSURE 101
FT /note="Q or K"
FT /evidence="ECO:0000269|PubMed:17140721"
FT NON_CONS 36..37
FT /evidence="ECO:0000303|PubMed:17140721"
FT NON_CONS 47..48
FT /evidence="ECO:0000303|PubMed:17140721"
FT NON_CONS 93..94
FT /evidence="ECO:0000303|PubMed:17140721"
SQ SEQUENCE 107 AA; 12224 MW; 09AE1FEDC478964F CRC64;
NLWQFGRENQ EVMGQHLPFH YLSYGCYCGW GGIEPKCCYV HDCCYGKLDL YTYSKETGDL
VCGGDDPCQK QLCECDRVAA LCFQDNKDTY DQKPYNAENC QEASEAC
