PA23_BOTHY
ID PA23_BOTHY Reviewed; 106 AA.
AC P0DUN0;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 02-JUN-2021, sequence version 1.
DT 03-AUG-2022, entry version 5.
DE RecName: Full=Acidic phospholipase A2 PhTX-III {ECO:0000303|PubMed:29124136};
DE Short=svPLA2;
DE EC=3.1.1.4 {ECO:0000269|PubMed:29124136};
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE Flags: Fragments;
OS Bothrocophias hyoprora (Amazonian hognose viper) (Porthidium hyoprora).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrocophias.
OX NCBI_TaxID=230469;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, MASS SPECTROMETRY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=29124136; DOI=10.1016/j.bbrep.2015.03.001;
RA Marques P.P., Esteves A., Lancellotti M., Ponce-Soto L.A., Marangoni S.;
RT "Novel acidic phospholipase A2 from Porthidium hyoprora causes inflammation
RT with mast cell rich infiltrate.";
RL Biochem. Biophys. Rep. 1:78-84(2015).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that induces inflammatory
CC response, with local edema and release of cytokines IL-1 alpha, IL-6
CC and TNF-alpha (PubMed:29124136). Does not exhibit myotoxic,
CC anticoagulant and antibacterial effects (PubMed:29124136). Release of
CC pro-inflammatory cytokines may be due to mast cell degranulation, and
CC edema may be induced by arachidonic acid that results from the PLA2
CC catalytic activity (PubMed:29124136). PLA2 catalyzes the calcium-
CC dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides
CC (PubMed:29124136). {ECO:0000269|PubMed:29124136}.
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:29124136};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:29124136};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Partially inhibited by magnesium ions and
CC completely inhibited by zinc ions These divalent cations may act as
CC competitive antagonists of the cofactor. {ECO:0000269|PubMed:29124136}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.43 mM for 4-nitro-3-(octanoyloxy) benzoic acid (NOBA)
CC {ECO:0000269|PubMed:29124136};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:29124136};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:29124136};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29124136}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:29124136}.
CC -!- MASS SPECTROMETRY: Mass=13620.9; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:29124136};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0DUN0; -.
DR SMR; P0DUN0; -.
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:InterPro.
DR GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR CDD; cd00125; PLA2c; 1.
DR Gene3D; 1.20.90.10; -; 2.
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; 2.
DR Pfam; PF00068; Phospholip_A2_1; 1.
DR PRINTS; PR00389; PHPHLIPASEA2.
DR SMART; SM00085; PA2c; 1.
DR SUPFAM; SSF48619; SSF48619; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Metal-binding; Secreted.
FT CHAIN 1..106
FT /note="Acidic phospholipase A2 PhTX-III"
FT /evidence="ECO:0000269|PubMed:29124136"
FT /id="PRO_0000452839"
FT ACT_SITE 43
FT /evidence="ECO:0000250|UniProtKB:P06859"
FT ACT_SITE 69
FT /evidence="ECO:0000250|UniProtKB:P06859"
FT BINDING 23
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT BINDING 25
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT BINDING 44
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 24..40
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 39..75
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 45..106
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 46..68
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 55..66
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT NON_CONS 11..12
FT /evidence="ECO:0000305|PubMed:29124136"
FT NON_CONS 49..50
FT /evidence="ECO:0000305|PubMed:29124136"
SQ SEQUENCE 106 AA; 12085 MW; 7234B5749B3B288F CRC64;
DLMQFETLIM KSGVWYYGSY GCYCGSGGQF RPQDASDRCC FVHDCCYGKN GDIVCGGDDP
CKKQICECDR VAATCFRDNK VTYDNKYWFF PAKFPPQNCK EESEPC
