PA22_BOTHY
ID PA22_BOTHY Reviewed; 123 AA.
AC P0DUN1;
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=Basic myotoxic phospholipase A2 PhTX-II {ECO:0000303|PubMed:25365526};
DE Short=svPLA2;
DE EC=3.1.1.4 {ECO:0000269|PubMed:25365526};
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
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, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, ACTIVITY REGULATION, COFACTOR,
RP AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=25365526; DOI=10.3390/toxins6113077;
RA Huancahuire-Vega S., Ponce-Soto L.A., Marangoni S.;
RT "PhTX-II a basic myotoxic phospholipase A(2) from Porthidium hyoprora snake
RT venom, pharmacological characterization and amino acid sequence by mass
RT spectrometry.";
RL Toxins 6:3077-3097(2014).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that induces myotoxicity
CC and local edema in mice (PubMed:25365526). In addition, it causes
CC neuromuscular blockade in avian neuromuscular preparations with a
CC significant direct action on skeletal muscle function
CC (PubMed:25365526). Myotoxic action is exerted by both enzymatic and
CC non-enzymatic mechanisms (PubMed:25365526). PLA2 catalyzes the calcium-
CC dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides
CC (PubMed:25365526). {ECO:0000269|PubMed:25365526}.
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:25365526};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:25365526};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000250};
CC -!- ACTIVITY REGULATION: P-bromophenacyl bromide (BPB) completely inhibits
CC the catalytic and edematogenic activities (PubMed:25365526). Enzymatic
CC activity is also diminished by EDTA, heparin and crotapotins F2 and F3
CC from C.d.collilineatus (PubMed:25365526). Inhibited by divalent cations
CC different from calcium ions (cadmium, magnesium, manganese, zinc),
CC since they act as competitive antagonists of this cofactor
CC (PubMed:25365526). {ECO:0000269|PubMed:25365526}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=9.65 nmol/min/mg enzyme {ECO:0000269|PubMed:25365526};
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:25365526};
CC Temperature dependence:
CC Optimum temperature is 40-45 degrees Celsius.
CC {ECO:0000269|PubMed:25365526};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:25365526}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25365526}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:25365526}.
CC -!- MASS SPECTROMETRY: Mass=14149.08; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:25365526};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0DUN1; -.
DR SMR; P0DUN1; -.
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:InterPro.
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.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Metal-binding; Myotoxin; Secreted; Toxin.
FT CHAIN 1..123
FT /note="Basic myotoxic phospholipase A2 PhTX-II"
FT /evidence="ECO:0000269|PubMed:25365526"
FT /id="PRO_0000452840"
FT ACT_SITE 48
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:P62022"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P62022"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P62022"
FT BINDING 49
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P62022"
FT DISULFID 26..116
FT /evidence="ECO:0000250|UniProtKB:P62022"
FT DISULFID 28..45
FT /evidence="ECO:0000250|UniProtKB:P62022"
FT DISULFID 44..95
FT /evidence="ECO:0000250|UniProtKB:P62022"
FT DISULFID 50..123
FT /evidence="ECO:0000250|UniProtKB:P62022"
FT DISULFID 51..88
FT /evidence="ECO:0000250|UniProtKB:P62022"
FT DISULFID 58..81
FT /evidence="ECO:0000250|UniProtKB:P62022"
FT DISULFID 75..86
FT /evidence="ECO:0000250|UniProtKB:P62022"
SQ SEQUENCE 123 AA; 14159 MW; 9338BFB893C29D22 CRC64;
NLLQFNKMIL KETGKNAIPF YAFYGCYCGW GGRGKPKDKT DDRCCFVHDC CYGKLTGCPK
WDIYPYSLKS GYITCGKGTW CEEQICECDR AAAICFRENL DTYNKYGYMF YPDSRCKGPS
EQC
