PA21_BOTHY
ID PA21_BOTHY Reviewed; 123 AA.
AC P0DUN2;
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 phospholipase A2 Ph-TX1 {ECO:0000303|PubMed:21496495};
DE Short=svPLA2;
DE EC=3.1.1.4 {ECO:0000269|PubMed:21496495};
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, MASS SPECTROMETRY, SUBUNIT,
RP SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Venom;
RX PubMed=21496495; DOI=10.1016/j.cbpc.2011.03.013;
RA Huancahuire-Vega S., Ponce-Soto L.A., Martins-de-Souza D., Marangoni S.;
RT "Biochemical and pharmacological characterization of PhTX-I a new myotoxic
RT phospholipase A2 isolated from Porthidium hyoprora snake venom.";
RL Comp. Biochem. Physiol. 154:108-119(2011).
RN [2]
RP FUNCTION OF CHEMICALLY MODIFIED DERIVATIVES.
RC TISSUE=Venom;
RX PubMed=23484072; DOI=10.1155/2013/103494;
RA Huancahuire-Vega S., Correa D.H., Hollanda L.M., Lancellotti M.,
RA Ramos C.H., Ponce-Soto L.A., Marangoni S.;
RT "Chemical modifications of PhTX-I myotoxin from Porthidium hyoprora snake
RT venom: effects on structural, enzymatic, and pharmacological properties.";
RL Biomed. Res. Int. 2013:103494-103494(2013).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that induces in vivo
CC myotoxicity, moderates footpad edema, and causes in vitro neuromuscular
CC blockade. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:21496495}.
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:21496495};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:21496495};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000250|UniProtKB:P14418};
CC -!- ACTIVITY REGULATION: Inhibited by divalent cations different from
CC calcium ions (cadmium, magnesium, manganese, zinc), since they act as
CC competitive antagonists of this cofactor.
CC {ECO:0000269|PubMed:21496495}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.96 mM for 4-nitro-3-(octanoyloxy) benzoic acid (NOBA)
CC {ECO:0000269|PubMed:21496495};
CC Vmax=11.76 nmol/min/mg enzyme {ECO:0000269|PubMed:21496495};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:21496495};
CC Temperature dependence:
CC Optimum temperature is 35-45 degrees Celsius.
CC {ECO:0000269|PubMed:21496495};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:21496495}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21496495}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:21496495}.
CC -!- MASS SPECTROMETRY: Mass=14249.22; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:21496495};
CC -!- MISCELLANEOUS: Lys and Tyr residues play critical role in myotoxic,
CC neurotoxic, and cytotoxic activities displayed by this toxin. In an
CC other hand, His residues are relevant for edematogenic, neurotoxic, and
CC myotoxic effects, but not for cytotoxic activity.
CC {ECO:0000269|PubMed:23484072}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; P0DUN2; -.
DR SMR; P0DUN2; -.
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 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 Lipid degradation; Lipid metabolism; Metal-binding; Myotoxin; Secreted;
KW Toxin.
FT CHAIN 1..123
FT /note="Basic phospholipase A2 Ph-TX1"
FT /evidence="ECO:0000269|PubMed:21496495"
FT /id="PRO_0000452841"
FT ACT_SITE 48
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT ACT_SITE 90
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT BINDING 49
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 28..45
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 44..96
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 50..123
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 51..89
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 59..83
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 77..87
FT /evidence="ECO:0000250|UniProtKB:P59071"
SQ SEQUENCE 123 AA; 14278 MW; 19C931FD3231F59E CRC64;
DLWEFGKMIL KETGKNPFPY YGAYGCYCGW GGRGKPKDKT DDRCCFVHDC CRYKKLTGCP
KTNDRYSYSW KDLTIVCGED DPCKELCECD KAAAVCFREN LGTYNKKYRY HLRSLCKKAD
KPC
