PA2BF_CRODU
ID PA2BF_CRODU Reviewed; 122 AA.
AC P0CAS6;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Basic phospholipase A2 F16;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=CdtF16;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
OS Crotalus durissus terrificus (South American rattlesnake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=8732;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC TISSUE=Venom;
RX PubMed=16283546; DOI=10.1007/s10930-005-6718-z;
RA Hernandez-Oliveira S., Toyama M.H., Toyama D.O., Marangoni S., Hyslop S.,
RA Rodrigues-Simioni L.;
RT "Biochemical, pharmacological and structural characterization of a new PLA2
RT from Crotalus durissus terrificus (South American rattlesnake) venom.";
RL Protein J. 24:233-242(2005).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that produces
CC neuromuscular blockade in chick biventer cervicis preparations in the
CC absence and presence of crotapotin. In contrast, in mouse phrenic
CC nerve-diaphragm preparations, the neuromuscular blockade is dependent
CC on crotapotin. PLA2 catalyzes the calcium-dependent hydrolysis of the
CC 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:16283546}.
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};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Pre-incubation with heparin markedly reduces the
CC neurotoxicity of this toxin. {ECO:0000269|PubMed:16283546}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.9. {ECO:0000269|PubMed:16283546};
CC Temperature dependence:
CC Optimum temperature is 25 degrees Celsius.
CC {ECO:0000269|PubMed:16283546};
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0CAS6; -.
DR SMR; P0CAS6; -.
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.
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; Neurotoxin; Secreted;
KW Toxin.
FT CHAIN 1..122
FT /note="Basic phospholipase A2 F16"
FT /id="PRO_0000376923"
FT ACT_SITE 47
FT /evidence="ECO:0000250|UniProtKB:P62022"
FT ACT_SITE 89
FT /evidence="ECO:0000250|UniProtKB:P62022"
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 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P62022"
FT DISULFID 26..115
FT /evidence="ECO:0000250|UniProtKB:P62022"
FT DISULFID 28..44
FT /evidence="ECO:0000250|UniProtKB:P62022"
FT DISULFID 43..95
FT /evidence="ECO:0000250|UniProtKB:P62022"
FT DISULFID 49..122
FT /evidence="ECO:0000250|UniProtKB:P62022"
FT DISULFID 50..88
FT /evidence="ECO:0000250|UniProtKB:P62022"
FT DISULFID 57..81
FT /evidence="ECO:0000250|UniProtKB:P62022"
FT DISULFID 75..86
FT /evidence="ECO:0000250|UniProtKB:P62022"
SQ SEQUENCE 122 AA; 14332 MW; 49A0BA3B85284C08 CRC64;
SLLQFNKMIK FETRKNAVPF YAFYGCYCGW GGRRRPKDAT DRCCFVHDCC YEKVTKCNTK
WDIYRYSLKS GYITCGKGTW CKEQICECDR VAAECLRRSL STYKNGYMFY PDSRCRGPSE
TC
