PA2BC_CRODR
ID PA2BC_CRODR Reviewed; 122 AA.
AC P0CAS3;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Basic phospholipase A2 Cdr-12;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
OS Crotalus durissus ruruima (South American rattlesnake) (Mt. Roraima
OS rattlesnake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=221570;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=17203396; DOI=10.1007/s10930-006-9042-3;
RA Ponce-Soto L.A., Baldasso P.A., Romero-Vargas F.F., Winck F.V.,
RA Novello J.C., Marangoni S.;
RT "Biochemical, pharmacological and structural characterization of two PLA2
RT isoforms Cdr-12 and Cdr-13 from Crotalus durissus ruruima snake venom.";
RL Protein J. 26:39-49(2007).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that induces myonecrosis
CC and edema upon intramuscular injections in mice. In vitro, causes a
CC potent blockade of neuromuscular transmission in young chicken biventer
CC cervicis preparation and produces cytotoxicity in murine C2C12 skeletal
CC muscle myotubes and lack cytolytic activity upon myoblasts in vitro.
CC PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in
CC 3-sn-phosphoglycerides. {ECO:0000269|PubMed:17203396}.
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 -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: Mass=14333.49; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:17203396};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0CAS3; -.
DR SMR; P0CAS3; -.
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; Myotoxin; Neurotoxin;
KW Secreted; Toxin.
FT CHAIN 1..122
FT /note="Basic phospholipase A2 Cdr-12"
FT /id="PRO_0000376920"
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; 14334 MW; 6908533F02C03AE4 CRC64;
SLLQFNKMIK FETRKNAIPF YAFYGCYCGW GGQGRPKDAT DRCCIVHDCC YGKLAKCNTK
WDFYRYSLRS GYFQCGKGTW CEQQICECDR VAAECLRRSL STYRYGYMIY PDSRCREPSE
TC
