PA2BG_CRODU
ID PA2BG_CRODU Reviewed; 121 AA.
AC P0CAS7;
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 F17;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=CdtF17;
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, COFACTOR, ACTIVITY REGULATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Venom;
RX PubMed=12018617; DOI=10.1023/a:1015320616206;
RA Oliveira D.G., Toyama M.H., Novello J.C., Beriam L.O.S., Marangoni S.;
RT "Structural and functional characterization of basic PLA2 isolated from
RT Crotalus durissus terrificus venom.";
RL J. Protein Chem. 21:161-168(2002).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that has anticoagulant
CC activity and inhibits bactericial growth of the Gram-negative bacteria
CC Xanthomonas axonopodis pv. passiflorae (in monomeric form). PLA2
CC catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-
CC sn-phosphoglycerides. {ECO:0000269|PubMed:12018617}.
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;
CC Evidence={ECO:0000269|PubMed:12018617};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000269|PubMed:12018617};
CC -!- ACTIVITY REGULATION: Activated by heparin. Inhibited by its chaperone
CC crotapotin. {ECO:0000269|PubMed:12018617}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=31.2 mM for 4-nitro-3-(octanoyloxy)benzoic acid
CC {ECO:0000269|PubMed:12018617};
CC Vmax=8.2 nmol/min/mg enzyme {ECO:0000269|PubMed:12018617};
CC pH dependence:
CC Optimum pH is 7.9. {ECO:0000269|PubMed:12018617};
CC Temperature dependence:
CC Optimum temperature is 10-30 degrees Celsius.
CC {ECO:0000269|PubMed:12018617};
CC -!- SUBUNIT: When this protein is associated with crotapotin (F5 or F7), it
CC forms the crotoxin protein.
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; P0CAS7; -.
DR SMR; P0CAS7; -.
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:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
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 Antibiotic; Antimicrobial; Blood coagulation cascade inhibiting toxin;
KW Calcium; Direct protein sequencing; Disulfide bond;
KW Hemostasis impairing toxin; Hydrolase; Lipid degradation; Lipid metabolism;
KW Metal-binding; Secreted; Toxin.
FT CHAIN 1..121
FT /note="Basic phospholipase A2 F17"
FT /id="PRO_0000376924"
FT ACT_SITE 46
FT /evidence="ECO:0000250"
FT ACT_SITE 88
FT /evidence="ECO:0000250"
FT BINDING 26
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 28
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 30
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 25..114
FT /evidence="ECO:0000250"
FT DISULFID 27..43
FT /evidence="ECO:0000250"
FT DISULFID 42..94
FT /evidence="ECO:0000250"
FT DISULFID 48..121
FT /evidence="ECO:0000250"
FT DISULFID 49..87
FT /evidence="ECO:0000250"
FT DISULFID 56..80
FT /evidence="ECO:0000250"
FT DISULFID 74..85
FT /evidence="ECO:0000250"
SQ SEQUENCE 121 AA; 14368 MW; E06F8697975E036D CRC64;
HLLQFNKMLK FETRKNAVPF YAFGCYCGWG GQRRPKDATD RCCFVHDCCY EKVTKCNTKW
DFYRYSLKSG YITCGKGTWC KEQICECDRV AAECLRRSLS TYKNEYMFYP DSRCREPSET
C
