PA2BA_CRODM
ID PA2BA_CRODM Reviewed; 122 AA.
AC P86806;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Basic phospholipase A2 10;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Cdc-10 {ECO:0000303|PubMed:19747981};
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase {ECO:0000250|UniProtKB:P84397};
OS Crotalus durissus cumanensis (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=184542;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RC TISSUE=Venom {ECO:0000269|PubMed:19747981};
RX PubMed=19747981; DOI=10.1016/j.cbpc.2009.08.011;
RA Romero-Vargas F.F., Ponce-Soto L.A., Martins-de-Souza D., Marangoni S.;
RT "Biological and biochemical characterization of two new PLA2 isoforms Cdc-9
RT and Cdc-10 from Crotalus durissus cumanensis snake venom.";
RL Comp. Biochem. Physiol. 151:66-74(2010).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that has a strong dose-
CC dependent anticoagulant effect. Intramuscular and intervenal injection
CC causes muscle necrosis. Induces moderate edema in the mouse foot pad.
CC PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in
CC 3-sn-phosphoglycerides. {ECO:0000269|PubMed:19747981}.
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, ECO:0000269|PubMed:19747981};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P59071};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000250|UniProtKB:P59071};
CC -!- ACTIVITY REGULATION: Inhibited by chemical modifications mediated by p-
CC BPB, anhydrous acetic acid and NBSF. {ECO:0000269|PubMed:19747981}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19747981}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:19747981}.
CC -!- MASS SPECTROMETRY: Mass=14228; Mass_error=3.5; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:19747981};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P86806; -.
DR SMR; P86806; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004623; F:phospholipase A2 activity; IDA:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR GO; GO:0044398; P:envenomation resulting in induction of edema in another organism; IDA:UniProtKB.
DR GO; GO:0044534; P:envenomation resulting in modulation of apoptotic process in another organism; IDA:UniProtKB.
DR GO; GO:0044521; P:envenomation resulting in muscle damage in another organism; IDA:UniProtKB.
DR GO; GO:0035899; P:negative regulation of blood coagulation in another organism; IDA:UniProtKB.
DR GO; GO:0009395; P:phospholipid catabolic process; IDA:UniProtKB.
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 Blood coagulation cascade inhibiting toxin; Calcium;
KW Direct protein sequencing; Disulfide bond; Hemostasis impairing toxin;
KW Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding; Myotoxin;
KW Secreted; Toxin.
FT CHAIN 1..122
FT /note="Basic phospholipase A2 10"
FT /id="PRO_0000401144"
FT ACT_SITE 46
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT ACT_SITE 88
FT /evidence="ECO:0000250|UniProtKB:P59071"
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 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 26..114
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 28..43
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 42..94
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 48..122
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 49..87
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 56..80
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 74..85
FT /evidence="ECO:0000250|UniProtKB:P59071"
SQ SEQUENCE 122 AA; 14229 MW; DB8B914BFC1CA46E CRC64;
SLLQFNKMIK FETRKSGVPF YAAYGCYCGW GGRRPKDPTD RCCFVHDCCY GKLTKCNTKW
DIYSYSLKSG YITCGKGTWC KEQICECDRV AAECLRRSLN TYKNEYMFYP DSRCRGPPEY
TC
