PA2BA_CRODR
ID PA2BA_CRODR Reviewed; 122 AA.
AC P86169;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Basic phospholipase A2 A;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Crotoxin basic chain 1 {ECO:0000303|PubMed:19013478};
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase {ECO:0000303|PubMed:19013478};
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] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND MASS SPECTROMETRY.
RC TISSUE=Venom {ECO:0000269|PubMed:19013478};
RX PubMed=19013478; DOI=10.1016/j.toxicon.2008.10.021;
RA Diz Filho E.B.S., Marangoni S., Toyama D.O., Fagundes F.H.R.,
RA Oliveira S.C.B., Fonseca F.V., Calgarotto A.K., Joazeiro P.P., Toyama M.H.;
RT "Enzymatic and structural characterization of new PLA2 isoform isolated
RT from white venom of Crotalus durissus ruruima.";
RL Toxicon 53:104-114(2009).
CC -!- FUNCTION: Snake venom phospholipase A that has strong antimicrobial
CC activity against the Gram-negative bacterium X.axonopodis.
CC Antimicrobial activity is not abolished by EDTA or p-BPB and is
CC therefore not strongly dependent on the enzymatic activity. PLA2
CC catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-
CC sn-phosphoglycerides. {ECO:0000269|PubMed:19013478}.
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:19013478};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:19013478};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000269|PubMed:19013478};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.3 mM for NOBA {ECO:0000269|PubMed:19013478};
CC Vmax=377 nmol/min/mg enzyme for NOBA {ECO:0000269|PubMed:19013478};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:19013478};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:19013478};
CC -!- SUBUNIT: This toxin consists of 2 subunits: acidic and basic. The
CC acidic subunit is non-toxic, without enzymatic activity and comprises 3
CC peptides that are cross-linked by 7 disulfide bridges. The basic
CC subunit is toxic, has phospholipase A2 activity and is composed of a
CC single chain. {ECO:0000269|PubMed:19013478}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19013478}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:19013478}.
CC -!- MASS SPECTROMETRY: Mass=14299.34; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:19013478};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P86169; -.
DR SMR; P86169; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; IDA:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
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; Calcium; Direct protein sequencing;
KW Disulfide bond; Hydrolase; Lipid degradation; Lipid metabolism;
KW Metal-binding; Neurotoxin; Presynaptic neurotoxin; Secreted; Toxin.
FT CHAIN 1..122
FT /note="Basic phospholipase A2 A"
FT /id="PRO_0000363990"
FT ACT_SITE 47
FT /evidence="ECO:0000250|UniProtKB:P14421"
FT ACT_SITE 89
FT /evidence="ECO:0000250|UniProtKB:P14421"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14421"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14421"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14421"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14421"
FT DISULFID 26..115
FT /evidence="ECO:0000250|UniProtKB:P14421"
FT DISULFID 28..44
FT /evidence="ECO:0000250|UniProtKB:P14421"
FT DISULFID 43..95
FT /evidence="ECO:0000250|UniProtKB:P14421"
FT DISULFID 49..122
FT /evidence="ECO:0000250|UniProtKB:P14421"
FT DISULFID 50..88
FT /evidence="ECO:0000250|UniProtKB:P14421"
FT DISULFID 57..81
FT /evidence="ECO:0000250|UniProtKB:P14421"
FT DISULFID 75..86
FT /evidence="ECO:0000250|UniProtKB:P14421"
SQ SEQUENCE 122 AA; 14199 MW; CC5CFF491931C79A CRC64;
HLLQFNKMIK FETRKNAIPF YAFYGCYCGW GGRGRPKDAT DRCCFVHDCC YGKLAKCNTK
WDIYPYSLKS GYITCGKGTW CEEQICECDR VAAECLRRSL STYKYGYMFY PDSRCRGPSE
TC
