PA2BN_CROVV
ID PA2BN_CROVV Reviewed; 138 AA.
AC Q71QE8;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Basic phospholipase A2 Cvv-N6 {ECO:0000303|PubMed:12623078, ECO:0000303|PubMed:15032748};
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Cvv myotoxin {ECO:0000303|PubMed:9028014, ECO:0000303|PubMed:9920492};
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE Flags: Precursor;
OS Crotalus viridis viridis (Prairie rattlesnake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=8742;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-39, FUNCTION, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MASS SPECTROMETRY, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Venom, and Venom gland;
RX PubMed=15032748; DOI=10.1042/bj20040125;
RA Chen Y.-H., Wang Y.-M., Hseu M.-J., Tsai I.-H.;
RT "Molecular evolution and structure-function relationships of crotoxin-like
RT and asparagine-6-containing phospholipases A2 in pit viper venoms.";
RL Biochem. J. 381:25-34(2004).
RN [2]
RP PROTEIN SEQUENCE OF 17-49, FUNCTION, ACTIVITY REGULATION, SUBUNIT,
RP CRYSTALLIZATION, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=9028014; DOI=10.1016/s0041-0101(96)00054-2;
RA Ownby C.L., Colberg T.R., White S.P.;
RT "Isolation, characterization and crystallization of a phospholipase A2
RT myotoxin from the venom of the prairie rattlesnake (Crotalus viridis
RT viridis).";
RL Toxicon 35:111-124(1997).
RN [3]
RP PROTEIN SEQUENCE OF 17-39, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC STRAIN=Colorado, New Mexico, South Dakota, Southeastern Arizona, Texas,
RC Western Oklahoma, and Wyoming; TISSUE=Venom, and Venom gland;
RX PubMed=12623078; DOI=10.1016/s0003-9861(02)00747-6;
RA Tsai I.-H., Wang Y.-M., Chen Y.-H., Tu A.T.;
RT "Geographic variations, cloning, and functional analyses of the venom
RT acidic phospholipases A2 of Crotalus viridis viridis.";
RL Arch. Biochem. Biophys. 411:289-296(2003).
RN [4]
RP FUNCTION, SUBUNIT, AND ACTIVITY REGULATION.
RC TISSUE=Venom;
RX PubMed=9920492; DOI=10.1016/s0041-0101(98)00183-4;
RA Melo P.A., Ownby C.L.;
RT "Ability of wedelolactone, heparin, and para-bromophenacyl bromide to
RT antagonize the myotoxic effects of two crotaline venoms and their PLA2
RT myotoxins.";
RL Toxicon 37:199-215(1999).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that is myotoxic and
CC displays moderate edema-inducing activity in rat paws (PubMed:9028014,
CC PubMed:12623078). Does not show neurotoxic activity (PubMed:15032748,
CC PubMed:9028014). PLA2 catalyzes the calcium-dependent hydrolysis of the
CC 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:12623078,
CC ECO:0000269|PubMed:15032748, ECO:0000269|PubMed:9028014}.
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:0000269|PubMed:12623078, ECO:0000269|PubMed:15032748};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:12623078};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000269|PubMed:12623078};
CC -!- ACTIVITY REGULATION: Heparin and wedelolactone inhibit the myotoxic
CC activity (PubMed:9920492). The PLA2 inhibitor, para-bromophenacyl
CC bromide (BPB), inhibits enzymatic and myotoxic activities
CC (PubMed:9028014, PubMed:9920492). {ECO:0000269|PubMed:9028014,
CC ECO:0000269|PubMed:9920492}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=280 umol/min/mg enzyme with DPPC + deoxycholate as substrate (at
CC pH 7.4 and 37 degrees Celsius) {ECO:0000269|PubMed:15032748};
CC Vmax=88 umol/min/mg enzyme with DPPC + Triton X-100 as substrate (at
CC pH 7.4 and 37 degrees Celsius) {ECO:0000269|PubMed:15032748};
CC Note=When tested as a monomer.;
CC -!- SUBUNIT: Monomer (PubMed:15032748, PubMed:9028014). Binds to calmodulin
CC (PubMed:15032748). {ECO:0000269|PubMed:15032748,
CC ECO:0000269|PubMed:9028014}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: Mass=14200; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:12623078, ECO:0000269|PubMed:15032748};
CC -!- MISCELLANEOUS: Does not show neurotoxic activities (PubMed:15032748 and
CC PubMed:9028014).
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR EMBL; AF403138; AAQ13337.1; -; mRNA.
DR AlphaFoldDB; Q71QE8; -.
DR SMR; Q71QE8; -.
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; Secreted;
KW Signal; Toxin.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:12623078,
FT ECO:0000269|PubMed:15032748, ECO:0000269|PubMed:9028014"
FT CHAIN 17..138
FT /note="Basic phospholipase A2 Cvv-N6"
FT /id="PRO_0000418574"
FT ACT_SITE 63
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT ACT_SITE 105
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT DISULFID 42..131
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT DISULFID 44..60
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT DISULFID 59..111
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT DISULFID 65..138
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT DISULFID 66..104
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT DISULFID 73..97
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT DISULFID 91..102
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT CONFLICT 28
FT /note="M -> E (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 38
FT /note="T -> A (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="G -> W (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 138 AA; 16000 MW; 7B5E4097E66A5B7A CRC64;
MRTFWIVALL LVGVEGNLLQ FNKMIKMMTK KNAFPFYTSY GCYCGWGGRG RPKDATDRCC
FVHDCCYEKL TNCSPKTDIY SYSWKRGVII CGKGTPCEKQ ICECDRAAAV CFRENLPTYK
KRYMFYLDFL CTDPSEKC
