PA2AD_CROOA
ID PA2AD_CROOA Reviewed; 138 AA.
AC Q7ZTA7;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Acidic phospholipase A2 CoaPLA2 {ECO:0000303|PubMed:24707493};
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Cvv-E6d {ECO:0000303|PubMed:12623078};
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE AltName: Full=Phospholipase A2 CoaTx-I {ECO:0000303|PubMed:27530662};
DE Flags: Precursor;
OS Crotalus oreganus abyssus (Grand Canyon rattlesnake) (Crotalus abyssus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=128077;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-39, FUNCTION, COFACTOR,
RP MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC STRAIN=Southeastern Arizona; 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 [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, MASS SPECTROMETRY, TOXIC DOSE, AND 3D-STRUCTURE MODELING.
RC TISSUE=Venom;
RX PubMed=24707493; DOI=10.1155/2014/654170;
RA Martins W., Baldasso P.A., Honorio K.M., Maltarollo V.G., Ribeiro R.I.,
RA Carvalho B.M., Soares A.M., Calderon L.A., Stabeli R.G., Caballol M.A.,
RA Acosta G., Oliveira E., Marangoni S., Albericio F., Da Silva S.L.;
RT "A novel phospholipase A 2 (D49) from the venom of the Crotalus oreganus
RT abyssus (North American Grand Canyon rattlesnake).";
RL Biomed. Res. Int. 2014:1-14(2014).
RN [3]
RP NOMENCLATURE, AND FUNCTION.
RC TISSUE=Venom;
RX PubMed=27530662; DOI=10.1016/j.toxicon.2016.08.007;
RA Almeida J.R., Lancellotti M., Soares A.M., Calderon L.A., Ramirez D.,
RA Gonzalez W., Marangoni S., Da Silva S.L.;
RT "CoaTx-II, a new dimeric Lys49 phospholipase A2 from Crotalus oreganus
RT abyssus snake venom with bactericidal potential: insights into its
RT structure and biological roles.";
RL Toxicon 120:147-158(2016).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that shows very low
CC inhibition of ADP-induced platelet aggregation in platelet-rich plasma
CC of human, rabbit and guinea pig (PubMed:12623078). Shows edema-inducing
CC activity and myotoxicity (PubMed:24707493). PLA2 catalyzes the calcium-
CC dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
CC {ECO:0000269|PubMed:12623078, ECO:0000269|PubMed:24707493}.
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:24707493};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:12623078, ECO:0000269|PubMed:24707493};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.9. {ECO:0000269|PubMed:24707493};
CC Temperature dependence:
CC Optimum temperature is 37.3 degrees Celsius.
CC {ECO:0000269|PubMed:24707493};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:24707493}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12623078}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:12623078}.
CC -!- MASS SPECTROMETRY: Mass=13782; Method=Electrospray; Note=Monoisotopic
CC mass.; Evidence={ECO:0000269|PubMed:12623078};
CC -!- MASS SPECTROMETRY: Mass=13793.8; Method=MALDI; Note=Average mass.;
CC Evidence={ECO:0000269|PubMed:24707493};
CC -!- TOXIC DOSE: LD(50) is 1.8 mg/kg by intravenous injection into mice.
CC {ECO:0000269|PubMed:24707493}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
CC -!- CAUTION: PubMed:12623078 presents this protein as coming from C.viridis
CC viridis, whereas PubMed:24707493 concludes it comes from C.oreganus
CC abyssus due to identical sequences, very similar catalytic activity,
CC and geographical origin. {ECO:0000305}.
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DR EMBL; AY120876; AAM80564.1; -; mRNA.
DR AlphaFoldDB; Q7ZTA7; -.
DR SMR; Q7ZTA7; -.
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;
KW Hemostasis impairing toxin; Hydrolase; Lipid degradation; Lipid metabolism;
KW Metal-binding; Myotoxin; Platelet aggregation inhibiting toxin; Secreted;
KW Signal; Toxin.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:12623078"
FT CHAIN 17..138
FT /note="Acidic phospholipase A2 CoaPLA2"
FT /evidence="ECO:0000305|PubMed:12623078"
FT /id="PRO_0000418556"
FT ACT_SITE 63
FT /evidence="ECO:0000250|UniProtKB:P06859"
FT ACT_SITE 105
FT /evidence="ECO:0000250|UniProtKB:P06859"
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"
SQ SEQUENCE 138 AA; 15549 MW; 04FF6D7266DB0BFE CRC64;
MRTLWIVAVL LLGVEGSLVQ FEMLIMKVAK RSGLFSYSAY GCYCGWGGHG RPQDATDHCC
FVHDCCYGKV TDCNPKTASY TYSEENGEIV CGGDDPCKKQ VCECDRVAAI CFRDNIPTYD
NKYWRFPPEN CQEEPEPC
