PA2BC_CROOL
ID PA2BC_CROOL Reviewed; 47 AA.
AC C0HK05;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 08-JUN-2016, sequence version 1.
DT 03-AUG-2022, entry version 16.
DE RecName: Full=Basic phospholipase A2 ColTx-1 {ECO:0000305|PubMed:26996495};
DE Short=svPLA2 {ECO:0000250|UniProtKB:P14421};
DE EC=3.1.1.4 {ECO:0000269|PubMed:26996495};
DE AltName: Full=Basic phospholipase A2 ColTx-I {ECO:0000303|PubMed:26996495};
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase {ECO:0000250|UniProtKB:P14421};
DE Flags: Fragment;
OS Crotalus oreganus lutosus (Great basin rattlesnake) (Crotalus viridis
OS lutosus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=332626 {ECO:0000303|PubMed:26996495};
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, MASS
RP SPECTROMETRY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom {ECO:0000303|PubMed:26996495};
RX PubMed=26996495; DOI=10.1016/j.toxicon.2016.03.008;
RA Almeida J.R., Resende L.M., Silva A.G., Ribeiro R.I., Stabeli R.G.,
RA Soares A.M., Calderon L.A., Marangoni S., Da Silva S.L.;
RT "Biochemical and functional studies of ColTx-I, a new myotoxic
RT phospholipase A2 isolated from Crotalus oreganus lutosus (Great Basin
RT rattlesnake) snake venom.";
RL Toxicon 117:1-12(2016).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that shows edema-inducing
CC activity and local and systemic myotoxicity. PLA2 catalyzes the
CC calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-
CC phosphoglycerides. {ECO:0000269|PubMed:26996495}.
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:26996495};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:26996495};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000250|UniProtKB:P14421};
CC -!- ACTIVITY REGULATION: In the presence of Ca(2+) ions, activated by
CC Mn(2+) or Mg(2+) ions. Inhibited by Cd(2+) or Zn(2+) ions. Inhibited by
CC metal chelators EDTA and EGTA. {ECO:0000269|PubMed:26996495}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.09 mM for 4-nitro-3-octanoyl benzioc acid (NOBA)
CC {ECO:0000269|PubMed:26996495};
CC Vmax=15.97 nmol/min/mg enzyme with NOBA as substrate
CC {ECO:0000269|PubMed:26996495};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:26996495};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:26996495};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26996495}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:26996495}.
CC -!- MASS SPECTROMETRY: Mass=14145; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:26996495};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR AlphaFoldDB; C0HK05; -.
DR SMR; C0HK05; -.
DR BRENDA; 3.1.1.4; 8635.
DR SABIO-RK; C0HK05; -.
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 Gene3D; 1.20.90.10; -; 1.
DR InterPro; IPR001211; PLipase_A2.
DR InterPro; IPR016090; PLipase_A2_dom.
DR InterPro; IPR036444; PLipase_A2_dom_sf.
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.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Lipid degradation; Lipid metabolism; Metal-binding; Myotoxin; Secreted;
KW Toxin.
FT CHAIN 1..>47
FT /note="Basic phospholipase A2 ColTx-1"
FT /evidence="ECO:0000269|PubMed:26996495"
FT /id="PRO_0000436391"
FT ACT_SITE 47
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 DISULFID 26..?
FT /evidence="ECO:0000250|UniProtKB:P14421"
FT DISULFID 28..44
FT /evidence="ECO:0000250|UniProtKB:P14421"
FT DISULFID 43..?
FT /evidence="ECO:0000250|UniProtKB:P14421"
FT NON_TER 47
FT /evidence="ECO:0000269|PubMed:26996495"
SQ SEQUENCE 47 AA; 5547 MW; DEA0265435675F6E CRC64;
HLLQFNKMIK FETRKNAIPF YAFYGCYCGW GGRGRPKDAT DRCCFVH
