PA2AB_CALRH
ID PA2AB_CALRH Reviewed; 126 AA.
AC Q9PVF0;
DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Acidic phospholipase A2 S1E6-b;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE Flags: Precursor; Fragment;
OS Calloselasma rhodostoma (Malayan pit viper) (Agkistrodon rhodostoma).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Calloselasma.
OX NCBI_TaxID=8717;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, AND MASS SPECTROMETRY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=11054123; DOI=10.1046/j.1432-1327.2000.01766.x;
RA Tsai I.-H., Wang Y.-M., Au L.-C., Ko T.-P., Chen Y.-H., Chu Y.-F.;
RT "Phospholipases A2 from Callosellasma rhodostoma venom gland. Cloning and
RT sequencing of 10 of the cDNAs, three-dimensional modelling and chemical
RT modification of the major isozyme.";
RL Eur. J. Biochem. 267:6684-6691(2000).
CC -!- FUNCTION: Snake venom phospholipase that inhibits ADP-induced platelet
CC aggregation. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-
CC acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:11054123}.
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};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11054123}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: Mass=14052; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:11054123};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR EMBL; AF104069; AAF03253.1; -; mRNA.
DR AlphaFoldDB; Q9PVF0; -.
DR SMR; Q9PVF0; -.
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; Disulfide bond; Hemostasis impairing toxin; Hydrolase;
KW Lipid degradation; Lipid metabolism; Metal-binding;
KW Platelet aggregation inhibiting toxin; Secreted; Signal; Toxin.
FT SIGNAL <1..3
FT CHAIN 4..126
FT /note="Acidic phospholipase A2 S1E6-b"
FT /id="PRO_0000022778"
FT ACT_SITE 50
FT /evidence="ECO:0000250"
FT ACT_SITE 92
FT /evidence="ECO:0000250"
FT BINDING 30
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 32
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 34
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 29..119
FT /evidence="ECO:0000250"
FT DISULFID 31..47
FT /evidence="ECO:0000250"
FT DISULFID 46..98
FT /evidence="ECO:0000250"
FT DISULFID 52..126
FT /evidence="ECO:0000250"
FT DISULFID 53..91
FT /evidence="ECO:0000250"
FT DISULFID 60..84
FT /evidence="ECO:0000250"
FT DISULFID 78..89
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 126 AA; 14352 MW; 4AE0C1B999E423B9 CRC64;
VEGSLVQFET LIMKLAKRSG FFWYSFYGCY CGWGGHGLPQ DPTDRCCFVH DCCYGKVTNC
NPKTATYSYT EENDGIVCGG DDPCKKQVCE CDRVAAMCFR DNKDTYDSDK YWKLPPQKCQ
EDPEPC
