PA2A7_DABSI
ID PA2A7_DABSI Reviewed; 138 AA.
AC P31100; B2YHV2;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Acidic phospholipase A2 RV-7;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=F7;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE AltName: Full=Phospholipase A2 inhibitor;
DE AltName: Full=S4;
DE AltName: Full=Viperotoxin F;
DE AltName: Full=Viperotoxin non-toxic acidic component;
DE Flags: Precursor;
OS Daboia siamensis (Eastern Russel's viper) (Daboia russelii siamensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Daboia.
OX NCBI_TaxID=343250;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 17-66.
RC TISSUE=Venom, and Venom gland;
RX PubMed=1425670; DOI=10.1111/j.1432-1033.1992.tb17330.x;
RA Wang Y.-M., Lu P.-J., Ho C.-L., Tsai I.-H.;
RT "Characterization and molecular cloning of neurotoxic phospholipases A2
RT from Taiwan viper (Vipera russelli formosensis).";
RL Eur. J. Biochem. 209:635-641(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Sai-Ngam A., Phongtananant S., Nuchprayoon I.;
RT "Study of phospholipase A2 genes and their expressions in Thai Russell's
RT viper venom glands.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 17-66, FUNCTION, AND TOXIC DOSE.
RC TISSUE=Venom;
RX PubMed=8835338; DOI=10.1016/0041-0101(95)00114-x;
RA Tsai I.-H., Lu P.-J., Su J.-C.;
RT "Two types of Russell's viper revealed by variation in phospholipases A2
RT from venom of the subspecies.";
RL Toxicon 34:99-109(1996).
RN [4]
RP PROTEIN SEQUENCE OF 17-28 AND 107-121.
RC TISSUE=Venom;
RX PubMed=19457351; DOI=10.1016/j.jprot.2009.01.006;
RA Risch M., Georgieva D., von Bergen M., Jehmlich N., Genov N., Arni R.K.,
RA Betzel C.;
RT "Snake venomics of the Siamese Russell's viper (Daboia russelli siamensis)
RT -- relation to pharmacological activities.";
RL J. Proteomics 72:256-269(2009).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 17-138, AND DISULFIDE BONDS.
RC TISSUE=Venom;
RX PubMed=14501106; DOI=10.1107/s0907444903014987;
RA Perbandt M., Tsai I.-H., Fuchs A., Banumathi S., Rajashankar K.R.,
RA Georgieva D., Kalkura N., Singh T.P., Genov N., Betzel C.;
RT "Structure of the heterodimeric neurotoxic complex viperotoxin F (RV-4/RV-
RT 7) from the venom of Vipera russelli formosensis at 1.9 A resolution.";
RL Acta Crystallogr. D 59:1679-1687(2003).
CC -!- FUNCTION: Heterodimer: RV-4/RV-7 targets the presynaptic sites of the
CC neuromuscular junction. {ECO:0000269|PubMed:8835338}.
CC -!- FUNCTION: Monomer: snake venom phospholipase A2 (PLA2) RV-7 that has
CC low enzymatic activity and is not toxic. It inhibits the enzymatic
CC activity of RV-4 in vitro but potentiates its lethal potency and
CC neurotoxicity. It may facilitate the specific binding of RV-4 to its
CC presynaptic binding sites, probably by acting as a chaperone,
CC minimizing distraction and destruction of RV-4 en route to the site of
CC action by reducing non-specific binding to muscle and other organs.
CC PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in
CC 3-sn-phosphoglycerides. {ECO:0000269|PubMed:8835338}.
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. {ECO:0000250};
CC -!- SUBUNIT: Heterodimer of a weakly toxic basic protein having
CC phospholipase A2 activity (RV-4) and a non-toxic acidic protein which
CC inhibits its enzymatic activity but potentiates its lethal potency and
CC neurotoxicity (RV-7).
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR EMBL; X68386; CAA48457.1; -; mRNA.
DR EMBL; EU556499; ACD43466.1; -; mRNA.
DR EMBL; EU556501; ACD43468.1; -; Genomic_DNA.
DR PDB; 1OQS; X-ray; 1.90 A; A/C/E/G=17-138.
DR PDBsum; 1OQS; -.
DR AlphaFoldDB; P31100; -.
DR SMR; P31100; -.
DR EvolutionaryTrace; P31100; -.
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:0019834; F:phospholipase A2 inhibitor activity; IEA:UniProtKB-KW.
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 3D-structure; Calcium; Direct protein sequencing; Disulfide bond;
KW Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding; Neurotoxin;
KW Phospholipase A2 inhibitor; Presynaptic neurotoxin; Secreted; Signal;
KW Toxin.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:1425670,
FT ECO:0000269|PubMed:8835338"
FT CHAIN 17..138
FT /note="Acidic phospholipase A2 RV-7"
FT /id="PRO_0000022978"
FT ACT_SITE 63
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT ACT_SITE 105
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT DISULFID 42..131
FT /evidence="ECO:0000269|PubMed:14501106"
FT DISULFID 44..60
FT /evidence="ECO:0000269|PubMed:14501106"
FT DISULFID 59..111
FT /evidence="ECO:0000269|PubMed:14501106"
FT DISULFID 65..138
FT /evidence="ECO:0000269|PubMed:14501106"
FT DISULFID 66..104
FT /evidence="ECO:0000269|PubMed:14501106"
FT DISULFID 73..97
FT /evidence="ECO:0000269|PubMed:14501106"
FT DISULFID 91..102
FT /evidence="ECO:0000269|PubMed:14501106"
FT CONFLICT 27
FT /note="E -> Q (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 18..29
FT /evidence="ECO:0007829|PDB:1OQS"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:1OQS"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:1OQS"
FT TURN 41..44
FT /evidence="ECO:0007829|PDB:1OQS"
FT HELIX 55..68
FT /evidence="ECO:0007829|PDB:1OQS"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:1OQS"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:1OQS"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:1OQS"
FT HELIX 96..115
FT /evidence="ECO:0007829|PDB:1OQS"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:1OQS"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:1OQS"
FT TURN 125..129
FT /evidence="ECO:0007829|PDB:1OQS"
SQ SEQUENCE 138 AA; 15421 MW; 6DC115BBA979827E CRC64;
MRTLWIVAVC LIGVEGNLFQ FGEMILEKTG KEVVHSYAIY GCYCGWGGQG RAQDATDRCC
FVHDCCYGTV NDCNPKTATY SYSFENGDIV CGDNDLCLRT VCECDRAAAI CLGQNVNTYD
KNYEYYSISH CTEESEQC
