PA2B_DABRR
ID PA2B_DABRR Reviewed; 121 AA.
AC P81458;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Basic phospholipase A2 RVV-VD;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE AltName: Full=R1;
OS Daboia russelii (Russel's viper) (Vipera russelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Daboia.
OX NCBI_TaxID=8707;
RN [1]
RP PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), AND DISULFIDE
RP BONDS.
RC TISSUE=Venom;
RX PubMed=9604284; DOI=10.1016/s0041-0101(97)00051-2;
RA Carredano E., Westerlund B., Persson B., Saarinen M., Ramaswamy S.,
RA Eaker D., Eklund H.;
RT "The three-dimensional structures of two toxins from snake venom throw
RT light on the anticoagulant and neurotoxic sites of phospholipase A2.";
RL Toxicon 36:75-92(1998).
RN [2]
RP PROTEIN SEQUENCE OF 1-50, FUNCTION, AND SUBCELLULAR LOCATION.
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).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that has low enzymatic
CC activity, is devoid of lethal activity but has strong anticoagulant
CC activity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC groups in 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;
CC Evidence={ECO:0000250|UniProtKB:P14418};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000250|UniProtKB:P14418};
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9604284}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:8835338}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR PDB; 1VIP; X-ray; 2.20 A; A=1-121.
DR PDBsum; 1VIP; -.
DR AlphaFoldDB; P81458; -.
DR SMR; P81458; -.
DR Allergome; 9633; Dab ru 1.
DR EvolutionaryTrace; P81458; -.
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 3D-structure; Blood coagulation cascade inhibiting toxin; Calcium;
KW Direct protein sequencing; Disulfide bond; Hemostasis impairing toxin;
KW Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding; Secreted;
KW Toxin.
FT CHAIN 1..121
FT /note="Basic phospholipase A2 RVV-VD"
FT /id="PRO_0000161716"
FT ACT_SITE 47
FT /evidence="ECO:0000305|PubMed:9604284"
FT ACT_SITE 89
FT /evidence="ECO:0000305|PubMed:9604284"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT DISULFID 26..115
FT /evidence="ECO:0000269|PubMed:9604284,
FT ECO:0007744|PDB:1VIP"
FT DISULFID 28..44
FT /evidence="ECO:0000269|PubMed:9604284,
FT ECO:0007744|PDB:1VIP"
FT DISULFID 43..95
FT /evidence="ECO:0000269|PubMed:9604284,
FT ECO:0007744|PDB:1VIP"
FT DISULFID 49..121
FT /evidence="ECO:0000269|PubMed:9604284,
FT ECO:0007744|PDB:1VIP"
FT DISULFID 50..88
FT /evidence="ECO:0000269|PubMed:9604284,
FT ECO:0007744|PDB:1VIP"
FT DISULFID 57..81
FT /evidence="ECO:0000269|PubMed:9604284,
FT ECO:0007744|PDB:1VIP"
FT DISULFID 75..86
FT /evidence="ECO:0000269|PubMed:9604284,
FT ECO:0007744|PDB:1VIP"
FT HELIX 2..13
FT /evidence="ECO:0007829|PDB:1VIP"
FT HELIX 17..20
FT /evidence="ECO:0007829|PDB:1VIP"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:1VIP"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:1VIP"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:1VIP"
FT HELIX 39..53
FT /evidence="ECO:0007829|PDB:1VIP"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:1VIP"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:1VIP"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:1VIP"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:1VIP"
FT HELIX 80..98
FT /evidence="ECO:0007829|PDB:1VIP"
FT TURN 99..102
FT /evidence="ECO:0007829|PDB:1VIP"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:1VIP"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:1VIP"
SQ SEQUENCE 121 AA; 13626 MW; 98CBC4A8922A89D1 CRC64;
NLFQFAEMIV KMTGKNPLSS YSDYGCYCGW GGKGKPQDAT DRCCFVHDCC YEKVKSCKPK
LSLYSYSFQN GGIVCGDNHS CKRAVCECDR VAATCFRDNL NTYDKKYHNY PPSQCTGTEQ
C
