PA2BD_DABRR
ID PA2BD_DABRR Reviewed; 121 AA.
AC C0HK16;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 06-JUL-2016, sequence version 1.
DT 03-AUG-2022, entry version 17.
DE RecName: Full=Basic phospholipase A2 daboxin P {ECO:0000303|PubMed:27089306};
DE Short=svPLA2 {ECO:0000305};
DE EC=3.1.1.4 {ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000269|PubMed:27089306};
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase {ECO:0000305};
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, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP MASS SPECTROMETRY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=27089306; DOI=10.1371/journal.pone.0153770;
RA Sharma M., Iyer J.K., Shih N., Majumder M., Mattaparthi V.S.,
RA Mukhopadhyay R., Doley R.;
RT "Daboxin P, a major phospholipase A2 enzyme from the Indian Daboia russelii
RT russelii venom targets factor X and factor Xa for its anticoagulant
RT activity.";
RL PLoS ONE 11:E0153770-E0153770(2016).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that exhibits
CC anticoagulant activity, probably by binding to factor X and its
CC activated form factor Xa (F10). Shows no cytotoxicity. PLA2 catalyzes
CC the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-
CC phosphoglycerides. {ECO:0000269|PubMed:27089306}.
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,
CC ECO:0000269|PubMed:27089306};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:27089306};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.6 mM for diheptanoyl thio-phosphatidylcholine
CC {ECO:0000269|PubMed:27089306};
CC Vmax=1.14 mmol/min/mg enzyme {ECO:0000269|PubMed:27089306};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27089306}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:27089306}.
CC -!- MASS SPECTROMETRY: Mass=13597.62; Mass_error=1.28; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:27089306};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR AlphaFoldDB; C0HK16; -.
DR SMR; C0HK16; -.
DR BRENDA; 3.1.1.4; 5485.
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 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 daboxin P"
FT /evidence="ECO:0000269|PubMed:27089306"
FT /id="PRO_0000436848"
FT ACT_SITE 47
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT ACT_SITE 89
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 26..115
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 28..44
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 43..95
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 49..121
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 50..88
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 57..81
FT /evidence="ECO:0000250|UniProtKB:P59071"
FT DISULFID 75..86
FT /evidence="ECO:0000250|UniProtKB:P59071"
SQ SEQUENCE 121 AA; 13612 MW; FCDD41EBB1C9EF29 CRC64;
SLLEFGKMIL EETGKLAIPS YSSYGCYCGW GGKGTPKDAT DRCCFVHDCC YGNLPDCNNK
SKRYRYKKVN GAIVCEKGTS CENRICECDK AAAICFRQNL NTYSKKYMLY PDFLCKGELV
C
