PA2BB_GLOHA
ID PA2BB_GLOHA Reviewed; 138 AA.
AC O42187;
DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 13-DEC-2002, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Basic phospholipase A2 B;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=BPLA(2);
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE AltName: Full=bAhp;
DE Flags: Precursor;
OS Gloydius halys (Chinese water mocassin) (Agkistrodon halys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Gloydius.
OX NCBI_TaxID=8714;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=12232583;
RA Pan H., Ou-Yang L.-L., Yang G.-Z., Zhou Y.-C., Wu X.-F.;
RT "Cloning of the BPLA(2) gene from Agkistrodon halys pallas.";
RL Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 28:579-582(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=9690782; DOI=10.1016/s0041-0101(98)00013-0;
RA Pan H., Liu X.-L., Ou-Yang L.-L., Yang G.-Z., Zhou Y.-C., Li Z.-P.,
RA Wu X.-F.;
RT "Diversity of cDNAs encoding phospholipase A2 from Agkistrodon halys pallas
RT venom, and its expression in E. coli.";
RL Toxicon 36:1155-1163(1998).
RN [3]
RP FUNCTION AS AN ANTICOAGULANT.
RX PubMed=18062812; DOI=10.1186/1472-6807-7-82;
RA Faure G., Gowda V.T., Maroun R.C.;
RT "Characterization of a human coagulation factor Xa-binding site on
RT Viperidae snake venom phospholipases A2 by affinity binding studies and
RT molecular bioinformatics.";
RL BMC Struct. Biol. 7:82-82(2007).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.13 ANGSTROMS) OF 18-138 IN COMPLEX WITH CALCIUM
RP ION, COFACTOR, AND DISULFIDE BONDS.
RC TISSUE=Venom;
RX PubMed=9761847; DOI=10.1107/s0907444997013644;
RA Zhao K., Song S., Lin Z., Zhou Y.-C.;
RT "Structure of a basic phospholipase A2 from Agkistrodon halys pallas at
RT 2.13 A resolution.";
RL Acta Crystallogr. D 54:510-521(1998).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 18-138, FUNCTION, AND DISULFIDE
RP BONDS.
RC TISSUE=Venom;
RX PubMed=10728829; DOI=10.1016/s0041-0101(99)00193-2;
RA Zhao K., Zhou Y.-C., Lin Z.;
RT "Structure of basic phospholipase A2 from Agkistrodon halys pallas:
RT implications for its association, hemolytic and anticoagulant activities.";
RL Toxicon 38:901-916(2000).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that shows potent
CC hemolytic activity, and exhibits medium anticoagulant effects by
CC binding to factor Xa (F10) and inhibiting the prothrombinase activity
CC (IC(50) is 90 nM). It is one of the few phospholipases A2 capable of
CC hydrolyzing the phospholipids of E.coli membranes in the presence of a
CC bactericidal/permeability-increasing protein (BPI) of neutrophils. PLA2
CC catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-
CC sn-phosphoglycerides. {ECO:0000269|PubMed:10728829,
CC ECO:0000269|PubMed:18062812}.
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:0000305|PubMed:9761847};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000305|PubMed:9761847};
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; AF015242; AAB71844.1; -; mRNA.
DR PIR; JC1342; JC1342.
DR PDB; 1B4W; X-ray; 2.60 A; A/B/C/D=17-138.
DR PDB; 1C1J; X-ray; 2.80 A; A/B/C/D=18-138.
DR PDB; 1JIA; X-ray; 2.13 A; A/B=18-138.
DR PDB; 4HG9; X-ray; 1.60 A; A/B/C/D=18-138.
DR PDBsum; 1B4W; -.
DR PDBsum; 1C1J; -.
DR PDBsum; 1JIA; -.
DR PDBsum; 4HG9; -.
DR AlphaFoldDB; O42187; -.
DR SMR; O42187; -.
DR EvolutionaryTrace; O42187; -.
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 Disulfide bond; Hemostasis impairing toxin; Hydrolase; Lipid degradation;
KW Lipid metabolism; Metal-binding; Secreted; Signal; Toxin.
FT SIGNAL 1..16
FT /evidence="ECO:0000250"
FT CHAIN 17..138
FT /note="Basic phospholipase A2 B"
FT /id="PRO_0000022776"
FT ACT_SITE 63
FT /evidence="ECO:0000250|UniProtKB:P06859"
FT ACT_SITE 105
FT /evidence="ECO:0000250|UniProtKB:P06859"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:9761847,
FT ECO:0007744|PDB:1JIA"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:9761847,
FT ECO:0007744|PDB:1JIA"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:9761847,
FT ECO:0007744|PDB:1JIA"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:9761847,
FT ECO:0007744|PDB:1JIA"
FT DISULFID 42..131
FT /evidence="ECO:0000269|PubMed:10728829,
FT ECO:0000269|PubMed:9761847, ECO:0007744|PDB:1B4W,
FT ECO:0007744|PDB:1JIA"
FT DISULFID 44..60
FT /evidence="ECO:0000269|PubMed:10728829,
FT ECO:0000269|PubMed:9761847, ECO:0007744|PDB:1B4W,
FT ECO:0007744|PDB:1JIA"
FT DISULFID 59..111
FT /evidence="ECO:0000269|PubMed:10728829,
FT ECO:0000269|PubMed:9761847, ECO:0007744|PDB:1B4W,
FT ECO:0007744|PDB:1JIA"
FT DISULFID 65..138
FT /evidence="ECO:0000269|PubMed:10728829,
FT ECO:0000269|PubMed:9761847, ECO:0007744|PDB:1B4W,
FT ECO:0007744|PDB:1JIA"
FT DISULFID 66..104
FT /evidence="ECO:0000269|PubMed:10728829,
FT ECO:0000269|PubMed:9761847, ECO:0007744|PDB:1B4W,
FT ECO:0007744|PDB:1JIA"
FT DISULFID 73..97
FT /evidence="ECO:0000269|PubMed:10728829,
FT ECO:0000269|PubMed:9761847, ECO:0007744|PDB:1B4W,
FT ECO:0007744|PDB:1JIA"
FT DISULFID 91..102
FT /evidence="ECO:0000269|PubMed:10728829,
FT ECO:0000269|PubMed:9761847, ECO:0007744|PDB:1B4W,
FT ECO:0007744|PDB:1JIA"
FT HELIX 18..29
FT /evidence="ECO:0007829|PDB:4HG9"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:4HG9"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:4HG9"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:4HG9"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:4HG9"
FT HELIX 55..69
FT /evidence="ECO:0007829|PDB:4HG9"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:4HG9"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:4HG9"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:4HG9"
FT HELIX 96..114
FT /evidence="ECO:0007829|PDB:4HG9"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:4HG9"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:4HG9"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:4HG9"
SQ SEQUENCE 138 AA; 15614 MW; 149D21704F4AA437 CRC64;
MRALWIVAVL LLGVEGSLLQ FRKMIKKMTG KEPVVSYAFY GCYCGSGGRG KPKDATDRCC
FVHDCCYEKL TGCDPKWDDY TYSWKNGTIV CGGDDPCKKE VCECDKAAAI CFRDNLKTYK
KRYMTYPNIL CSSKSEKC
