PA2B1_VIPBN
ID PA2B1_VIPBN Reviewed; 138 AA.
AC Q1RP79;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Basic phospholipase A2 chain HDP-1P;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Heterodimeric neurotoxic phospholipases A2 basic subunit 1;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE Flags: Precursor;
OS Vipera berus nikolskii (Nikolsky's adder) (Vipera nikolskii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Vipera.
OX NCBI_TaxID=1808362;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-32, FUNCTION, AND MASS
RP SPECTROMETRY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=18083205; DOI=10.1016/j.toxicon.2007.11.001;
RA Ramazanova A.S., Zavada L.L., Starkov V.G., Kovyazina I.V., Subbotina T.F.,
RA Kostyukhina E.E., Dementieva I.N., Ovchinnikova T.V., Utkin Y.N.;
RT "Heterodimeric neurotoxic phospholipases A2 -- the first proteins from
RT venom of recently established species Vipera nikolskii: implication of
RT venom composition in viper systematics.";
RL Toxicon 51:524-537(2008).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 17-138, FUNCTION, ACTIVITY
RP REGULATION, AND DISULFIDE BONDS.
RC TISSUE=Venom;
RX PubMed=19500614; DOI=10.1016/j.toxicon.2009.05.024;
RA Gao W., Starkov V.G., He Z.X., Wang Q.H., Tsetlin V.I., Utkin Y.N.,
RA Lin Z.J., Bi R.C.;
RT "Functions, structures and Triton X-100 effect for the catalytic subunits
RT of heterodimeric phospholipases A2 from Vipera nikolskii venom.";
RL Toxicon 54:709-716(2009).
CC -!- FUNCTION: Heterodimer: shows the same activities as the monomer, but
CC with a lower potency.
CC -!- FUNCTION: Monomer: snake venom phospholipase A2 (PLA2) that shows
CC presynaptic neurotoxicity, anticoagulant activity and that weakly
CC inhibits ADP-induced platelet aggregation (PubMed:18083205). Inhibits
CC exocytosis in pancreatic beta cells, confirming it can act
CC presynaptically in inhibiting the exocytosis of neurotransmitters in
CC neurons (PubMed:19500614). PLA2 catalyzes the calcium-dependent
CC hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
CC {ECO:0000269|PubMed:18083205, ECO:0000269|PubMed:19500614}.
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 -!- ACTIVITY REGULATION: Enzymatic activity and neurotoxicity are inhibited
CC by Triton X-100, which has been determined to be located in the center
CC of the hydrophobic channel of the enzyme.
CC {ECO:0000269|PubMed:19500614}.
CC -!- SUBUNIT: Heterodimer; non-covalently linked. The toxic basic protein
CC has phospholipase A2 activity (chain HDP-1P) and the non-toxic acidic
CC protein functions as its inhibitor (chain HPD-1I (AC A4VBF0)).
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: Mass=13798; Mass_error=1; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18083205};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR EMBL; AM238698; CAJ87658.1; -; mRNA.
DR PDB; 2I0U; X-ray; 2.20 A; A/E=17-138.
DR PDBsum; 2I0U; -.
DR AlphaFoldDB; Q1RP79; -.
DR SMR; Q1RP79; -.
DR EvolutionaryTrace; Q1RP79; -.
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:InterPro.
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;
KW Direct protein sequencing; Disulfide bond; Hemostasis impairing toxin;
KW Hydrolase; Metal-binding; Neurotoxin;
KW Platelet aggregation inhibiting toxin; Presynaptic neurotoxin; Secreted;
KW Signal; Toxin.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:18083205"
FT CHAIN 17..138
FT /note="Basic phospholipase A2 chain HDP-1P"
FT /id="PRO_5000079752"
FT ACT_SITE 63
FT /evidence="ECO:0000250"
FT ACT_SITE 105
FT /evidence="ECO:0000250"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 42..131
FT /evidence="ECO:0000269|PubMed:19500614"
FT DISULFID 44..60
FT /evidence="ECO:0000269|PubMed:19500614"
FT DISULFID 59..111
FT /evidence="ECO:0000269|PubMed:19500614"
FT DISULFID 65..138
FT /evidence="ECO:0000269|PubMed:19500614"
FT DISULFID 66..104
FT /evidence="ECO:0000269|PubMed:19500614"
FT DISULFID 73..97
FT /evidence="ECO:0000269|PubMed:19500614"
FT DISULFID 91..102
FT /evidence="ECO:0000269|PubMed:19500614"
FT HELIX 18..29
FT /evidence="ECO:0007829|PDB:2I0U"
FT HELIX 33..37
FT /evidence="ECO:0007829|PDB:2I0U"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:2I0U"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:2I0U"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:2I0U"
FT HELIX 55..69
FT /evidence="ECO:0007829|PDB:2I0U"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:2I0U"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:2I0U"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:2I0U"
FT HELIX 97..114
FT /evidence="ECO:0007829|PDB:2I0U"
FT TURN 115..118
FT /evidence="ECO:0007829|PDB:2I0U"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:2I0U"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:2I0U"
SQ SEQUENCE 138 AA; 15566 MW; 72D55BD516C3E5D9 CRC64;
MRILWIVAVC LIGVEGNLFQ FAKMINGKLG AFSVWNYISY GCYCGWGGQG TPKDATDRCC
FVHDCCYGRV RGCNPKLAIY AYSFKKGNIV CGKNNGCLRD ICECDRVAAN CFHQNQNTYN
KNYKFLSSSR CRQTSEQC
