PA2HA_VIPAE
ID PA2HA_VIPAE Reviewed; 122 AA.
AC P04084;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 3.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=Acidic phospholipase A2 homolog vipoxin A chain;
DE Short=svPLA2 homolog;
DE AltName: Full=Acidic phospholipase A2 inhibitor vipoxin A chain;
DE AltName: Full=Vipoxin acidic component;
DE Short=VAC;
DE AltName: Full=Vipoxin non-toxic component;
OS Vipera ammodytes meridionalis (Eastern sand viper).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Vipera.
OX NCBI_TaxID=73841;
RN [1]
RP PROTEIN SEQUENCE.
RC STRAIN=Bulgarian; TISSUE=Venom;
RX PubMed=6489936; DOI=10.1515/bchm2.1984.365.2.885;
RA Mancheva I., Kleinschmidt T., Aleksiev B., Braunitzer G.;
RT "Sequence homology between phospholipase and its inhibitor in snake venom.
RT The primary structure of the inhibitor of vipoxin from the venom of the
RT Bulgarian viper (Vipera ammodytes ammodytes, Serpentes).";
RL Hoppe-Seyler's Z. Physiol. Chem. 365:885-894(1984).
RN [2]
RP FUNCTION, SUBUNIT, AND LETHAL DOSES.
RX PubMed=23554559; DOI=10.2478/v10102-012-0028-z;
RA Atanasov V.N., Stoykova S., Goranova Y., Mitewa M., Petrova S.;
RT "Acute toxicity of vipoxin and its components: is the acidic component an
RT 'inhibitor' of PLA2 toxicity?";
RL Interdiscip. Toxicol. 5:169-172(2012).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RC TISSUE=Venom;
RX PubMed=8510159; DOI=10.1006/jmbi.1993.1297;
RA Betzel C., Visanji M., Wilson K.S., Genov N., Mancheva I., Aleksiev B.,
RA Singh T.P.;
RT "Crystallization and preliminary X-ray analysis of vipoxin, a complex
RT between a toxic phospholipase A2 and its natural polypeptide inhibitor.";
RL J. Mol. Biol. 231:498-500(1993).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH VIPOXIN B CHAIN, AND
RP DISULFIDE BONDS.
RX PubMed=9276469; DOI=10.1016/s0014-5793(97)00853-3;
RA Perbandt M., Wilson J.C., Eschenburg S., Mancheva I., Aleksiev B.,
RA Genov N., Willingmann P., Weber W., Singh T.P., Betzel C.;
RT "Crystal structure of vipoxin at 2.0 A: an example of regulation of a toxic
RT function generated by molecular evolution.";
RL FEBS Lett. 412:573-577(1997).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS), AND SEQUENCE REVISION TO 34.
RC TISSUE=Venom;
RX PubMed=9054978; DOI=10.1006/jmbi.1996.0778;
RA Devedjiev Y., Popov A., Atanasov B., Bartunik H.-D.;
RT "X-ray structure at 1.76-A resolution of a polypeptide phospholipase A2
RT inhibitor.";
RL J. Mol. Biol. 266:160-172(1997).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH VIPOXIN B CHAIN, AND
RP DISULFIDE BONDS.
RX PubMed=11679719; DOI=10.1107/s0907444901013543;
RA Banumathi S., Rajashankar K.R., Notzel C., Aleksiev B., Singh T.P.,
RA Genov N., Betzel C.;
RT "Structure of the neurotoxic complex vipoxin at 1.4 A resolution.";
RL Acta Crystallogr. D 57:1552-1559(2001).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF HOMODIMER IN COMPLEX WITH SULFATE
RP IONS WHICH MIMIC THE TARGET MEMBRANE, AND DISULFIDE BONDS.
RC TISSUE=Venom;
RX PubMed=15003507; DOI=10.1016/j.bbrc.2004.01.174;
RA Georgieva D.N., Perbandt M., Rypniewski W., Hristov K., Genov N.,
RA Betzel C.;
RT "The X-ray structure of a snake venom Gln48 phospholipase A2 at 1.9A
RT resolution reveals anion-binding sites.";
RL Biochem. Biophys. Res. Commun. 316:33-38(2004).
CC -!- FUNCTION: Heterodimer: postsynaptic neurotoxin.
CC {ECO:0000269|PubMed:23554559}.
CC -!- FUNCTION: Monomer: Acidic phospholipase A2 homolog that is non-toxic.
CC {ECO:0000269|PubMed:23554559}.
CC -!- SUBUNIT: Heterodimer of A and B (AC P14420) chains; non-covalently
CC linked. The A chain (acidic) is non-toxic, and increases the toxicity
CC of the B chain (basic). The A chain may act as factor stabilizing the
CC complex structure and hence retaining its toxicity by preventing non-
CC specific binding. Upon binding to the target membranes the A chain may
CC dissociate. {ECO:0000269|PubMed:11679719, ECO:0000269|PubMed:15003507,
CC ECO:0000269|PubMed:23554559, ECO:0000269|PubMed:9276469}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- TOXIC DOSE: Heterodimer: LD(50) is 0.7-1.2 mg/kg by intraperitoneal
CC injection into mice and 0.9-1.3 mg/kg by intravenous injection into
CC mice. {ECO:0000269|PubMed:23554559}.
CC -!- TOXIC DOSE: Heterodimer: LD(50) is 0.9-1.3 mg/kg by intravenous
CC injection into mice. {ECO:0000269|PubMed:23554559}.
CC -!- TOXIC DOSE: Monomer: LD(50) is >30 mg/kg by intraperitoneal injection
CC into mice. {ECO:0000269|PubMed:23554559}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
CC -!- CAUTION: In contrast to other phospholipases, it lacks the typical His
CC active site (His->Gln in position 47). {ECO:0000305}.
CC -!- CAUTION: The acidic chain was originally postulated to act as an
CC inhibitor of the basic chain. {ECO:0000305|PubMed:6489936}.
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DR PIR; B29290; PSVII.
DR PDB; 1AOK; X-ray; 2.00 A; A=1-122.
DR PDB; 1JLT; X-ray; 1.40 A; A=1-122.
DR PDB; 1Q5T; X-ray; 1.90 A; A/B=1-122.
DR PDB; 1VPI; X-ray; 1.76 A; A=1-122.
DR PDBsum; 1AOK; -.
DR PDBsum; 1JLT; -.
DR PDBsum; 1Q5T; -.
DR PDBsum; 1VPI; -.
DR AlphaFoldDB; P04084; -.
DR SMR; P04084; -.
DR MINT; P04084; -.
DR EvolutionaryTrace; P04084; -.
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:InterPro.
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 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.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Neurotoxin;
KW Postsynaptic neurotoxin; Secreted; Toxin.
FT CHAIN 1..122
FT /note="Acidic phospholipase A2 homolog vipoxin A chain"
FT /id="PRO_0000161713"
FT DISULFID 26..115
FT /evidence="ECO:0000269|PubMed:11679719,
FT ECO:0000269|PubMed:9276469, ECO:0007744|PDB:1AOK,
FT ECO:0007744|PDB:1JLT"
FT DISULFID 28..44
FT /evidence="ECO:0000269|PubMed:11679719,
FT ECO:0000269|PubMed:9276469, ECO:0007744|PDB:1AOK,
FT ECO:0007744|PDB:1JLT"
FT DISULFID 43..95
FT /evidence="ECO:0000269|PubMed:11679719,
FT ECO:0000269|PubMed:9276469, ECO:0007744|PDB:1AOK,
FT ECO:0007744|PDB:1JLT"
FT DISULFID 49..122
FT /evidence="ECO:0000269|PubMed:11679719,
FT ECO:0000269|PubMed:9276469, ECO:0007744|PDB:1AOK,
FT ECO:0007744|PDB:1JLT"
FT DISULFID 50..88
FT /evidence="ECO:0000269|PubMed:11679719,
FT ECO:0000269|PubMed:9276469, ECO:0007744|PDB:1AOK,
FT ECO:0007744|PDB:1JLT"
FT DISULFID 57..81
FT /evidence="ECO:0000269|PubMed:11679719,
FT ECO:0000269|PubMed:9276469, ECO:0007744|PDB:1AOK,
FT ECO:0007744|PDB:1JLT"
FT DISULFID 75..86
FT /evidence="ECO:0000269|PubMed:11679719,
FT ECO:0000269|PubMed:9276469, ECO:0007744|PDB:1AOK,
FT ECO:0007744|PDB:1JLT"
FT HELIX 2..13
FT /evidence="ECO:0007829|PDB:1JLT"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:1JLT"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:1JLT"
FT TURN 25..28
FT /evidence="ECO:0007829|PDB:1JLT"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:1Q5T"
FT HELIX 39..52
FT /evidence="ECO:0007829|PDB:1JLT"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:1Q5T"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:1JLT"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:1JLT"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:1JLT"
FT HELIX 80..98
FT /evidence="ECO:0007829|PDB:1JLT"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:1JLT"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:1JLT"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:1JLT"
SQ SEQUENCE 122 AA; 13639 MW; 3759601D80ABA697 CRC64;
NLFQFGDMIL QKTGKEAVHS YAIYGCYCGW GGQGRAQDAT DRCCFAQDCC YGRVNDCNPK
TATYTYSFEN GDIVCGDNDL CLRAVCECDR AAAICLGENV NTYDKNYEYY SISHCTEESE
QC
