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UniProtKB/Swiss-Prot entry P04084


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PA2I_VIPAE
Primary accession number P04084
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1986
Sequence was last modified on July 15, 1998 (Sequence version 3)
Annotations were last modified on    November 4, 2008 (Entry version 78)
Name and origin of the protein
Protein name Phospholipase A2 inhibitor
Synonyms Vipoxin toxic component
Vipoxin A chain
Inh
Gene name None
From
Vipera ammodytes meridionalis (Eastern sand viper) [TaxID: 73841] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea; Viperidae; Viperinae; Vipera.
Protein existence 1: Evidence at protein level;
References
[1]
PROTEIN SEQUENCE.
STRAIN=Bulgarian;
TISSUE=Venom;
PubMed=6489936 [NCBI, ExPASy, EBI, Israel, Japan]
Mancheva I., Kleinschmidt T., Aleksiev B., Braunitzer G.;
"Sequence homology between phospholipase and its inhibitor in snake venom. The primary structure of the inhibitor of vipoxin from the venom of the Bulgarian viper (Vipera ammodytes ammodytes, Serpentes).";
Hoppe-Seyler's Z. Physiol. Chem. 365:885-894(1984).
[2]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
TISSUE=Venom;
DOI=10.1006/jmbi.1993.1297; PubMed=8510159 [NCBI, ExPASy, EBI, Israel, Japan]
Betzel C., Visanji M., Wilson K.S., Genov N., Mancheva I., Aleksiev B., Singh T.P.;
"Crystallization and preliminary X-ray analysis of vipoxin, a complex between a toxic phospholipase A2 and its natural polypeptide inhibitor.";
J. Mol. Biol. 231:498-500(1993).
[3]
X-RAY CRYSTALLOGRAPHY (2 ANGSTROMS).
DOI=10.1016/S0014-5793(97)00853-3; PubMed=9276469 [NCBI, ExPASy, EBI, Israel, Japan]
Perbandt M., Wilson J.C., Eschenburg S., Mancheva I., Aleksiev B., Genov N., Willingmann P., Weber W., Singh T.P., Betzel C.;
"Crystal structure of vipoxin at 2.0 A: an example of regulation of a toxic function generated by molecular evolution.";
FEBS Lett. 412:573-577(1997).
[4]
X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS), AND SEQUENCE REVISION TO 34.
TISSUE=Venom;
DOI=10.1006/jmbi.1996.0778; PubMed=9054978 [NCBI, ExPASy, EBI, Israel, Japan]
Devedjiev Y., Popov A., Atanasov B., Bartunik H.-D.;
"X-ray structure at 1.76-A resolution of a polypeptide phospholipase A2 inhibitor.";
J. Mol. Biol. 266:160-172(1997).
[5]
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).
DOI=10.1107/S0907444901013543; PubMed=11679719 [NCBI, ExPASy, EBI, Israel, Japan]
Banumathi S., Rajashankar K.R., Notzel C., Aleksiev B., Singh T.P., Genov N., Betzel C.;
"Structure of the neurotoxic complex vipoxin at 1.4 A resolution.";
Acta Crystallogr. D 57:1552-1559(2001).
Comments
  • FUNCTION: The vipoxin complex shows postsynaptic neurotoxicity. Phospholipase A2 inhibitor inhibits the phospholipase A2 of vipoxin (up to 60%) and also the phospholipases A2 from other snake venoms (15%-20%).
  • COFACTOR: Binds 1 calcium ion per subunit (By similarity).
  • SUBUNIT: The main toxin of this snake venom is vipoxin, a complex of a toxic basic protein (B chain) having phospholipase A2 activity and a nontoxic acidic protein (A chain) functioning as its inhibitor. Without the inhibitor, the basic protein becomes unstable and within 12-14 days loses its enzymatic activity.
  • SUBCELLULAR LOCATION: Secreted.
  • TISSUE SPECIFICITY: Expressed by the venom gland.
  • MISCELLANEOUS: The supposed calcium binding region close to Asp-48 of the basic phospholipase A2 is blocked by the side chain of Lys-60 of its inhibitor.
  • SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
  • CAUTION: The tryptic peptide in position 54-60 was incorrectly assigned to be after what is now position 83.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
PIR B29290; PSVII.
3D structure databases
PDB
1AOK; X-ray; 2.00 A; A=1-122.[ExPASy / RCSB / EBI]
1JLT; X-ray; 1.40 A; A=1-122.[ExPASy / RCSB / EBI]
1Q5T; X-ray; 1.90 A; A/B=1-122.[ExPASy / RCSB / EBI]
1VPI; X-ray; 1.76 A; A=1-122.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1AOK; -.
1JLT; -.
1Q5T; -.
1VPI; -.
ModBase P04084.
Ontologies
GO
GO:0005576; Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0045211; Cellular component: postsynaptic membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0030550; Molecular function: acetylcholine receptor inhibitor activity (inferred from electronic annotation from UniProtKB-KW).
GO:0019834; Molecular function: phospholipase A2 inhibitor activity (inferred from electronic annotation from UniProtKB-KW).
GO:0009405; Biological process: pathogenesis (inferred from electronic annotation from UniProtKB-KW).
GO:0007268; Biological process: synaptic transmission (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR016090; Phospholipase_A2.
IPR013090; Phospholipase_A2_AS.
IPR001211; Phospholipase_A2_euk.
Graphical view of domain structure.
Gene3D G3DSA:1.20.90.10; Phospholipase_A2; 1.
PANTHER PTHR11716; Phospholipase_A2; 1.
Pfam PF00068; Phospholip_A2_1; 1.
Pfam graphical view of domain structure.
PRINTS PR00389; PHPHLIPASEA2.
ProDom PD000303; PhospholipaseA2; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00085; PA2c; 1.
SMART graphical view of domain structure.
PROSITE PS00119; PA2_ASP; 1.
PS00118; PA2_HIS; FALSE_NEG.
BLOCKS P04084.
ProtoNet P04084.
Phylogenomic databases
HOVERGEN P04084; -.
Other
LinkHub P04084; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Calcium; Direct protein sequencing; Metal-binding; Neurotoxin; Phospholipase A2 inhibitor; Postsynaptic neurotoxin; Secreted; Toxin.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   122  122     Phospholipase A2 inhibitor. PRO_0000161713
METAL   27    27        Calcium; via carbonyl oxygen (By similarity). 
METAL   29    29        Calcium; via carbonyl oxygen (By similarity). 
METAL   31    31        Calcium; via carbonyl oxygen (By similarity). 
METAL   48    48        Calcium (By similarity). 
DISULFID   26   115         
DISULFID   28    44         
DISULFID   43    95         
DISULFID   49   122         
DISULFID   50    88         
DISULFID   57    81         
DISULFID   75    86         
HELIX   2    13  12      
HELIX   17    19  3      
HELIX   21    23  3      
TURN   25    28  4      
HELIX   39    52  14      
TURN   59    61  3      
STRAND   66    69  4      
STRAND   72    75  4      
HELIX   80    98  19      
HELIX   99   102  4      
HELIX   105   107  3      
HELIX   111   113  3      
Sequence information
Length: 122 AA [This is the length of the unprocessed precursor] Molecular weight: 13639 Da [This is the MW of the unprocessed precursor] CRC64: 3759601D80ABA697 [This is a checksum on the sequence]
        10         20         30         40         50         60 
NLFQFGDMIL QKTGKEAVHS YAIYGCYCGW GGQGRAQDAT DRCCFAQDCC YGRVNDCNPK 

        70         80         90        100        110        120 
TATYTYSFEN GDIVCGDNDL CLRAVCECDR AAAICLGENV NTYDKNYEYY SISHCTEESE 


QC 

P04084 in FASTA format

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