Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P01441 (CX2_NAJOX) Reviewed, UniProtKB/Swiss-Prot

Last modified June 26, 2013. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytotoxin 2
Alternative name(s):
Cytotoxin II
Short name=CTII
OrganismNaja oxiana (Central Asian cobra) (Oxus cobra)
Taxonomic identifier8657 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeElapinaeNaja

Protein attributes

Sequence length60 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This three-finger cytotoxin is a basic protein that interacts and penetrates into the cell membrane, with the tips of all the three loops. Cytotoxins which have a Pro-30 (P-type) interacts with membrane stronger that those which have a 'Ser-28' (S-type). CTII interacts with membrane stronger than CTI. Ref.2 Ref.3 Ref.4

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Sequence similarities

Belongs to the snake three-finger toxin family. Type IA cytotoxin subfamily.

Ontologies

Keywords
   Biological processCytolysis
   Cellular componentSecreted
   Molecular functionCardiotoxin
Toxin
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processcytolysis

Inferred from electronic annotation. Source: UniProtKB-KW

modification of morphology or physiology of other organism

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 6060Cytotoxin 2
PRO_0000093517

Amino acid modifications

Disulfide bond3 ↔ 21 Ref.5 Ref.6
Disulfide bond14 ↔ 38 Ref.5 Ref.6
Disulfide bond42 ↔ 53 Ref.5 Ref.6
Disulfide bond54 ↔ 59 Ref.5 Ref.6

Secondary structure

........... 60
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P01441 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 3512FDB5EED2C5F7

FASTA606,636
        10         20         30         40         50         60 
LKCKKLVPLF SKTCPAGKNL CYKMFMVAAP HVPVKRGCID VCPKSSLLVK YVCCNTDKCN 

« Hide

References

[1]"The isolation and sequence determination of a cytotoxin from the venom of the Middle-Asian cobra Naja naja oxiana."
Grishin E.V., Sukhikh A.P., Adamovich T.B., Ovchinnikov Y.A., Yukelson L.Y.
FEBS Lett. 48:179-183(1974) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Venom.
[2]"ESR study of the interaction of cytotoxin II with model membranes."
Dubinnyi M.A., Dubovskii P.V., Utkin Y.N., Simonova T.N., Barsukov L.I., Arseniev A.S.
Bioorg. Khim. 27:102-113(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[3]"Interaction of the P-type cardiotoxin with phospholipid membranes."
Dubovskii P.V., Lesovoy D.M., Dubinnyi M.A., Utkin Y.N., Arseniev A.S.
Eur. J. Biochem. 270:2038-2046(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PHOSPHOLIPID MEMBRANES.
[4]"Interaction of three-finger toxins with phospholipid membranes: comparison of S- and P-type cytotoxins."
Dubovskii P.V., Lesovoy D.M., Dubinnyi M.A., Konshina A.G., Utkin Y.N., Efremov R.G., Arseniev A.S.
Biochem. J. 387:807-815(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, APPARTENANCE TO P-TYPE CYTOTOXINS.
[5]"Two forms of cytotoxin II (cardiotoxin) from Naja naja oxiana in aqueous solution: spatial structures with tightly bound water molecules."
Dementieva D.V., Bocharov E.V., Arseniev A.S.
Eur. J. Biochem. 263:152-162(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR, DISULFIDE BONDS.
[6]"Membrane binding motif of the P-type cardiotoxin."
Dubovskii P.V., Dementieva D.V., Bocharov E.V., Utkin Y.N., Arseniev A.S.
J. Mol. Biol. 305:137-149(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR, DISULFIDE BONDS.

Cross-references

Sequence databases

PIRH3NJ2R. A01709.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CB9NMR-A1-60[»]
1CCQNMR-A1-60[»]
1FFJNMR-A1-60[»]
ProteinModelPortalP01441.
SMRP01441. Positions 1-60.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG006553.

Family and domain databases

InterProIPR003572. Cytotoxin.
IPR003571. Snake_toxin.
IPR018354. Snake_toxin_BS.
[Graphical view]
PfamPF00087. Toxin_1. 1 hit.
[Graphical view]
PRINTSPR00282. CYTOTOXIN.
PROSITEPS00272. SNAKE_TOXIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP01441.

Entry information

Entry nameCX2_NAJOX
AccessionPrimary (citable) accession number: P01441
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 26, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references