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P28879 (CAS2_CONST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Alpha-conotoxin S2
Alternative name(s):
Alpha-conotoxin SII
OrganismConus striatus (Striated cone)
Taxonomic identifier6493 [NCBI]
Taxonomic lineageEukaryotaMetazoaLophotrochozoaMolluscaGastropodaCaenogastropodaHypsogastropodaNeogastropodaConoideaConidaeConus

Protein attributes

Sequence length72 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. Has no effect on the release of catecholamines evoked by nicotine. Ref.5

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom duct.

Domain

The cysteine framework is II (CCC-C-C-C).

Sequence similarities

Belongs to the conotoxin A superfamily.

Mass spectrometry

Molecular mass is 1790.3 Da from positions 51 - 69. Determined by ESI. Ref.5

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionAcetylcholine receptor inhibiting toxin
Neurotoxin
Postsynaptic neurotoxin
Toxin
   PTMDisulfide bond
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processpathogenesis

Inferred from electronic annotation. Source: InterPro

   Cellular_componentother organism postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionacetylcholine receptor inhibitor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Propeptide22 – 5029
PRO_0000034889
Peptide51 – 6919Alpha-conotoxin S2 Ref.4
PRO_0000034890
Propeptide70 – 723
PRO_0000034891

Amino acid modifications

Disulfide bond52 ↔ 68 Ref.5
Disulfide bond53 ↔ 58 Ref.5
Disulfide bond54 ↔ 64 Ref.5

Experimental info

Sequence conflict231P → T no nucleotide entry Ref.1
Sequence conflict721L → I in AAN77902. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P28879 [UniParc].

Last modified September 5, 2006. Version 3.
Checksum: 521191749F4A94CF

FASTA727,830
        10         20         30         40         50         60 
MGMRMMFTVF LLVVLATTVV SFPSDRASDG RDDEAKDERS DMHESDRNGR GCCCNPACGP 

        70 
NYGCGTSCSR TL 

« Hide

References

[1]"Conopeptides from Conus striatus and Conus textile by cDNA cloning."
Lu B.-S., Yu F., Zhao D., Huang P.-T., Huang C.-F.
Peptides 20:1139-1144(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Venom duct.
[2]"cDNA cloning of two A-superfamily conotoxins from Conus striatus."
Wang C.-Z., Jiang H., Ou Z.-L., Chen J.-S., Chi C.-W.
Toxicon 42:613-619(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Venom duct.
[3]"The A-superfamily of conotoxins: structural and functional divergence."
Santos A.D., McIntosh J.M., Hillyard D.R., Cruz L.J., Olivera B.M.
J. Biol. Chem. 279:17596-17606(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Venom duct.
[4]"Novel alpha- and omega-conotoxins from Conus striatus venom."
Ramilo C., Zafaralla G.C., Nadasdi L., Hammerland L.G., Yoshikami D., Gray W.R., Kristipati R., Ramachandran J., Miljanich G.P., Olivera B.M., Cruz L.J.
Biochemistry 31:9919-9926(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 51-69, SYNTHESIS OF 51-69.
Tissue: Venom.
[5]"Optimizing the connectivity in disulfide-rich peptides: alpha-conotoxin SII as a case study."
Bingham J.-P., Broxton N.M., Livett B.G., Down J.G., Jones A., Moczydlowski E.G.
Anal. Biochem. 338:48-61(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS, SYNTHESIS OF 51-69, MASS SPECTROMETRY, FUNCTION.
Tissue: Venom.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY157497 mRNA. Translation: AAN77902.1.
PIRA44379.

3D structure databases

ProteinModelPortalP28879.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

ConoServer3900. SII precursor.
9. SII precursor.
91. SII precursor.

Family and domain databases

InterProIPR009958. Conotoxin_a-typ.
IPR018072. Conotoxin_a-typ_CS.
[Graphical view]
PfamPF07365. Toxin_8. 1 hit.
[Graphical view]
PROSITEPS60014. ALPHA_CONOTOXIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCAS2_CONST
AccessionPrimary (citable) accession number: P28879
Secondary accession number(s): Q8I6R6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: September 5, 2006
Last modified: May 1, 2013
This is version 69 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families