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P22947 (TXCAS_DENPO) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 64. 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:
Calciseptin
Alternative name(s):
Calciseptine
Short name=CaS
L-type calcium channel blocker
OrganismDendroaspis polylepis polylepis (Black mamba)
Taxonomic identifier8620 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeElapinaeDendroaspis

Protein attributes

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

General annotation (Comments)

Function

This specific blocker of the L-type calcium channel (Cav1/CACNA1) is a smooth muscle relaxant and an inhibitor of cardiac contractions. Ref.3

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Miscellaneous

The sensitivity is higher in cells of the cardiovascular system. Neuronal, and insulinoma cells L-type calcium channel are more resistant. A total resistance is found in skeletal muscle cells.

Sequence similarities

Belongs to the snake three-finger toxin family. L-type calcium blocker subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 6060Calciseptin
PRO_0000093667

Amino acid modifications

Disulfide bond3 ↔ 22 By similarity
Disulfide bond17 ↔ 39 By similarity
Disulfide bond41 ↔ 52 By similarity
Disulfide bond53 ↔ 58 By similarity

Sequences

Sequence LengthMass (Da)Tools
P22947 [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: 2F14B05972A40FFF

FASTA607,044
        10         20         30         40         50         60 
RICYIHKASL PRATKTCVEN TCYKMFIRTQ REYISERGCG CPTAMWPYQT ECCKGDRCNK 

« Hide

References

[1]"Calciseptine, a peptide isolated from black mamba venom, is a specific blocker of the L-type calcium channel."
de Weille J.R., Schweitz H., Maes P., Tartar A., Lazdunski M.
Proc. Natl. Acad. Sci. U.S.A. 88:2437-2440(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Venom.
[2]"Solution synthesis of calciseptine, an L-type specific calcium channel blocker."
Kuroda H., Chen Y.-N., Watanabe T.X., Kimura T., Sakakibara S.
Pept. Res. 5:265-268(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: SYNTHESIS.
[3]"Flanking proline residues identify the L-type Ca2+ channel binding site of calciseptine and FS2."
Kini R.M., Caldwell R.A., Wu Q.Y., Baumgarten C.M., Feher J.J., Evans H.J.
Biochemistry 37:9058-9063(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SYNTHESIS OF 41-48.

Cross-references

Sequence databases

PIRA39165.

3D structure databases

ProteinModelPortalP22947.
SMRP22947. Positions 1-60.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG006553.

Family and domain databases

InterProIPR003571. Snake_toxin.
IPR018354. Snake_toxin_BS.
[Graphical view]
PfamPF00087. Toxin_1. 1 hit.
[Graphical view]
PROSITEPS00272. SNAKE_TOXIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTXCAS_DENPO
AccessionPrimary (citable) accession number: P22947
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: October 16, 2013
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families