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P22947

- TXCAS_DENPO

UniProt

P22947 - TXCAS_DENPO

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Protein

Calciseptin

Gene
N/A
Organism
Dendroaspis polylepis polylepis (Black mamba)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli

Functioni

This specific blocker of the L-type calcium channel (Cav1/CACNA1) is a smooth muscle relaxant and an inhibitor of cardiac contractions.1 Publication

GO - Biological processi

  1. modification of morphology or physiology of other organism Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Calcium channel impairing toxin, Cardiotoxin, Ion channel impairing toxin, Neurotoxin, Toxin, Voltage-gated calcium channel impairing toxin

Names & Taxonomyi

Protein namesi
Recommended name:
Calciseptin
Alternative name(s):
Calciseptine
Short name:
CaS
L-type calcium channel blocker
OrganismiDendroaspis polylepis polylepis (Black mamba)
Taxonomic identifieri8620 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeElapinaeDendroaspis

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 6060CalciseptinPRO_0000093667Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi3 ↔ 22By similarity
Disulfide bondi17 ↔ 39By similarity
Disulfide bondi41 ↔ 52By similarity
Disulfide bondi53 ↔ 58By similarity

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.

Structurei

3D structure databases

ProteinModelPortaliP22947.
SMRiP22947. Positions 1-60.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG006553.

Family and domain databases

InterProiIPR003571. Snake_toxin.
IPR018354. Snake_toxin_BS.
[Graphical view]
PfamiPF00087. Toxin_1. 1 hit.
[Graphical view]
PROSITEiPS00272. SNAKE_TOXIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P22947-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
RICYIHKASL PRATKTCVEN TCYKMFIRTQ REYISERGCG CPTAMWPYQT
60
ECCKGDRCNK
Length:60
Mass (Da):7,044
Last modified:August 1, 1991 - v1
Checksum:i2F14B05972A40FFF
GO

Sequence databases

PIRiA39165.

Cross-referencesi

Sequence databases

PIRi A39165.

3D structure databases

ProteinModelPortali P22947.
SMRi P22947. Positions 1-60.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG006553.

Family and domain databases

InterProi IPR003571. Snake_toxin.
IPR018354. Snake_toxin_BS.
[Graphical view ]
Pfami PF00087. Toxin_1. 1 hit.
[Graphical view ]
PROSITEi PS00272. SNAKE_TOXIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiTXCAS_DENPO
AccessioniPrimary (citable) accession number: P22947
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: October 29, 2014
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3