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P80163

- SRTXB_ATRBI

UniProt

P80163 - SRTXB_ATRBI

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Protein

Bibrotoxin

Gene
N/A
Organism
Atractaspis bibronii (Bibron's mole viper) (Southern stiletto snake)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli

Functioni

Vasoconstrictor activity. These toxins cause cardiac arrest probably as a result of coronary vasospasm. May act by displaying agonistic activities towards endothelin-1 and -2 receptors (EDNRA and EDNRB).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei21 – 211Endothelin-receptor binding siteBy similarity

GO - Biological processi

  1. regulation of vasoconstriction Source: InterPro
  2. vasoconstriction Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Cardiotoxin, G-protein coupled receptor impairing toxin, Toxin, Vasoactive, Vasoconstrictor

Names & Taxonomyi

Protein namesi
Recommended name:
Bibrotoxin
Short name:
BTX
OrganismiAtractaspis bibronii (Bibron's mole viper) (Southern stiletto snake)
Taxonomic identifieri61304 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaLamprophiidaeAtractaspidinaeAtractaspis

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
Peptidei1 – 2121BibrotoxinPRO_0000043645Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi1 ↔ 15By similarity
Disulfide bondi3 ↔ 11By similarity

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.

Family & Domainsi

Sequence similaritiesi

Belongs to the endothelin/sarafotoxin family.Curated

Family and domain databases

InterProiIPR019764. Endothelin_toxin_CS.
IPR001928. Endothln-like_toxin.
[Graphical view]
PfamiPF00322. Endothelin. 1 hit.
[Graphical view]
SMARTiSM00272. END. 1 hit.
[Graphical view]
PROSITEiPS00270. ENDOTHELIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P80163-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20 
CSCADMTDKE CLYFCHQDVI W
Length:21
Mass (Da):2,511
Last modified:April 1, 1993 - v1
Checksum:i83A5DFB81D036AE2
GO

Sequence databases

PIRiS27039.

Cross-referencesi

Sequence databases

PIRi S27039.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

InterProi IPR019764. Endothelin_toxin_CS.
IPR001928. Endothln-like_toxin.
[Graphical view ]
Pfami PF00322. Endothelin. 1 hit.
[Graphical view ]
SMARTi SM00272. END. 1 hit.
[Graphical view ]
PROSITEi PS00270. ENDOTHELIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Bibrotoxin, a novel member of the endothelin/sarafotoxin peptide family, from the venom of the burrowing asp Atractaspis bibroni."
    Becker A., Dowdle E.B., Hechler U., Kauser K., Donner P., Schleuning W.-D.
    FEBS Lett. 315:100-103(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, FUNCTION.
    Tissue: Venom.

Entry informationi

Entry nameiSRTXB_ATRBI
AccessioniPrimary (citable) accession number: P80163
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: October 29, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3