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Protein

Rho-conotoxin TIA

Gene
N/A
Organism
Conus tulipa (Fish-hunting cone snail) (Tulip cone)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Allosteric inhibitor of alpha-1B adrenergic receptors (ADRA1B). Binds to an allosteric modulatory site on transmembrane helix 6 and 7 at the base of extracellular loop 3 of ADRA1B (PubMed:23184947). Also weekly inhibits alpha-1A (ADRA1A) and alpha-1D (ADRA1D) adrenergic receptors in a competive manner (PubMed:15194691). Potently inhibits contractions of vas deferens, spleen and aorta in response to noradrenaline (PubMed:15680270).5 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor impairing toxin, Toxin

Names & Taxonomyi

Protein namesi
Recommended name:
Rho-conotoxin TIA
Short name:
Rho-TIA
OrganismiConus tulipa (Fish-hunting cone snail) (Tulip cone)
Taxonomic identifieri6495 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaCaenogastropodaHypsogastropodaNeogastropodaConoideaConidaeConus

Organism-specific databases

ConoServeri1634. TIA.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Pharmaceutical usei

Is under preclinical trial by Xenome.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi40 – 401N → A: Little loss in inhibition. 1 Publication
Mutagenesisi41 – 411W → A: Important loss in inhibition. 1 Publication
Mutagenesisi42 – 421R → A: Most important loss in inhibition. 1 Publication
Mutagenesisi45 – 451L → A: Little loss in inhibition. 1 Publication
Mutagenesisi46 – 461I → A: Important loss in inhibition, and change from non-competitive to competitive antagonist of alpha-1B receptor subtype. 2 Publications
Mutagenesisi50 – 501R → A: Little loss in inhibition. 1 Publication
Mutagenesisi56 – 561F → A or N: Selectivity increase for alpha-1B subtype. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Sequence analysisAdd
BLAST
Propeptidei17 – 38221 PublicationPRO_0000404204Add
BLAST
Peptidei39 – 5719Rho-conotoxin TIAPRO_0000044510Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi43 ↔ 49
Disulfide bondi44 ↔ 57
Modified residuei57 – 571Cysteine amide1 Publication

Keywords - PTMi

Amidation, Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom duct.

Structurei

Secondary structure

1
58
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi42 – 454Combined sources
Helixi47 – 504Combined sources
Helixi54 – 563Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IENNMR-A39-57[»]
2LR9NMR-A39-57[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP58811.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni40 – 423Interacts with ADRA1B

Domaini

The cysteine framework is I (CC-C-C). Alpha4/7 pattern.

Sequence similaritiesi

Belongs to the conotoxin A superfamily.Curated

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR009958. Conotoxin_a-typ.
[Graphical view]
PfamiPF07365. Toxin_8. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P58811-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFTVFLLVVL ATTGVSFTLD RASDGGNAVA KKSDVTARFN WRCCLIPACR

RNHKKFCG
Length:58
Mass (Da):6,395
Last modified:February 8, 2011 - v2
Checksum:iEAA3234432D865A6
GO

Sequence cautioni

The sequence ADN79119 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Mass spectrometryi

Molecular mass is 2390.15 Da from positions 1 - 19. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GQ981400 mRNA. Translation: ADN79119.1. Different initiation.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GQ981400 mRNA. Translation: ADN79119.1. Different initiation.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IENNMR-A39-57[»]
2LR9NMR-A39-57[»]
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

ConoServeri1634. TIA.

Miscellaneous databases

EvolutionaryTraceiP58811.

Family and domain databases

InterProiIPR009958. Conotoxin_a-typ.
[Graphical view]
PfamiPF07365. Toxin_8. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCA1A_CONTU
AccessioniPrimary (citable) accession number: P58811
Secondary accession number(s): E2DEK8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: February 8, 2011
Last modified: January 7, 2015
This is version 58 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Miscellaneous

Has no effect on alpha-2 adrenergic receptors (ADRA2) (PubMed:11528421, PubMed:12824165).2 Publications

Keywords - Technical termi

3D-structure, Direct protein sequencing, Pharmaceutical

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.