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Protein

Omega-conotoxin SVIA

Gene
N/A
Organism
Conus striatus (Striated cone)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Omega-conotoxins act at presynaptic membranes, they bind and block voltage-gated calcium channels (Cav).

GO - Molecular functioni

  1. ion channel inhibitor activity Source: InterPro

GO - Biological processi

  1. pathogenesis Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

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

Names & Taxonomyi

Protein namesi
Recommended name:
Omega-conotoxin SVIA
Alternative name(s):
SNX-157
OrganismiConus striatus (Striated cone)
Taxonomic identifieri6493 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaCaenogastropodaHypsogastropodaNeogastropodaConoideaConidaeConus

Organism-specific databases

ConoServeri863. SVIA precursor.

Subcellular locationi

GO - Cellular componenti

  1. other organism presynaptic membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Propeptidei23 – 48261 PublicationPRO_0000034924Add
BLAST
Peptidei49 – 7224Omega-conotoxin SVIAPRO_0000034925Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi49 ↔ 63
Modified residuei55 – 5514-hydroxyproline1 Publication
Disulfide bondi56 ↔ 66
Disulfide bondi62 ↔ 71
Modified residuei72 – 721Threonine amide1 Publication

Keywords - PTMi

Amidation, Disulfide bond, Hydroxylation

Expressioni

Tissue specificityi

Expressed by the venom duct.

Family & Domainsi

Domaini

The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
The cysteine framework is VI/VII (C-C-CC-C-C).

Sequence similaritiesi

Belongs to the conotoxin O1 superfamily.Curated

Keywords - Domaini

Knottin, Signal

Family and domain databases

InterProiIPR004214. Conotoxin.
IPR012321. Conotoxin_omega-typ_CS.
[Graphical view]
PfamiPF02950. Conotoxin. 1 hit.
[Graphical view]
PROSITEiPS60004. OMEGA_CONOTOXIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P28880-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKLTCVMIVA VLLLTACQLI TAEDSRGTQK HRTLRSTARR SKSESTTRCR
60 70
SSGSPCGVTS ICCGRCYRGK CT
Length:72
Mass (Da):7,830
Last modified:August 29, 2001 - v2
Checksum:i4A6A412E450469A1
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti51 – 511S → P in SVIA-1, SVIA-2 and SVIA-5. 1 Publication
Natural varianti54 – 541S → P in SVIA-4. 1 Publication
Natural varianti55 – 551P → S in SVIA-3. 1 Publication
Natural varianti59 – 591T → A in SVIA-5. 1 Publication
Natural varianti67 – 671Y → S in SVIA-2 and SVIA-5. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF146347 mRNA. Translation: AAD31907.1.
PIRiB44379.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF146347 mRNA. Translation: AAD31907.1.
PIRiB44379.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

ConoServeri863. SVIA precursor.

Family and domain databases

InterProiIPR004214. Conotoxin.
IPR012321. Conotoxin_omega-typ_CS.
[Graphical view]
PfamiPF02950. Conotoxin. 1 hit.
[Graphical view]
PROSITEiPS60004. OMEGA_CONOTOXIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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. Cited for: PROTEIN SEQUENCE OF 49-72, SYNTHESIS OF 49-72, HYDROXYLATION AT PRO-55, AMIDATION AT THR-72.
    Tissue: Venom.
  3. "Analysis of expressed sequence tags from the venom ducts of Conus striatus: focusing on the expression profile of conotoxins."
    Pi C., Liu Y., Peng C., Jiang X., Liu J., Xu B., Yu X., Yu Y., Jiang X., Wang L., Dong M., Chen S., Xu A.-L.
    Biochimie 88:131-140(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 49-72, VARIANTS PRO-51; PRO-54; SER-55; ALA-59 AND SER-67.
    Tissue: Venom duct.

Entry informationi

Entry nameiCO16A_CONST
AccessioniPrimary (citable) accession number: P28880
Secondary accession number(s): Q9UB26
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: August 29, 2001
Last modified: October 1, 2014
This is version 72 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Caution

Thr-72 is not followed in the nucleotide sequence by the expected Gly residue required to produce amidation.Curated

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.