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Protein

Kappa-conotoxin-like MIVA

Gene
N/A
Organism
Conus magus (Magus cone) (Magician's cone snail)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Kappa-conotoxins bind and inhibit voltage-gated potassium channels (By similarity). This highly potent excitatory peptide elicits repetitive action potentials and causes the same spastic symptomatology as kappa-conotoxin SIVA.By similarity

GO - Molecular functioni

Keywordsi

Molecular functionIon channel impairing toxin, Neurotoxin, Potassium channel impairing toxin, Toxin

Names & Taxonomyi

Protein namesi
Recommended name:
Kappa-conotoxin-like MIVA
OrganismiConus magus (Magus cone) (Magician's cone snail)
Taxonomic identifieri6492 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaCaenogastropodaNeogastropodaConoideaConidaeConusPionoconus

Organism-specific databases

ConoServeri18 MIVA precursor

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Sequence analysisAdd BLAST21
PropeptideiPRO_000024980022 – 381 PublicationAdd BLAST17
PeptideiPRO_000024980139 – 74Kappa-conotoxin-like MIVAAdd BLAST36
PropeptideiPRO_000024980275 – 795

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei404-hydroxyproline1 Publication1
Modified residuei414-carboxyglutamate1 Publication1
Glycosylationi45O-linked (HexNAc...) threonineCurated1
Glycosylationi47O-linked (HexNAc...) threonineCurated1
Modified residuei554-hydroxyproline1 Publication1
Modified residuei604-hydroxyproline1 Publication1
Modified residuei614-hydroxyproline1 Publication1
Modified residuei694-hydroxyproline1 Publication1
Modified residuei704-hydroxyproline1 Publication1
Modified residuei744-hydroxyproline1 Publication1
Modified residuei74Proline amide1 Publication1

Post-translational modificationi

Contains 3 disulfide bonds (By similarity). They are not added, since framework IV presents two different connectivities (I-V, II-III, IV-VI and I-III, II-V, IV-VI).By similarity

Keywords - PTMi

Amidation, Disulfide bond, Gamma-carboxyglutamic acid, Glycoprotein, Hydroxylation

Proteomic databases

PRIDEiP0C1X1

Expressioni

Tissue specificityi

Expressed by the venom duct.

Structurei

3D structure databases

ProteinModelPortaliP0C1X1
SMRiP0C1X1
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The cysteine framework is IV (CC-C-C-C-C).

Sequence similaritiesi

Belongs to the conotoxin A superfamily.Curated

Keywords - Domaini

Signal

Family and domain databases

InterProiView protein in InterPro
IPR009958 Conotoxin_a-typ
PfamiView protein in Pfam
PF07365 Toxin_8, 1 hit

Sequencei

Sequence statusi: Complete.

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

P0C1X1-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGMRMMFTVF LLVVLATTVV SIPSDRASDG RNAVVHERAP ELVVTATTNC
60 70
CGYNPMTICP PCMCTYSCPP KRKPGRRND
Length:79
Mass (Da):8,680
Last modified:September 19, 2006 - v1
Checksum:i46AC083059DF97CA
GO

Mass spectrometryi

Molecular mass is 5095.3 Da from positions 39 - 74. Determined by LSI. 1 Publication

Similar proteinsi

Entry informationi

Entry nameiCA4A_CONMA
AccessioniPrimary (citable) accession number: P0C1X1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 19, 2006
Last sequence update: September 19, 2006
Last modified: September 12, 2018
This is version 36 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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