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Literature summary for 1.21.1.1 extracted from

  • de la Cruz, I.P.; Ma, L.; Horvitz, H.R.
    The Caenorhabditis elegans iodotyrosine deiodinase ortholog SUP-18 functions through a conserved channel SC-box to regulate the muscle two-pore domain potassium channel SUP-9 (2014), PLoS Genet., 10, e1004175.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.21.1.1

Activating Compound

Activating Compound Comment Organism Structure
additional information an evolutionarily conserved serine-cysteine-rich region in the C-terminal cytoplasmic domain of SUP-9 is required for its specific activation by SUP-18 Caenorhabditis elegans

Cloned(Commentary)

Cloned (Comment) Organism
gene sup-18, genotyping, encodes the Caenorhabditis elegans orthologue of mammalian iodotyrosine deiodinase (IYD) Caenorhabditis elegans

Protein Variants

Protein Variants Comment Organism
G258D a naturally occuring sup-18 loss-of-function mutation Caenorhabditis elegans
G258S a naturally occuring sup-18 loss-of-function mutation Caenorhabditis elegans
G280R a naturally occuring sup-18 loss-of-function mutation Caenorhabditis elegans
additional information naturally occuring sup-18 loss-of-function mutations, e.g. splice-junction mutants and spontaneaous mutations, overview Caenorhabditis elegans
R289K a naturally occuring sup-18 loss-of-function mutation Caenorhabditis elegans
S137N a naturally occuring sup-18 loss-of-function mutation Caenorhabditis elegans
T271I a naturally occuring sup-18 loss-of-function mutation Caenorhabditis elegans
T322P a naturally occuring sup-18 loss-of-function mutation Caenorhabditis elegans

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane enzyme SUP-18 is a type-I transmembrane protein that can function independently of membrane anchoring Caenorhabditis elegans 16020
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Organism

Organism UniProt Comment Textmining
Caenorhabditis elegans Q17374 gene sup-18
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Source Tissue

Source Tissue Comment Organism Textmining
body wall muscle
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 Caenorhabditis elegans
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Synonyms

Synonyms Comment Organism
NADH oxidase/flavin reductase
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 Caenorhabditis elegans
SUP-18
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 Caenorhabditis elegans
SUP-18 IYD
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 Caenorhabditis elegans

Cofactor

Cofactor Comment Organism Structure
FMN the FMN-binding site of mammalian IYD is conserved in SUP-18, FMN appears to require catalytic activity to function Caenorhabditis elegans
NADH
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 Caenorhabditis elegans

General Information

General Information Comment Organism
malfunction increased sup-18(+) expression in body-wall muscles specifically enhances the behavioral defects of sup-10(n983gf) mutants Caenorhabditis elegans
metabolism genetic analyses suggest that SUP-10 can function with SUP-18 to activate SUP-9 through a pathway that is independent of the presumptive SUP-9 regulatory subunit UNC-93. The SUP-9 two-pore domain K+ channel is most closely related to human TASK-3. unc-93 encodes a conserved multi-pass transmembrane protein. An evolutionarily conserved serine-cysteine-rich region in the C-terminal cytoplasmic domain of SUP-9 is required for its specific activation by SUP-10 and SUP-18 but not by UNC-93 Caenorhabditis elegans
physiological function the NADH oxidase/flavin reductase, an orthologue of mammalian iodotyrosine deiodinase (IYD), functions in iodine recycling and is important for the biosynthesis of thyroid hormones that regulate metabolism. The enzyme SUP-18 is a type-I transmembrane protein with an NADH oxidase/flavin reductase domain that resides intracellularly and can function without plasma membrane localization. The enzyme regulates the activity of the muscle two-pore domain potassium SUP-9 channel using NADH as a coenzyme and thus couples the metabolic state of muscle cells to muscle membrane excitability Caenorhabditis elegans