Literature summary 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.
Activating Compound
EC Number |
Activating Compound |
Comment |
Organism |
Structure |
---|
1.21.1.1 |
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)
EC Number |
Cloned (Comment) |
Organism |
---|
1.21.1.1 |
gene sup-18, genotyping, encodes the Caenorhabditis elegans orthologue of mammalian iodotyrosine deiodinase (IYD) |
Caenorhabditis elegans |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
1.21.1.1 |
G258D |
a naturally occuring sup-18 loss-of-function mutation |
Caenorhabditis elegans |
1.21.1.1 |
G258S |
a naturally occuring sup-18 loss-of-function mutation |
Caenorhabditis elegans |
1.21.1.1 |
G280R |
a naturally occuring sup-18 loss-of-function mutation |
Caenorhabditis elegans |
1.21.1.1 |
additional information |
naturally occuring sup-18 loss-of-function mutations, e.g. splice-junction mutants and spontaneaous mutations, overview |
Caenorhabditis elegans |
1.21.1.1 |
R289K |
a naturally occuring sup-18 loss-of-function mutation |
Caenorhabditis elegans |
1.21.1.1 |
S137N |
a naturally occuring sup-18 loss-of-function mutation |
Caenorhabditis elegans |
1.21.1.1 |
T271I |
a naturally occuring sup-18 loss-of-function mutation |
Caenorhabditis elegans |
1.21.1.1 |
T322P |
a naturally occuring sup-18 loss-of-function mutation |
Caenorhabditis elegans |
Localization
EC Number |
Localization |
Comment |
Organism |
GeneOntology No. |
Textmining |
---|
1.21.1.1 |
membrane |
enzyme SUP-18 is a type-I transmembrane protein that can function independently of membrane anchoring |
Caenorhabditis elegans |
16020 |
- |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.21.1.1 |
Caenorhabditis elegans |
Q17374 |
gene sup-18 |
- |
Source Tissue
EC Number |
Source Tissue |
Comment |
Organism |
Textmining |
---|
1.21.1.1 |
body wall muscle |
- |
Caenorhabditis elegans |
- |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
1.21.1.1 |
NADH oxidase/flavin reductase |
- |
Caenorhabditis elegans |
1.21.1.1 |
SUP-18 |
- |
Caenorhabditis elegans |
1.21.1.1 |
SUP-18 IYD |
- |
Caenorhabditis elegans |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
1.21.1.1 |
FMN |
the FMN-binding site of mammalian IYD is conserved in SUP-18, FMN appears to require catalytic activity to function |
Caenorhabditis elegans |
|
1.21.1.1 |
NADH |
- |
Caenorhabditis elegans |
|
General Information
EC Number |
General Information |
Comment |
Organism |
---|
1.21.1.1 |
malfunction |
increased sup-18(+) expression in body-wall muscles specifically enhances the behavioral defects of sup-10(n983gf) mutants |
Caenorhabditis elegans |
1.21.1.1 |
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 |
1.21.1.1 |
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 |