Cysteine dioxygenase type 1 (CDO1)
The protein contains 200 amino acids for an estimated molecular weight of 22972 Da.
Initiates several important metabolic pathways related to pyruvate and several sulfurate compounds including sulfate, hypotaurine and taurine. Critical regulator of cellular cysteine concentrations. Has an important role in maintaining the hepatic concentation of intracellular free cysteine within a proper narrow range. (updated: Sept. 12, 2018)
Protein identification was indicated in the following studies:
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
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| Variant | Description |
|---|---|
| dbSNP:rs1042867 | |
| a colorectal cancer sample; somatic mutation |
No binding partner found
Biological Process
Cysteine metabolic process
Inflammatory response
L-cysteine catabolic process
Lactation
Oxidation-reduction process
Response to amino acid
Response to cAMP
Response to ethanol
Response to glucagon
Response to glucocorticoid
Sulfur amino acid biosynthetic process
Taurine biosynthetic process
The reference OMIM entry for this protein is 603943
Cysteine dioxygenase; cdo
Cysteine dioxygenase, type i; cdo1
L-cysteine: oxygen oxidoreductase
CLONING
The first step in the oxidation of cysteine to inorganic sulfate is its conversion to cysteine sulfinate by cysteine dioxygenase (CDO; EC 1.13.11.20). In rat, at least 2 enzymes catalyze this reaction, one cytosolic (CDO-I) and the other membrane-bound. Rat liver CDO contains 1 atom of iron per molecule of protein, and the enzyme is activated by anaerobic incubation with either L-cysteine or its analogs. Hosokawa et al. (1990) isolated rat liver cDNAs encoding the cytosolic CDO. By screening a human liver library with a rat CDO-I cDNA, McCann et al. (1994) identified human CDO-I cDNAs. The predicted 200-amino acid human and rat proteins are 94% identical. Northern blot analysis revealed that CDO-I is expressed as an approximately 1.5-kb mRNA in liver.GENE STRUCTURE
Ramsden et al. (1997) reported that the human CDO-I gene contains 5 exons and spans more than 12 kb.MAPPING
By analysis of somatic cell hybrids and by fluorescence in situ hybridization, Jeremiah et al. (1996) mapped the CDO1 gene to human chromosome 5q22-q23. Using an interspecific backcross, these authors mapped the mouse homolog to the central region of mouse chromosome 18, in a region sharing homology of synteny with human chromosome 5. ... More on the omim web site
June 30, 2020: Protein entry updated
Automatic update: OMIM entry 603943 was added.
Feb. 23, 2019: Protein entry updated
Automatic update: comparative model was added.
Feb. 23, 2019: Protein entry updated
Automatic update: model status changed
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).