Mitochondrial amidoxime reducing component 2 (MARC2)
The protein contains 335 amino acids for an estimated molecular weight of 38023 Da.
Catalyzes the reduction of N-oxygenated molecules, acting as a counterpart of cytochrome P450 and flavin-containing monooxygenases in metabolic cycles (PubMed:21029045, PubMed:24423752). As a component of prodrug-converting system, reduces a multitude of N-hydroxylated prodrugs particularly amidoximes, leading to increased drug bioavailability (PubMed:21029045, PubMed:24423752). May be involved in mitochondrial N(omega)-hydroxy-L-arginine (NOHA) reduction, regulating endogenous nitric oxide levels and biosynthesis (PubMed:21029045). Postulated to cleave the N-OH bond of N-hydroxylated substrates in concert with electron transfer from NADH to cytochrome b5 reductase then to cytochrome b5, the ultimate electron donor that primes the active site for substrate reduction (PubMed:21029045). (updated: Nov. 13, 2019)
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.
This protein is predicted to be membranous by TOPCONS.
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No binding partner found
The reference OMIM entry for this protein is 614127
Molybdenum cofactor sulfurase c-terminal domain-containing protein 2; mosc2
Moco sulfurase c-terminal domain-containing protein 2
Mosc domain-containing protein 2
Mitochondrial amidoxime-reducing component 2; marc2
DESCRIPTION
Nitric oxide synthases (see 163731) catalyze the oxidation of L-arginine to L-citrulline and nitric oxide via the intermediate N(omega)-hydroxy-L-arginine (NOHA). This intermediate can be converted further, or it can be reduced to L-arginine by the molybdenum cofactor (Moco)-containing enzymes MOSC1 (614126) and MOSC2. MOSC enzymes can also reduce and detoxify xenobiotic compounds (Kotthaus et al., 2011).CLONING
By RT-PCR of human HepG2 RNA, Kotthaus et al. (2011) cloned MOSC2. The deduced 335-amino acid protein has an N-terminal mitochondrial localization signal.GENE FUNCTION
Kotthaus et al. (2011) showed that recombinant human MARC1 and MARC2 bound Moco and reduced the physiologic substrate NOHA in the presence of cytochrome b5 and NADH cytochrome b5 reductase. Kinetic analysis revealed that MARC2 had higher affinity and reaction velocity than MARC1 in the reduction of NOHA. Both enzymes also reduced the potent nonphysiologic arginase inhibitor N(omega)-hydroxy-N(delta)-methyl-L-arginine. Kotthaus et al. (2011) concluded that MARC1 and MARC2 may be involved in mitochondrial NOHA reduction and detoxification of xenobiotics.MAPPING
Hartz (2011) mapped the MOSC2 gene to chromosome 1q41 based on an alignment of the MOSC1 sequence (GenBank GENBANK AK000612) with the genomic sequence (GRCh37). ... More on the omim web site
Dec. 2, 2019: Protein entry updated
Automatic update: Entry updated from uniprot information.
Oct. 20, 2018: Protein entry updated
Automatic update: OMIM entry 614127 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).