ADP-ribose glycohydrolase OARD1 (OARD1)
The protein contains 152 amino acids for an estimated molecular weight of 17025 Da.
ADP-ribose glycohydrolase that hydrolyzes ADP-ribose and acts on different substrates, such as proteins ADP-ribosylated on glutamate and O-acetyl-ADP-D-ribose (PubMed:23481255, PubMed:23474714, PubMed:21849506). Specifically acts as a glutamate mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to glutamate residues on proteins (PubMed:23481255, PubMed:23474714). Does not act on poly-ADP-ribosylated proteins: the poly-ADP-ribose chain of poly-ADP-ribosylated glutamate residues must by hydrolyzed into mono-ADP-ribosylated glutamate by PARG to become a substrate for OARD1 (PubMed:23481255). Deacetylates O-acetyl-ADP ribose, a signaling molecule generated by the deacetylation of acetylated lysine residues in histones and other proteins (PubMed:21849506). Catalyzes the deacylation of O-acetyl-ADP-ribose, O-propionyl-ADP-ribose and O-butyryl-ADP-ribose, yielding ADP-ribose plus acetate, propionate and butyrate, respectively (PubMed:21849506). (updated: Jan. 16, 2019)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
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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The reference OMIM entry for this protein is 614393
Chromosome 6 open reading frame 130; c6orf130
O-acyl-adp-ribose deacylase
DESCRIPTION
O-acyl-ADP-ribose is produced by NAD(+)-dependent deacylation of acyl-modified lysines and can function as a cell signaling molecule. C6ORF130 is a deacylase that converts O-acetyl-ADP-ribose, O-propionyl-ADP-ribose, and O-butyryl-ADP-ribose to ADP-ribose and acetate, propionate, and butyrate, respectively (Peterson et al., 2011).CLONING
Peterson et al. (2011) found that the deduced 152-amino acid C6ORF130 protein is made up almost entirely of a globular macrodomain. The C6ORF130 macrodomain shares limited homology with the approximately 140-amino acid macrodomains of MACROD1 (610400) and MACROD2 (611567), but C6ORF130 lacks the extended N- and C-terminal sequences of these proteins.GENE FUNCTION
Peterson et al. (2011) found that recombinant C6ORF130 efficiently deacylated O-acyl-ADP-ribose, O-propionyl-ADP-ribose, and O-butyryl-ADP-ribose to produce ADP-ribose and acetate, propionate, and butyrate, respectively. C6ORF130 showed slight preference for substrates with shorter acyl chain lengths. Peterson et al. (2011) also showed that ADP-ribose functioned as a competitive feedback inhibitor. Site-directed mutagenesis experiments revealed critical roles for ser35 and asp125 of C6ORF130 in catalysis.BIOCHEMICAL FEATURES
Using nuclear magnetic resonance spectroscopy, Peterson et al. (2011) found that the macrodomain of C6ORF130 exhibited the canonical 3-layered alpha-beta-alpha sandwich, with a central 6-stranded beta-sheet containing a mixture of anti-parallel and parallel strands and a deep ligand-binding cleft. ADP-ribose bound deep within the macrodomain cleft, with the diphosphate ribose portion completely buried. A beta-alpha loop covered the bound ADP-ribose and appeared to function as a gate to sequester the substrate and offer flexibility to accommodate alternative substrates.MAPPING
Hartz (2011) mapped the C6ORF130 gene to chromosome 6p21.1 based on an alignment of the C6ORF130 sequence (GenBank GENBANK AJ420538) with the genomic sequence (GRCh37). ... More on the omim web site
Jan. 21, 2019: Protein entry updated
Automatic update: Entry updated from uniprot information.
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 614393 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed