Nardilysin (NRDC)
The protein contains 1151 amino acids for an estimated molecular weight of 131701 Da.
Cleaves peptide substrates on the N-terminus of arginine residues in dibasic pairs. (updated: Oct. 10, 2018)
Protein identification was indicated in the following studies:
- 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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| Variant | Description |
|---|---|
| dbSNP:rs34957144 |
Biological Process
Cell migration
Cell population proliferation
Negative regulation of cold-induced thermogenesis
Neuromuscular junction development
Peptide catabolic process
Positive regulation of membrane protein ectodomain proteolysis
Proteolysis
Proteolysis involved in cellular protein catabolic process
Regulation of endopeptidase activity
The reference OMIM entry for this protein is 602651
Nardilysin; nrd1
N-arginine dibasic convertase; nrd convertase
CLONING
Endoproteases that activate protein precursors by cleavage at basic residues belong to the 4 classes of proteases: aspartyl, serine, thiol, and metalloenzymes. Pierotti et al. (1994) noted that nardilysin (NRD1; EC 3.4.24.61), a metalloendopeptidase that cleaves peptide substrates at the N terminus of arginine residues in dibasic moieties, had previously been purified from rat testis. By screening a rat testis cDNA library with oligonucleotides based on the sequence of the purified Nrd1 protein, Pierotti et al. (1994) cloned a cDNA encoding Nrd1, called N-arginine dibasic (Nrd) convertase by them. The predicted 1,161-amino acid Nrd1 protein has a calculated molecular mass of 133 kD, consistent with the mass of the largest form of the purified enzyme. Nrd1 contains a putative signal peptide, a 71-residue acidic stretch, and a zinc-binding motif. The amino acid sequence of rat Nrd1 is 31% identical to that of human insulinase (IDE; 146680). Hospital et al. (1997) cloned cDNAs encoding NRD convertase by screening a human testis cDNA library with a rat Nrd convertase cDNA. They found that NRD convertase is expressed in both human and rat as 2 distinct mRNAs that differ by the presence or absence of a 204-nucleotide in-frame insertion. This insertion adds 68 amino acids between the acidic stretch and the zinc-binding motif. The longer, 3.9-kb human mRNA and the shorter, 3.7-kb human mRNA encode predicted 1,219-amino acid and 1,151-amino acid proteins, respectively. The human NRD convertase proteins are 92% identical to the rat Nrd convertases. Northern blot analysis of rat RNAs showed that Nrd convertase is expressed abundantly in testis and at lower levels in most other tissues. Fumagalli et al. (1998) cloned a human NRD convertase cDNA encoding a predicted 1,147-amino acid protein. By Northern blot analysis of human RNAs, they found that NRD convertase is expressed as a 3.6-kb transcript primarily in adult heart, skeletal muscle, and testis and at much lower levels in other tissues. During early mouse development, Nrd convertase is expressed almost exclusively in neural tissues.MAPPING
By fluorescence in situ hybridization, Hospital et al. (1997) mapped the human NRD convertase gene to 1p32.2-p32.1, and Fumagalli et al. (1998) refined the localization to 1p32.2. ... More on the omim web site
Oct. 20, 2018: Protein entry updated
Automatic update: OMIM entry 602651 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).