Ribonuclease inhibitor (RNH1)
The protein contains 461 amino acids for an estimated molecular weight of 49973 Da.
Ribonuclease inhibitor which inhibits RNASE1, RNASE2 and ANG. May play a role in redox homeostasis. (updated: March 4, 2015)
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.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
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:rs17585 |
The reference OMIM entry for this protein is 173320
Ribonuclease/angiogenin inhibitor 1; rnh1
Rnh
Ribonuclease inhibitor; ri
Placental ribonuclease inhibitor; pri
Cytosolic ribonuclease inhibitor; cri
DESCRIPTION
RNH1 belongs to a family of proteinaceous cytoplasmic RNase inhibitors found in many tissues that bind to both intracellular and extracellular RNases. In addition to inhibiting intracellular RNases, RNH1 may have a role in the regulation of angiogenin (ANG; 105850) (summary by Lee et al., 1988).CLONING
Lee et al. (1988) determined the primary structure of PRI from the cDNA. The mature protein encodes a 460-amino acid polypeptide with a molecular mass of 49.8 kD. The amino acid sequence contains 7 direct internal repeat units, each 57 amino acids in length. These repeat units comprise 87% of the molecule. The average degree of identity between any 2 is 39%. By cell fractionation and immunohistochemical analysis of human HeLa and HCT cells, Furia et al. (2011) found that RNH1 localized to mitochondria and nucleus, in addition to cytoplasm. RNH1 copurified with proteins of the mitochondrial matrix and inner membrane.GENE FUNCTION
Monti and D'Alessio (2004) found that knockdown of CRI via small interfering RNA (siRNA) made HeLa cells more sensitive to cytotoxic RNases, such as bovine seminal RNase and human pancreatic RNase (RNASE1; 180440). Knockdown of CRI did not render benign RNases cytotoxic. Because of its high cysteine content (32 residues), Monti et al. (2007) hypothesized that CRI might contribute to cellular redox homeostasis. Knockdown of CRI via siRNA lowered the content of reduced glutathione and other small thiol compounds in HeLa cells and human umbilical vein endothelial cells. Knockdown of CRI also increased DNA damage and cell sensitivity to oxidative insult. Monti et al. (2007) found that reducing agents inhibited binding of CRI to immobilized RNase A. PTEN (601728) is a lipid phosphatase that regulates cell signaling via phosphatidylinositols and functions as a tumor suppressor. Kim et al. (2011) presented evidence that PTEN regulates RNH1. Tandem affinity purification, followed by mass spectrometric analysis, identified RNH1 as a protein that interacted with PTEN in HEK293 cells. Kim et al. (2011) also found that RNH1 accelerated nuclear Drosha (RNASEN; 608828)-dependent processing of the microRNA-21 (MIR21; 611020) primary transcript (pri-MIR21) to the precursor stem-loop structure (pre-MIR21). RNH1 interacted directly with Drosha and appeared to interact with pri-MIR21. Addition of a nuclear localization signal to the RNH1 N terminus accelerated pri-MIR21 processing. Interaction of PTEN with RNH1 prevented interaction of RNH1 with Drosha and reduced pri-MIR21 processing in vitro and in HEK293 cells. Kim et al. (2011) concluded that PTEN tumor suppressor activity may, in part, be due to inhibited processing of MIR21, which can function as an oncogene. Zhao et al. (2013) found that Rnh1 promoted differentiation and myelination of cultured primary rat oligodendrocytes. Rnh1 affected oligodendrocyte differentiation through RhoA (165390)-Rock (see 601702) signaling and elevated expression and phosphorylation of Fyn (137025).MAPPING
By study of human-rodent somatic cell hybrids and by in situ hybridization, Weremowicz et al. (1990) mapped the PRI gene to 11p15. The localization was further refined to 11p15.5, distal to the IGF2 gene, by in situ hybridization to metaphase chromosomes from a cell line with a well-characterized translocation involving a breakpoint between IGF2 (147470) and HRAS (190020). Zneimer et al. (1990) localized the RNH gene to 11p15.5 by in sit ... More on the omim web site
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 173320 was added.