RNA 3'-terminal phosphate cyclase (RTCA)
The protein contains 366 amino acids for an estimated molecular weight of 39337 Da.
Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing. (updated: April 1, 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.
- 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.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- 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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The reference OMIM entry for this protein is 611286
Rna terminal phosphate cyclase domain-containing protein 1; rtcd1
Rtc domain-containing protein 1
Rna 3-prime-terminal phosphate cyclase: rpc
DESCRIPTION
RNA 3-prime-terminal phosphate cyclase (RPC; EC 6.5.1.4) catalyzes the ATP-dependent conversion of a 3-prime phosphate to a 2-prime,3-prime-cyclic phosphodiester at the end of RNA (Genschik et al., 1997).CLONING
Genschik et al. (1997) purified RPC from HeLa cells and obtained a full-length RPC clone by PCR and screening a HeLa cell cDNA library. The deduced 366-amino acid protein has a calculated molecular mass of 39.4 kD. Northern blot analysis detected ubiquitous expression of 1.8- and 3.0-kb transcripts in human tissues and cell lines, although the ratio between the transcripts varied among tissues. Highest expression was in skeletal muscle. Immunofluorescence analysis localized epitope-tagged RPC primarily to the nucleus in HeLa cells and other mammalian cell lines. RPC is conserved among eukaryotes, bacteria, and archaea.GENE FUNCTION
Genschik et al. (1997) expressed recombinant human RPC in E. coli and found that it underwent adenylation in the presence of radiolabeled ATP and catalyzed cyclization of the 3-prime-terminal phosphate in different RNA substrates. Comparison of RNA and DNA substrates with identical sequences showed that the latter were 500-fold poorer substrates for RPC. Genschik et al. (1997) stated that ATP is the best cofactor for this reaction, but GTP, CTP, and UTP, but not dATP, can also act as cofactors, although less efficiently.GENE STRUCTURE
Genschik et al. (1997) determined that the upstream region of the RTCD1 gene is associated with a CpG island.MAPPING
The International Radiation Hybrid Mapping Consortium mapped the RTCD1 gene to chromosome 1 (TMAP SHGC-53265). ... 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 611286 was added.