Leucine carboxyl methyltransferase 1 (LCMT1)
The protein contains 334 amino acids for an estimated molecular weight of 38379 Da.
Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues. (updated: Jan. 7, 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.
- 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.
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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Biological Process
C-terminal protein methylation
Cellular protein modification process
G2/M transition of mitotic cell cycle
Negative regulation of protein-containing complex assembly
Protein methylation
Regulation of apoptotic process
Regulation of glucose metabolic process
Regulation of mitotic cell cycle spindle assembly checkpoint
The reference OMIM entry for this protein is 610286
Leucine carboxyl methyltransferase 1; lcmt1
DESCRIPTION
LCMT
1 catalyzes the methylation of the carboxyl group of the C-terminal leucine residue (leu309) of the catalytic subunit of protein phosphatase-2A (PPP2CA; 176915) (De Baere et al., 1999).CLONING
By database analysis with partial peptide sequences of a leucine carboxyl methyltransferase purified from porcine brain as probe, De Baere et al. (1999) identified overlapping EST clones and used PCR techniques to generate the complete human LCMT
1 open reading frame. The deduced 334-amino acid LCMT
1 protein has a predicted molecular mass of 38.305 kD and shares high sequence similarity in the methyltransferase domain with other leucine carboxyl methyltransferases across diverse species.GENE FUNCTION
Using a variety of techniques including HPLC analysis of radiolabeled, methylated peptides, multiple inhibitors, and recognition by antibodies sensitive to substrate methylation, De Baere et al. (1999) determined that recombinant LCMT
1 expressed in bacterial cells catalyzes the specific methylation of the C-terminal leu309 of the catalytic subunit of protein phosphatase-2A, and that methylation does not affect phosphatase activity. De Baere et al. (1999) determined that the specific activities, Km, and other properties of the recombinant LCMT
1 enzyme corresponded well with those of the native porcine brain leucine carboxyl methyltransferase. Lee and Pallas (2007) found that knockdown of LCMT
1 by small hairpin RNA substantially reduced PP2A methylation in HeLa cells, indicating that LCMT
1 is the major PP2A-methylating enzyme. LCMT
1 knockdown also decreased association of the PP2A regulatory subunit B-alpha (PPP2R2A; 604941) with the PP2A catalytic subunit, induced apoptosis, and sensitized HeLa and colon carcinoma cells to the microtubule spindle-targeting drug nocodazole. Lee and Pallas (2007) concluded that LCMT
1 is important for normal progression through mitosis and for cell survival.MAPPING
The International Radiation Hybrid Mapping Consortium mapped the LCMT
1 gene to chromosome 16 (TMAP RH64916).ANIMAL MODEL
Lee and Pallas (2007) found that Lcmt1 knockout in mice was embryonic lethal. ... 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
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
June 20, 2017: Protein entry updated
Automatic update: comparative model was added.
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 610286 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed