LanC-like protein 2 (LANCL2)
The protein contains 450 amino acids for an estimated molecular weight of 50854 Da.
Necessary for abscisic acid (ABA) binding on the cell membrane and activation of the ABA signaling pathway in granulocytes. (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.
- 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.
This protein is annotated as membranous in Gene Ontology, is annotated as membranous in UniProt.
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| Variant | Description |
|---|---|
| dbSNP:rs2272263 | |
| dbSNP:rs6961412 |
Biological Process
Carbohydrate metabolic process
Negative regulation of transcription, DNA-templated
Positive regulation of abscisic acid-activated signaling pathway
Cellular Component
Cortical actin cytoskeleton
Cytoplasm
Cytosol
Nucleoplasm
Nucleus
Plasma membrane
The reference OMIM entry for this protein is 612919
Lanc-like 2; lancl2
Testis-specific adriamycin sensitivity protein; tasp
CLONING
By searching for genes similar to LANCL1 (604155), followed by 3-prime RACE of a human cerebral cortex cDNA library, Mayer et al. (2001) cloned LANCL2. The deduced 450-amino acid protein contains a Walker A box and 7 repetitive hydrophobic regions that contain GxxG motifs. It shares 57.9% amino acid identity with LANCL1. Northern blot analysis detected high expression of 4.7- and 4.1-kb transcripts and weaker expression of 2.5- and 1.8-kb transcripts in brain. The 1.8-kb transcript was highly expressed in testis. All other tissues examined showed weak expression of the 4.1- and 1.8-kb transcripts. RNA dot blot analysis confirmed ubiquitous LANCL2 expression, with highest levels in amygdala, followed by temporal lobe and testis. Database analysis revealed conservation of LANCL proteins in bacteria, plant, and animal genomes. Using Western blot and immunohistochemical analyses, Park and James (2003) found that epitope-tagged LANCL2 distributed to the plasma membrane, cytosol, and nucleus of a transfected human uterine sarcoma cell line.GENE FUNCTION
Using a human uterine sarcoma cell line and a multidrug-resistant derivative, Park and James (2003) found that ectopic expression of LANCL2 significantly reduced expression of the multidrug resistance gene MDR1 (ABCB1; 171050) and increased cell sensitivity toward the chemotherapeutic agent adriamycin. Reporter gene assays revealed that LANCL2 repressed transcription of the MDR1 promoter. Zhang et al. (2009) showed that LANCL2 exhibited Zn(2+)-dependent glutathione binding. LANCL2 bound the SH3 domain of mouse Eps8 (600206), but not other SH3-containing proteins. The interaction between LANCL2 and Eps8 did not require either of the PxxP motifs of LANCL2, but it was inhibited by glutathione.MAPPING
Park and James (2003) stated that the LANCL2 gene maps within 200 bp of the EGFR gene (131550) on chromosome 7p11.2. ... 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
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 612919 was added.