Clathrin light chain A (CLTA)
The protein contains 248 amino acids for an estimated molecular weight of 27077 Da.
Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Acts as component of the TACC3/ch-TOG/clathrin complex proposed to contribute to stabilization of kinetochore fibers of the mitotic spindle by acting as inter-microtubule bridge (PubMed:15858577, PubMed:21297582). (updated: Nov. 22, 2017)
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.
This protein is annotated as membranous in Gene Ontology.
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Biological Process
Antigen processing and presentation of exogenous peptide antigen via MHC class II
Axon guidance
Cell cycle
Cell division
Clathrin coat assembly
Clathrin-dependent endocytosis
Endocytosis
Epidermal growth factor receptor signaling pathway
Intracellular protein transport
Low-density lipoprotein particle clearance
Low-density lipoprotein particle receptor catabolic process
Membrane organization
Microtubule-based movement
Negative regulation of epidermal growth factor receptor signaling pathway
Neurotrophin TRK receptor signaling pathway
Post-Golgi vesicle-mediated transport
Cellular Component
Clathrin coat
Clathrin coat of coated pit
Clathrin coat of trans-Golgi network vesicle
Clathrin complex
Clathrin vesicle coat
Clathrin-coated endocytic vesicle
Clathrin-coated endocytic vesicle membrane
Cytoplasmic vesicle
Cytoplasmic, membrane-bounded vesicle
Cytosol
Endolysosome membrane
Intracellular membrane-bounded organelle
Membrane
Plasma membrane
Postsynaptic endocytic zone cytoplasmic component
Presynaptic endocytic zone membrane
Spindle
Synaptic vesicle membrane
Trans-Golgi network membrane
The reference OMIM entry for this protein is 118960
Clathrin, light polypeptide a; clta
Lca
DESCRIPTION
Clathrin is the main structural component of the lattice covering the cytoplasmic face of the coated pits and coated vesicles in which specific macromolecules are entrapped in the process of receptor-mediated endocytosis. Clathrin is a large, soluble protein composed of heavy chains, which have molecular masses of about 192 kD, and light chains, which have molecular masses of about 32 to 38 kD. Two major classes of clathrin light chains, referred to as LCA (CLTA) and LCB (CTLB; 118970), have been identified (summary by Kirchhausen et al., 1987).CLONING
Jackson et al. (1987) identified 4 distinct forms of bovine clathrin light chains. This molecular variability derived from tissue-specific splicing of Lca and Lcb genes. Brodsky et al. (1987) identified that part of the light chain sequence that mediates heavy chain binding and is the region of strongest homology with intermediate filament proteins. Sequence analysis shows an overall homology of 60% between LCA and LCB and the presence of brain-specific insertion sequences. Jackson and Parham (1988) compared cDNAs encoding the brain and nonbrain forms of human LCA and LCB with their homologs in cow and rat. The significant differences that distinguish LCA from LCB and the brain from the nonbrain forms show remarkable preservation in all 3 species. Each clathrin triskelion consists of 3 heavy chains and 3 light chains. In the brain, tissue-specific mRNA splicing yields larger forms of LCA and LCB, containing additional insertion sequences of 30 and 18 amino acids, respectively. Xiao et al. (2006) reported that the 248-amino acid CLTA protein has a conserved sequence near its N terminus, followed by an HSC70 (HSPA8; 600816)-binding domain, a calcium-binding domain, a heavy chain-binding site, a neuron-specific insert, and a C-terminal segment that includes a calmodulin (see 114180)-binding site.MAPPING
By Southern blot analysis on genomic DNA extracted from a panel of mouse-human somatic cell hybrids and by isotopic in situ hybridization, Ponnambalam et al. (1994) assigned the CLTA gene to human 12q23-q24. However, Gross (2011) mapped the CLTA gene to chromosome 9p13.3 based on an alignment of the CLTA sequence (GenBank GENBANK AK225153) with the genomic sequence (GRCh37).BIOCHEMICAL FEATURES
Kirchhausen et al. (1987) studied the structure of the clathrin light chains. The clathrin unit that assembles into coats has 3 extended legs, 500 angstroms in length, splayed out in a pinwheel-like structure (triskelion). Each of the legs is built from a single heavy chain, with a light chain bound to each proximal segment.GENE FUNCTION
Royle et al. (2005) showed that clathrin stabilizes fibers of the mitotic spindle to aid congression of chromosomes. Clathrin bound to the spindle directly by the N-terminal domain of clathrin heavy chain. Depletion of clathrin heavy chain using RNA interference prolonged mitosis; kinetochore fibers were destabilized, leading to defective congression of chromosomes to the metaphase plate and persistent activation of the spindle checkpoint. Normal mitosis was rescued by clathrin triskelia but not the N-terminal domain of clathrin heavy chain, indicating that stabilization of kinetochore fibers was dependent on the unique structure of clathrin. Using yeast 2-hybrid analysis of a human brain cDNA library, Xiao et al. (2006) found that the heavy chain-binding region and C-terminal domain of CLTA interac ... More on the omim web site
Feb. 10, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.
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 118960 was added.