Clathrin heavy chain 2 (CLTCL1)
The protein contains 1640 amino acids for an estimated molecular weight of 187030 Da.
Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Two different adapter protein complexes link the clathrin lattice either to the plasma membrane or to the trans-Golgi network (By similarity). (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.
- 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.
- 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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Biological Process
Anatomical structure morphogenesis
Clathrin coat assembly
Intracellular protein transport
Membrane organization
Mitotic cell cycle
Mitotic nuclear division
Positive regulation of glucose import
Receptor-mediated endocytosis
Retrograde transport, endosome to Golgi
Signal transduction
The reference OMIM entry for this protein is 601273
Clathrin, heavy polypeptide-like 1; cltcl1
Clathrin, heavy polypeptide d; cltd
Clh22
Chc22
CLONING
Using a YAC clone containing the velocardiofacial syndrome (VCFS; 192430) critical region on chromosome 22q11 as a substrate for cDNA selection, Sirotkin et al. (1996) derived a cDNA, which they designated CLTD, that encodes a protein with a high degree of homology at the amino acid level to human rat and Drosophila clathrin heavy chain. The CLTD protein is 7% divergent at the amino acid level from that of the human clathrin heavy chain gene (CLTC; 118955) located on chromosome 17q11-qter. Kedra et al. (1996) cloned and characterized a clathrin heavy chain gene, which they referred to as CLH22. The gene was cloned using a software-based exon-trapping approach based on sequencing of genomic DNA present in chromosome 22q11 contigs combined with the use of exon-prediction computer programs. The 5,470-bp sequence covering the entire open reading frame encodes a 1,640-amino acid polypeptide that is identical to the polypeptide described by Sirotkin et al. (1996). Although expression of the CLTD gene was ubiquitous, it was relatively low in all tissues except skeletal muscle, testis, and heart. The main transcript was 6 kb, and alternate transcripts were detected in several tissues. Kedra et al. (1996) demonstrated loss of expression of the CLTD gene in 37 out of 46 sporadic meningiomas examined. In genomic DNA from 82 sporadic meningiomas, they demonstrated aberrant restriction patterns consistent with intragenic rearrangements in 4 tumors. Based on these findings, the authors proposed that CLTD may be considered a candidate meningioma tumor suppressor gene. Long et al. (1996) cloned and characterized a gene they symbolized CLTCL for 'CLTC-like.' The gene was expressed in all fetal tissues tested and was selectively expressed in certain adult tissues, particularly skeletal muscle. They observed alternative splicing of an exon near the C terminus of the predicted polypeptide.GENE FUNCTION
Intracellular trafficking of the glucose transporter GLUT4 (138190) from storage compartments to the plasma membrane is triggered in muscle and fat during the body's response to insulin. Clathrin is involved in intracellular trafficking, and in humans, the clathrin heavy-chain isoform CHC22 is highly expressed in skeletal muscle. Vassilopoulos et al. (2009) found a role for CHC22 in the formation of insulin-responsive GLUT4 compartments in human muscle and adipocytes. CHC22 also associated with expanded GLUT4 compartments in muscle from patients with type 2 diabetes (125853). Tissue-specific introduction of CHC22 in mice, which have only a pseudogene for this protein, caused aberrant localization of GLUT4 transport pathway components in their muscle, as well as features of diabetes. Thus, Vassilopoulos et al. (2009) concluded that CHC22-dependent membrane trafficking constitutes a species-restricted pathway in human muscle and fat with potential implications for type 2 diabetes.MAPPING
Long et al. (1996) used fluorescence in situ hybridization to map CLTCL to proximal 22q near the region commonly deleted in DiGeorge syndrome (DGS; 188400) and VCFS. In the course of comparative mapping of the human 22q11 region in mice, Puech et al. (1997) found that CLTCL gene, which lies in the center of a cluster of genes whose homologs reside on chromosome 16, is not located there in the mouse. A gene they referred to as Cltd-rs-4 was located in the central region of mouse chromosome 11 that shares a large region of homology with ... 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 601273 was added.