| TCID | Name | Domain | Kingdom/Phylum | Protein(s) |
|---|---|---|---|---|
|
1.A.12.1.1 | Organellar chloride (anion selective) channel, p64 (outwardly rectifying) (437 aas and 1 TMS). CLIC5 was the first mitochondrial chloride channel to be identified in the inner mitochondrial membrane, while CLIC4 is located predominantly in the outer mitochondrial membrane. Gururaja Rao et al. 2020 discussed the intracellular chloride channels, their roles in pathologies, such as cardiovascular, cancer, and neurodegenerative diseases, and developments concerning their usage as theraputic targets in humans. | Eukaryota |
Metazoa | CLIC5 or p64 of Bos taurus |
|
1.A.12.1.2 | Nuclear chloride channel-27, NCC27 or CLIC1 (Br- > Cl- > I-) (241 aas). CLIC1 has two charged residues, K37 and R29, in its single TMS which are important for the biophysical properties of the channel (Averaimo et al. 2013). A putative Lys37-Trp35 cation-pi interaction stabilizes the active dimeric form of the CLIC1 TMS in membranes (Peter et al. 2013). This channel may play a role in cancer (Peretti et al. 2014). A positively charged motif at the C-terminus of the single TMS enhances membrane partitioning and insertion via electrostatic contacts. It also functions as an electrostatic plug to anchor the TMS in membranes and is involved in orientating the TMS with respect to the cis and trans faces of the membrane (Peter et al. 2014). The CLIC1 protein accumulates in the circulating monocyte membrane during neurodegeneration (Carlini et al. 2020). The involvement of CLIC1 protein functions in physiological and in pathological conditions has been reviewed (Cianci and Verduci 2021). | Eukaryota |
Metazoa | CLIC1 or NCC27 of Homo sapiens |
|
1.A.12.1.3 | Organellar chloride channel, CLIC-5A (251 aas; 2 TMSs; one of six homologous human genes) (95% identical to 1.A.12.1.1 but lacks the N-terminal 185 residues.) It associates with the cortical actin cytoskeleton (Berryman et al., 2004). | Eukaryota |
Metazoa | CLIC-5A of Homo sapiens (Q53G01) |
|
1.A.12.1.4 | Organellar chloride channel CLIC-6 (704 aas) [The C-terminal half (residues 400-704) resembles a CLIC channel; the N-terminal half (residues 104-356) resembles a repeated C-terminal region of the bovine Na+/Ca2+,K+ exchanger (TC #2.A.19.4.1) as well as several other bacterial and eukaryotic proteins]. | Eukaryota |
Metazoa | CLIC-6 of Homo sapiens (Q96NY7) |
|
1.A.12.1.5 | The Janus protein, CLIC2. The 3-D structure of its water soluble form has been determined at 1.8 Å resolution (Cromer et al., 2007). CLIC2 interacts with the skeletal ryanodine receptor (RyR1) and modulates its channel activity (Meng et al., 2009). | Eukaryota |
Metazoa | CLIC2 of Homo sapiens (O15247) |
|
1.A.12.1.6 | Chloride intracellular channel protein 4, CLIC4. Regulates the histamine H3 receptor (Maeda et al., 2008)) Discriminates poorly between anions and cations (Singh and Ashley, 2007). 76% identical to CLIC5; it may play a role in cancer (Peretti et al. 2014). CLIC5 was the first mitochondrial chloride channel to be identified in the inner mitochondrial membrane, while CLIC4 is located predominantly in the outer mitochondrial membrane. Gururaja Rao et al. 2020 discussed the intracellular chloride channels, their roles in pathologies, such as cardiovascular, cancer, and neurodegenerative diseases, and developments concerning their usage as theraputic targets in humans. | Eukaryota |
Metazoa | CLIC4 of Homo sapiens (Q9Y696) |
|
1.A.12.1.7 | Intracellular Cl- channel-3 (CLIC3). The 3-d structure is known (3FY7). This protein is associated with pregnancy disorders (Murthi et al., 2012). | Eukaryota |
Metazoa | CLIC3 of Homo sapiens (O95833) |
|
1.A.12.2.1 | The plant Cl- intracellular channel protein DHAR1 (glutathione dehydrogenase/dehydroascorbate reductase) (Elter et al., 2007) | Eukaryota |
Viridiplantae | DHAR1 of Arabidopsis thaliana (NP_173387) |
|
1.A.12.2.2 | Putative Glutathione S-transferase. Pore formation has not been demonstrated in prokaryotes. | Bacteria |
Spirochaetes | Probable glutathione S-transferase of Leptospira interrogans |
|
1.A.12.3.1 | The bacterial CLIC homologue, stringent starvation protein A, SspA (212 aas; 0 TMSs) [N-terminal Trx domain; C-terminal glutathione S-transferase (GST) domain]. May be involved in acid (Hansen et al. 2005) and sodium ion tolerance (Wu et al. 2014). | Bacteria |
Proteobacteria | Stringent starvation protein A of E. coli (P0ACA3) |
|
1.A.12.3.2 | Glutathione S-transferase, YfcF of 214 aas. Pore formation has not been demostrated. | Bacteria |
Proteobacteria | YfcF of E. coli |