Human Gene CLIC1 (uc011hbd.1) Description and Page Index
  Description: Homo sapiens chloride intracellular channel 1 (CLIC1), mRNA.
RefSeq Summary (NM_001288): Chloride channels are a diverse group of proteins that regulate fundamental cellular processes including stabilization of cell membrane potential, transepithelial transport, maintenance of intracellular pH, and regulation of cell volume. Chloride intracellular channel 1 is a member of the p64 family; the protein localizes principally to the cell nucleus and exhibits both nuclear and plasma membrane chloride ion channel activity. [provided by RefSeq, Jul 2008].
Transcript (Including UTRs)
   Position: chr6_mann_hap4:3,041,248-3,047,235 Size: 5,988 Total Exon Count: 6 Strand: -
Coding Region
   Position: chr6_mann_hap4:3,041,509-3,046,971 Size: 5,463 Coding Exon Count: 6 

Page IndexSequence and LinksUniProtKB CommentsGenetic AssociationsCTDMicroarray
RNA StructureProtein StructureOther SpeciesmRNA DescriptionsOther NamesModel Information
Data last updated: 2013-06-14

+  Sequence and Links to Tools and Databases
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-  Comments and Description Text from UniProtKB
DESCRIPTION: RecName: Full=Chloride intracellular channel protein 1; AltName: Full=Chloride channel ABP; AltName: Full=Nuclear chloride ion channel 27; Short=NCC27; AltName: Full=Regulatory nuclear chloride ion channel protein; Short=hRNCC;
FUNCTION: Can insert into membranes and form chloride ion channels. Channel activity depends on the pH. Membrane insertion seems to be redox-regulated and may occur only under oxydizing conditions. Involved in regulation of the cell cycle.
SUBUNIT: Monomer. Homodimer (in vitro). Interacts with TRAPPC2. Dimerization requires a conformation change that leads to the exposure of a large hydrophobic surface. In vivo, this may lead to membrane insertion. Interacts with AKAP9.
SUBCELLULAR LOCATION: Nucleus. Nucleus membrane; Single-pass membrane protein (Probable). Cytoplasm. Cell membrane; Single-pass membrane protein (Probable). Note=Mostly in the nucleus including in the nuclear membrane. Small amount in the cytoplasm and the plasma membrane. Exists both as soluble cytoplasmic protein and as membrane protein with probably a single transmembrane domain.
TISSUE SPECIFICITY: Expression is prominent in heart, placenta, liver, kidney and pancreas.
DOMAIN: Members of this family may change from a globular, soluble state to a state where the N-terminal domain is inserted into the membrane and functions as chloride channel. A conformation change of the N-terminal domain is thought to expose hydrophobic surfaces that trigger membrane insertion.
PTM: Hydrogen peroxide treatment causes a conformation change, leading to dimerization and formation of an intramolecular disulfide bond between Cys-24 and Cys-59.
MISCELLANEOUS: The protein seems to have very low affinity for glutathione, even though glutathione binding was observed in protein crystals.
SIMILARITY: Belongs to the chloride channel CLIC family.
SIMILARITY: Contains 1 GST C-terminal domain.
WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="";

+  Genetic Association Studies of Complex Diseases and Disorders
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+  Comparative Toxicogenomics Database (CTD)
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+  Microarray Expression Data
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+  mRNA Secondary Structure of 3' and 5' UTRs
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-  Protein Domain and Structure Information
  InterPro Domains: Graphical view of domain structure
IPR010987 - Glutathione-S-Trfase_C-like
IPR004045 - Glutathione_S-Trfase_N
IPR002946 - Int_Cl_channel
IPR012336 - Thioredoxin-like_fold

SCOP Domains:
47616 - Glutathione S-transferase (GST), C-terminal domain
52833 - Thioredoxin-like

Protein Data Bank (PDB) 3-D Structure

- X-ray Chimera LS-SNP

- X-ray Chimera LS-SNP

- X-ray Chimera LS-SNP
To conserve bandwidth, only the images from the first 3 structures are shown.
1RK4 - X-ray Chimera LS-SNP 3O3T - X-ray Chimera LS-SNP 3P8W - X-ray Chimera LS-SNP
3P90 - X-ray Chimera LS-SNP 3QR6 - X-ray Chimera 3SWL - X-ray Chimera
3TGZ - X-ray Chimera 3UVH - X-ray Chimera 4IQA - X-ray Chimera
Chimera help

ModBase Predicted Comparative 3D Structure on O00299
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.

-  Orthologous Genes in Other Species
  Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
MouseRatZebrafishD. melanogasterC. elegansS. cerevisiae
Genome BrowserGenome BrowserNo orthologNo orthologNo orthologNo ortholog
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Protein Sequence     

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+  Other Names for This Gene
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+  Gene Model Information
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-  Methods, Credits, and Use Restrictions
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