1RK4,1K0N


Conserved Protein Domain Family
GST_C_CLIC1

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cd10300: GST_C_CLIC1 
Click on image for an interactive view with Cn3D
C-terminal, alpha helical domain of Chloride Intracellular Channel 1
Glutathione S-transferase (GST) C-terminal domain family, Chloride Intracellular Channel (CLIC) 1 subfamily; CLICs are auto-inserting, self-assembling intracellular anion channels involved in a wide variety of functions including regulated secretion, cell division, and apoptosis. They can exist in both water-soluble and membrane-bound states and are found in various vesicles and membranes, and they may play roles in the maintenance of these intracellular membranes. The membrane localization domain is present in the N-terminal part of the protein. Soluble CLIC1 is monomeric and adopts a fold similar to GSTs, containing an N-terminal domain with a thioredoxin fold and a C-terminal alpha helical domain. Upon oxidation, the N-terminal domain of CLIC1 undergoes a structural change to form a non-covalent dimer stabilized by the formation of an intramolecular disulfide bond between two cysteines that are far apart in the reduced form. The CLIC1 dimer bears no similarity to GST dimers. The redox-controlled structural rearrangement exposes a large hydrophobic surface, which is masked by dimerization in vitro. In vivo, this surface may represent the docking interface of CLIC1 in its membrane-bound state. The two cysteines in CLIC1 that form the disulfide bond in oxidizing conditions are essential for dimerization and chloride channel activity. CLIC1 is widely expressed in many tissues and its subcellular localization is dependent on cell type and cell cycle phase. It acts as a sensor of cell oxidation and appears to have a role in diseases that involve oxidative stress including tumorigenic and neurodegenerative diseases.
Statistics
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PSSM-Id: 198333
Aligned: 6 rows
Threshold Bit Score: 249.088
Created: 4-Apr-2011
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
N-terminal
Conserved site includes 11 residues -Click on image for an interactive view with Cn3D
Feature 1:N-terminal domain interface [polypeptide binding site]
Evidence:

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                                                                      ##
1RK4_B       102 NPESNTAGLDIFAKFSAYIKNSNPALNDNLEKGLLKALKVLDNYLTSPLPEEVDetSAEDEGVSQRKFLDGNELTLADCN 181 human
1K0N_A       100 NPESNTAGLDIFAKFSAYIKNSNPALNDNLEKGLLKALKVLDNYLTSPLPEGVDetSAEDEGVSQRKFLDGNELTLADCN 179 human
AAH73268      99 NPESNNAGVNVFAKFSAYIKNPNPALNQNLVNGLLKALNVLDRYLNTPLPDEIDenCAEDETVSNRKFLDGNELTLADCN 178 African clawed ...
AAH66618     100 NPESNTAGLDVFSKFSAYIKNSNPQMNDNLEKGLLKALKKLDDYLSSPLPDEIDenSADDVISSTRSFLDGQELTLADCN 179 zebrafish
NP_001037092 100 NPESNTAGLDIFAKFSAYIKNSNPALNDNLEKGLLKALKVLDNYLTSPLPEEVDetSAEDEGVSQRKFLDGNELTLADCN 179 domestic silkworm
XP_003228103 100 NPESNTAGLDVFAKYSAYIKNSNPALNANLEKGLLKALKVLDMYLMAPLPEEVDenSAEDEGQSSRKFLDGDELTLADCN 179 green anole
Feature 1          #   #                               ##  ##    #  ##      
1RK4_B       182 LLPKLHIVQVVCKKYRGFTIPEAFRGVHRYLSNAYAREEFASTCPDDEEIELAYEQVAK 240 human
1K0N_A       180 LLPKLHIVQVVCKKYRGFTIPEAFRGVHRYLSNAYAREEFASTCPDDEEIELAYEQVAK 238 human
AAH73268     179 LLPKLNIVQVVCEHFRGFKIPAEFTGIHRYLQNAYKREEFASTCPDAAEISRAYAEVAK 237 African clawed frog
AAH66618     180 LLPKLHIVKVVCLKFRGFSIPRSLTSLWRYLDAAYAREEFSSTCPSDEEIYVAYSSVVK 238 zebrafish
NP_001037092 180 LLPKLHIVQVVCKKYRGFTIPEAFRGVHRYLSNAYAREEFASTCPDDEEIELAYEQVAK 238 domestic silkworm
XP_003228103 180 LLPKLHIVKVVCKKYRNFTIPEEFCGIHRYLKNAYAREEFASTCPDDEEIELAYELVAK 238 green anole

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