Q9Z1Q5 · CLIC1_MOUSE
- ProteinChloride intracellular channel protein 1
- GeneClic1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids241 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
In the soluble state, catalyzes glutaredoxin-like thiol disulfide exchange reactions with reduced glutathione as electron donor. Reduces selenite and dehydroascorbate and may act as an antioxidant during oxidative stress response (By similarity).
Can insert into membranes and form voltage-dependent multi-ion conductive channels. Membrane insertion seems to be redox-regulated and may occur only under oxidizing conditions. Involved in regulation of the cell cycle (By similarity).
Can insert into membranes and form voltage-dependent multi-ion conductive channels. Membrane insertion seems to be redox-regulated and may occur only under oxidizing conditions. Involved in regulation of the cell cycle (By similarity).
Catalytic activity
- 2 glutathione + L-dehydroascorbate = glutathione disulfide + L-ascorbateThis reaction proceeds in the forward direction.
- chloride(in) = chloride(out)
- iodide(out) = iodide(in)
- thiocyanate(in) = thiocyanate(out)
- nitrate(in) = nitrate(out)
- bromide(in) = bromide(out)
- fluoride(in) = fluoride(out)
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloride channel complex | |
Cellular Component | cytoplasm | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | extracellular exosome | |
Cellular Component | membrane | |
Cellular Component | mitochondrion | |
Cellular Component | nuclear envelope | |
Cellular Component | nuclear membrane | |
Cellular Component | nucleus | |
Cellular Component | perinuclear region of cytoplasm | |
Cellular Component | plasma membrane | |
Molecular Function | chloride channel activity | |
Molecular Function | oxidoreductase activity | |
Biological Process | chloride transport | |
Biological Process | positive regulation of osteoblast differentiation | |
Biological Process | regulation of mitochondrial membrane potential |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameChloride intracellular channel protein 1
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ9Z1Q5
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Nucleus membrane ; Single-pass membrane protein
Cell membrane ; Single-pass membrane protein
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 (By similarity).
Might not be present in the nucleus of cardiac cells (By similarity).
Might not be present in the nucleus of cardiac cells (By similarity).
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 26-46 | Helical; Note=After insertion into the membrane | ||||
Sequence: FSQRLFMVLWLKGVTFNVTTV |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000144202 | 2-241 | Chloride intracellular channel protein 1 | |||
Sequence: AEEQPQVELFVKAGSDGAKIGNCPFSQRLFMVLWLKGVTFNVTTVDTKRRTETVQKLCPGGQLPFLLYGTEVHTDTNKIEEFLEAMLCPPRYPKLAALNPESNTSGLDIFAKFSAYIKNSNPALNDNLEKGLLKALKVLDNYLTSPLPEEVDETSAEDEGISQRKFLDGNELTLADCNLLPKLHIVQVVCKKYRGFTIPEAFRGVHRYLSNAYAREEFASTCPDDEEIELAYEQVARALK | ||||||
Modified residue | 13 | N6-acetyllysine | ||||
Sequence: K | ||||||
Disulfide bond | 24↔59 | |||||
Sequence: CPFSQRLFMVLWLKGVTFNVTTVDTKRRTETVQKLC | ||||||
Modified residue | 119 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 121 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 131 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 156 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 211 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 233 | Phosphotyrosine | ||||
Sequence: Y |
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Gene expression databases
Interaction
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 (By similarity).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, motif, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 2-90 | Required for insertion into the membrane | ||||
Sequence: AEEQPQVELFVKAGSDGAKIGNCPFSQRLFMVLWLKGVTFNVTTVDTKRRTETVQKLCPGGQLPFLLYGTEVHTDTNKIEEFLEAMLCP | ||||||
Motif | 24-27 | G-site | ||||
Sequence: CPFS | ||||||
Domain | 93-233 | GST C-terminal | ||||
Sequence: YPKLAALNPESNTSGLDIFAKFSAYIKNSNPALNDNLEKGLLKALKVLDNYLTSPLPEEVDETSAEDEGISQRKFLDGNELTLADCNLLPKLHIVQVVCKKYRGFTIPEAFRGVHRYLSNAYAREEFASTCPDDEEIELAY |
Domain
The active G-site contains a monothiol Cys-X-X-Ser motif which mediates glutathione-dependent redox catalysis.
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 a channel. The redox status of the active cysteine in Cys-X-X-Cys/Ser motif likely determines the capacity to adopt a soluble or membrane-inserted state. A conformation change of the N-terminal domain is thought to expose hydrophobic surfaces that trigger membrane insertion.
Sequence similarities
Belongs to the chloride channel CLIC family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length241
- Mass (Da)27,013
- Last updated2007-01-23 v3
- Checksum0260A9ECEDA51B1C
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF109905 EMBL· GenBank· DDBJ | AAC84155.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC004658 EMBL· GenBank· DDBJ | AAH04658.1 EMBL· GenBank· DDBJ | mRNA |