Q8BXK9 · CLIC5_MOUSE
- ProteinChloride intracellular channel protein 5
- GeneClic5
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids251 (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 (By similarity).
Can insert into membranes and form non-selective ion channels almost equally permeable to Na+, K+ and Cl- (By similarity).
Required for normal hearing (By similarity).
Necessary for the formation of stereocilia in the inner ear and normal development of the organ of Corti (PubMed:17021174, PubMed:24285636).
Required for the proper localization of PTPRQ and RDX to the stereocilium base during postnatal maturation of hair bundles (PubMed:24285636).
Can insert into membranes and form poorly selective ion channels that may also transport chloride ions (By similarity).
Required for the development and/or maintenance of the proper glomerular endothelial cell and podocyte architecture (By similarity).
Plays a role in formation of the lens suture in the eye, which is important for normal optical properties of the lens (PubMed:29425878).
Can insert into membranes and form non-selective ion channels almost equally permeable to Na+, K+ and Cl- (By similarity).
Required for normal hearing (By similarity).
Necessary for the formation of stereocilia in the inner ear and normal development of the organ of Corti (PubMed:17021174, PubMed:24285636).
Required for the proper localization of PTPRQ and RDX to the stereocilium base during postnatal maturation of hair bundles (PubMed:24285636).
Can insert into membranes and form poorly selective ion channels that may also transport chloride ions (By similarity).
Required for the development and/or maintenance of the proper glomerular endothelial cell and podocyte architecture (By similarity).
Plays a role in formation of the lens suture in the eye, which is important for normal optical properties of the lens (PubMed:29425878).
Catalytic activity
- Na+(in) = Na+(out)
- K+(in) = K+(out)
- chloride(in) = chloride(out)
Activity regulation
Inhibited by F-actin.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | actin cytoskeleton | |
Cellular Component | apical plasma membrane | |
Cellular Component | cell cortex | |
Cellular Component | centrosome | |
Cellular Component | chloride channel complex | |
Cellular Component | cytoplasm | |
Cellular Component | Golgi apparatus | |
Cellular Component | membrane | |
Cellular Component | mitochondrion | |
Cellular Component | plasma membrane | |
Cellular Component | stereocilium | |
Cellular Component | stereocilium base | |
Cellular Component | stereocilium bundle | |
Molecular Function | chloride channel activity | |
Molecular Function | oxidoreductase activity | |
Biological Process | auditory receptor cell stereocilium organization | |
Biological Process | chloride transport | |
Biological Process | diet induced thermogenesis | |
Biological Process | inner ear receptor cell stereocilium organization | |
Biological Process | neuromuscular process controlling balance | |
Biological Process | protein localization | |
Biological Process | response to dietary excess | |
Biological Process | sensory perception of sound | |
Biological Process | visual perception |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameChloride intracellular channel protein 5
- 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 accessionQ8BXK9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Single-pass membrane protein
Apical cell membrane ; Single-pass membrane protein
Note: Colocalized with AKAP9 at the Golgi apparatus as well as, to a lesser extent, the centrosome (By similarity).
Associates with the cortical actin cytoskeleton (By similarity).
Localizes to the apical region of cochlear hair cells, at the base of the actin-rich hair bundle (PubMed:17021174).
Colocalizes with podocalyxin at the apical cell membrane in renal glomeruli (By similarity).
May localize to the centrosome in lens epithelial cells (PubMed:29425878).
Exists both as soluble cytoplasmic protein and as membrane protein with probably a single transmembrane domain (By similarity).
Associates with the cortical actin cytoskeleton (By similarity).
Localizes to the apical region of cochlear hair cells, at the base of the actin-rich hair bundle (PubMed:17021174).
Colocalizes with podocalyxin at the apical cell membrane in renal glomeruli (By similarity).
May localize to the centrosome in lens epithelial cells (PubMed:29425878).
Exists both as soluble cytoplasmic protein and as membrane protein with probably a single transmembrane domain (By similarity).
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 34-54 | Helical; Note=After insertion into the membrane | ||||
Sequence: FSQRLFMILWLKGVVFNVTTV |
Keywords
- Cellular component
Phenotypes & Variants
Involvement in disease
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 16 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000144215 | 1-251 | Chloride intracellular channel protein 5 | |||
Sequence: MTDSATTNGDDRDPEIELFVKAGIDGESIGNCPFSQRLFMILWLKGVVFNVTTVDLKRKPADLHNLAPGTHPPFLTFNGDVKTDVNKIEEFLEETLTPEKYPKLAAKHRESNTAGIDIFSKFSAYIKNTKQQNNAALERGLTKALRKLDDYLNSPLPEEIDTNTHGDEKGSQRKFLDGDELTLADCNLLPKLHVVKIVAKKYRNYDIPAEMTGLWRYLKNAYARDEFTNTCAADSEIELAYADVARRLSRS |
Proteomic databases
PTM databases
Expression
Tissue specificity
Detected in lung and inner ear. Detected in embryonic cochlea, on microvilli-covered apical surfaces of interdental cells, columnar cells of Kolliker's organ, and on stereocilia of inner and outer hair cells (at protein level) (PubMed:17021174).
Also detected in the eye, where it localizes to lens fiber cells in the lens epithelium (at protein level) (PubMed:29425878).
Also detected in the eye, where it localizes to lens fiber cells in the lens epithelium (at protein level) (PubMed:29425878).
Gene expression databases
Interaction
Subunit
Component of a multimeric complex consisting of several cytoskeletal proteins, including actin, ezrin, alpha-actinin, gelsolin, and IQGAP1 (By similarity).
Interacts with AKAP9 (By similarity).
Interacts with TPRN (PubMed:37952086).
TPRN, CLIC5 and PTPQR form concentric rings at the base of stereocilia and may form a complex (PubMed:37952086).
Interacts with EZR, MYO6 and RDX; the proteins may work together as a complex to stabilize linkages between the plasma membrane and subjacent actin cytoskeleton at the stereocilium base (PubMed:24285636).
Interacts with AKAP9 (By similarity).
Interacts with TPRN (PubMed:37952086).
TPRN, CLIC5 and PTPQR form concentric rings at the base of stereocilia and may form a complex (PubMed:37952086).
Interacts with EZR, MYO6 and RDX; the proteins may work together as a complex to stabilize linkages between the plasma membrane and subjacent actin cytoskeleton at the stereocilium base (PubMed:24285636).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, motif, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-98 | Required for insertion into the membrane | ||||
Sequence: MTDSATTNGDDRDPEIELFVKAGIDGESIGNCPFSQRLFMILWLKGVVFNVTTVDLKRKPADLHNLAPGTHPPFLTFNGDVKTDVNKIEEFLEETLTP | ||||||
Motif | 32-35 | G-site | ||||
Sequence: CPFS | ||||||
Domain | 101-241 | GST C-terminal | ||||
Sequence: YPKLAAKHRESNTAGIDIFSKFSAYIKNTKQQNNAALERGLTKALRKLDDYLNSPLPEEIDTNTHGDEKGSQRKFLDGDELTLADCNLLPKLHVVKIVAKKYRNYDIPAEMTGLWRYLKNAYARDEFTNTCAADSEIELAY |
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 chloride 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 (By similarity).
Sequence similarities
Belongs to the chloride channel CLIC family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length251
- Mass (Da)28,287
- Last updated2003-03-01 v1
- Checksum7055A17D22977974
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A668KLB7 | A0A668KLB7_MOUSE | Clic5 | 485 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK046522 EMBL· GenBank· DDBJ | BAC32769.1 EMBL· GenBank· DDBJ | mRNA | ||
AK156849 EMBL· GenBank· DDBJ | BAE33875.1 EMBL· GenBank· DDBJ | mRNA | ||
BC064037 EMBL· GenBank· DDBJ | AAH64037.1 EMBL· GenBank· DDBJ | mRNA |