Clic5
entrez
224796
canonical
uniprot
Q8BXK9
canonical
ensembl
ENSMUSG00000023959
resolver
ensp
ENSMUSP00000024755
resolver
ensp
ENSMUSP00000159274
resolver
enst
ENSMUST00000024755
resolver
enst
ENSMUST00000239215
resolver
genesymbol
Clic5
resolver
uniprot
A0A668KLB7
resolver
uniprot
Q3U0H8
resolver
uniprot_entry
A0A668KLB7_MOUSE
resolver
uniprot_entry
CLIC5_MOUSE
resolver
uniprot_sec
Q3U0H8
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by F-actin. {ECO:0000250|UniProtKB:Q9NZA1}.
uniprot
proteins
amino_acid_sequence
MTDSATTNGDDRDPEIELFVKAGIDGESIGNCPFSQRLFMILWLKGVVFNVTTVDLKRKPADLHNLAPGTHPPFLTFNGDVKTDVNKIEEFLEETLTPEKYPKLAAKHRESNTAGIDIFSKFSAYIKNTKQQNNAALERGLTKALRKLDDYLNSPLPEEIDTNTHGDEKGSQRKFLDGDELTLADCNLLPKLHVVKIVAKKYRNYDIPAEMTGLWRYLKNAYARDEFTNTCAADSEIELAYADVARRLSRS
uniprot
proteins
disease_involvement
DISEASE: Note=Defects in Clic5 are a cause of the jitterbug (jbg) phenotype (PubMed:17021174, PubMed:24285636). Jbg is the result of a spontaneous mutation that leads to severe degeneration of the organ of Corti in the inner ear (PubMed:17021174). Jbg leads to progressive degeneration of inner ear hair cells (PubMed:17021174, PubMed:24285636). Affected mice are identified by head bobbing, circling behavior and their inability to swim (PubMed:17021174). They cannot hear well when young, and become completely deaf after 5 months (PubMed:17021174). In addition, there are eye defects with aberrant development of the lens suture and formation of lens opacities (PubMed:29425878). {ECO:0000269|PubMed:17021174, ECO:0000269|PubMed:24285636, ECO:0000269|PubMed:29425878}.
uniprot
proteins
ec_number
1.8.-.-
uniprot
proteins
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). {ECO:0000250|UniProtKB:O00299, ECO:0000250|UniProtKB:Q9NZA1, ECO:0000269|PubMed:17021174, ECO:0000269|PubMed:24285636, ECO:0000269|PubMed:29425878}.
uniprot
proteins
mass_dalton
28287
uniprot
proteins
protein_family
Chloride channel CLIC family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17021174
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
24285636
uniprot
proteins
pubmed
29425878
uniprot
proteins
pubmed
37952086
uniprot
proteins
sequence_length
251
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:Q9NZA1}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:29425878}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9NZA1}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q9NZA1}. Membrane {ECO:0000250|UniProtKB:Q9NZA1}; Single-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:17021174}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:O00299}. Mitochondrion {ECO:0000250|UniProtKB:Q9EPT8}. Cell projection, stereocilium {ECO:0000269|PubMed:17021174, ECO:0000269|PubMed:24285636, ECO:0000269|PubMed:37952086}. 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). {ECO:0000250|UniProtKB:O00299, ECO:0000250|UniProtKB:Q9NZA1, ECO:0000269|PubMed:17021174, ECO:0000269|PubMed:29425878}.
uniprot
proteins
transmembrane_region
TRANSMEM 34..54; /note="Helical; Note=After insertion into the membrane"; /evidence="ECO:0000255
uniprot
proteins