Q9Z1Q5 · CLIC1_MOUSE

  • Protein
    Chloride intracellular channel protein 1
  • Gene
    Clic1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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).

Catalytic activity

GO annotations

AspectTerm
Cellular Componentchloride channel complex
Cellular Componentcytoplasm
Cellular Componentendoplasmic reticulum
Cellular Componentextracellular exosome
Cellular Componentmembrane
Cellular Componentmitochondrion
Cellular Componentnuclear envelope
Cellular Componentnuclear membrane
Cellular Componentnucleus
Cellular Componentperinuclear region of cytoplasm
Cellular Componentplasma membrane
Molecular Functionchloride channel activity
Molecular Functionoxidoreductase activity
Biological Processchloride transport
Biological Processpositive regulation of osteoblast differentiation
Biological Processregulation of mitochondrial membrane potential

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Chloride intracellular channel protein 1
  • Alternative names
    • Glutaredoxin-like oxidoreductase CLIC1
      (EC:1.8.-.-
      ) . EC:1.8.-.- (UniProtKB | ENZYME | Rhea)
    • Glutathione-dependent dehydroascorbate reductase CLIC1
      (EC:1.8.5.1
      ) . EC:1.8.5.1 (UniProtKB | ENZYME | Rhea)
    • Nuclear chloride ion channel 27 (NCC27)

Gene names

    • Name
      Clic1

Organism names

  • Taxonomic identifier
  • Strains
    • 129
    • FVB/N
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q9Z1Q5

Proteomes

Organism-specific databases

Subcellular Location

Nucleus
Nucleus membrane
; Single-pass membrane protein
Cytoplasm
Cell membrane
; Single-pass membrane protein
Endoplasmic reticulum
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).

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane26-46Helical; Note=After insertion into the membrane

Keywords

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain, disulfide bond.

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylalanine
ChainPRO_00001442022-241Chloride intracellular channel protein 1
Modified residue13N6-acetyllysine
Disulfide bond24↔59
Modified residue119N6-acetyllysine
Modified residue121Phosphoserine
Modified residue131N6-acetyllysine
Modified residue156Phosphoserine
Modified residue211Phosphoserine
Modified residue233Phosphotyrosine

Keywords

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.

TypeIDPosition(s)Description
Region2-90Required for insertion into the membrane
Motif24-27G-site
Domain93-233GST C-terminal

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    241
  • Mass (Da)
    27,013
  • Last updated
    2007-01-23 v3
  • Checksum
    0260A9ECEDA51B1C
MAEEQPQVELFVKAGSDGAKIGNCPFSQRLFMVLWLKGVTFNVTTVDTKRRTETVQKLCPGGQLPFLLYGTEVHTDTNKIEEFLEAMLCPPRYPKLAALNPESNTSGLDIFAKFSAYIKNSNPALNDNLEKGLLKALKVLDNYLTSPLPEEVDETSAEDEGISQRKFLDGNELTLADCNLLPKLHIVQVVCKKYRGFTIPEAFRGVHRYLSNAYAREEFASTCPDDEEIELAYEQVARALK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF109905
EMBL· GenBank· DDBJ
AAC84155.1
EMBL· GenBank· DDBJ
Genomic DNA
BC004658
EMBL· GenBank· DDBJ
AAH04658.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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