Chloride intracellular channel protein 1 (CLIC1)

The protein contains 241 amino acids for an estimated molecular weight of 26923 Da.

 

Can insert into membranes and form chloride ion channels. Channel activity depends on the pH. Membrane insertion seems to be redox-regulated and may occur only under oxydizing conditions. Involved in regulation of the cell cycle. (updated: April 1, 2015)

Protein identification was indicated in the following studies:

  1. Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
  2. Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
  3. Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
  4. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  5. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.

Methods

The following articles were analysed to gather the proteome content of erythrocytes.

The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete
TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry

The compilation of older studies can be retrieved from the Red Blood Cell Collection database.

The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.

No sequence conservation computed yet.

This protein is annotated as membranous in Gene Ontology, is annotated as membranous in UniProt.


Interpro domains
Total structural coverage: 100%
Model score: 100
No model available.

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The reference OMIM entry for this protein is 602872

Chloride intracellular channel 1; clic1
Ncc27

CLONING

Ion channels are present on the plasma membrane of virtually all cells and have been found on the membranes of various organelles. Valenzuela et al. (1997) identified a cDNA encoding a nuclear chloride channel protein, CLIC1, which they called NCC27. The predicted 241-amino acid protein is 57% identical to a bovine chloride channel protein, p64, thought to localize to organelles. NCC27 contains 2 putative transmembrane domains and 2 putative nuclear localization sequences. It migrated as a 27-kD protein on Western blots of mammalian cell extracts. Using immunohistochemistry, Valenzuela et al. (1997) showed that NCC27 localized principally to the nucleus and nuclear membrane in Chinese hamster ovary (CHO) cells. Northern blot analysis showed that NCC27 was expressed as 1.0- and 1.2-kb mRNAs in various cells and cell lines.

GENE FUNCTION

Valenzuela et al. (1997) used patch clamp studies of CHO cells expressing NCC27 and observed an increased level of chloride ion channel activity at their nuclear membrane. Singh et al. (2007) showed that recombinant human CLIC1 mediated a single-channel current when reconstituted on a planar lipid bilayer. Currents produced by CLIC1 and by CLIC5 (607293) were strongly and reversibly inactivated by addition of purified platelet F-actin (see 102560) to the cytosolic face of the bilayer. Inhibition by F-actin was reversed by disruption of F-actin. ... More on the omim web site

Subscribe to this protein entry history

Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated

Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated

Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 602872 was added.

Jan. 27, 2016: Protein entry updated
Automatic update: model status changed

Jan. 24, 2016: Protein entry updated
Automatic update: model status changed