CLIC1_HUMAN
ID CLIC1_HUMAN Reviewed; 241 AA.
AC O00299; Q15089; Q502X1;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 226.
DE RecName: Full=Chloride intracellular channel protein 1;
DE AltName: Full=Chloride channel ABP;
DE AltName: Full=Nuclear chloride ion channel 27;
DE Short=NCC27;
DE AltName: Full=Regulatory nuclear chloride ion channel protein;
DE Short=hRNCC;
GN Name=CLIC1; Synonyms=G6, NCC27;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Lymphoma;
RX PubMed=9139710; DOI=10.1074/jbc.272.19.12575;
RA Valenzuela S.M., Martin D.K., Por S.B., Robbins J.M., Warton K.,
RA Bootcov M.R., Schofield P.R., Campbell T.J., Breit S.N.;
RT "Molecular cloning and expression of a chloride ion channel of cell
RT nuclei.";
RL J. Biol. Chem. 272:12575-12582(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Thymus;
RA Noh Y.H., Hahn M.J.;
RT "Cloning and sequence analysis of the gene encoding the xxx-binding
RT protein.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10191309; DOI=10.1523/jneurosci.19-08-02919.1999;
RA Chuang J.Z., Milner T.A., Zhu M., Sung C.H.;
RT "A 29 kDa intracellular chloride channel p64H1 is associated with large
RT dense-core vesicles in rat hippocampal neurons.";
RL J. Neurosci. 19:2919-2928(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10384126;
RA Ribas G., Neville M., Wixon J.L., Cheng J., Campbell R.D.;
RT "Genes encoding three new members of the leukocyte antigen 6 superfamily
RT and a novel member of Ig superfamily, together with genes encoding the
RT regulatory nuclear chloride ion channel protein (hRNCC) and an N omega-N
RT omega-dimethylarginine dimethylaminohydrolase homologue, are found in a 30-
RT kb segment of the MHC class III region.";
RL J. Immunol. 163:278-287(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14656967; DOI=10.1101/gr.1736803;
RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D.,
RA Hood L.;
RT "Analysis of the gene-dense major histocompatibility complex class III
RT region and its comparison to mouse.";
RL Genome Res. 13:2621-2636(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Shiina S., Tamiya G., Oka A., Inoko H.;
RT "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP PROTEIN SEQUENCE OF 2-13, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (JUL-2004) to UniProtKB.
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 32-241.
RA Borsani G.;
RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP FUNCTION.
RX PubMed=10834939; DOI=10.1096/fasebj.14.9.1171;
RA Tonini R., Ferroni A., Valenzuela S.M., Warton K., Campbell T.J.,
RA Breit S.N., Mazzanti M.;
RT "Functional characterization of the NCC27 nuclear protein in stable
RT transfected CHO-K1 cells.";
RL FASEB J. 14:1171-1178(2000).
RN [13]
RP FUNCTION.
RX PubMed=11195932; DOI=10.1111/j.1469-7793.2000.00541.x;
RA Valenzuela S.M., Mazzanti M., Tonini R., Qiu M.R., Warton K.,
RA Musgrove E.A., Campbell T.J., Breit S.N.;
RT "The nuclear chloride ion channel NCC27 is involved in regulation of the
RT cell cycle.";
RL J. Physiol. (Lond.) 529:541-552(2000).
RN [14]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=10793131; DOI=10.1091/mbc.11.5.1509;
RA Berryman M., Bretscher A.;
RT "Identification of a novel member of the chloride intracellular channel
RT gene family (CLIC5) that associates with the actin cytoskeleton of
RT placental microvilli.";
RL Mol. Biol. Cell 11:1509-1521(2000).
RN [15]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11940526; DOI=10.1152/ajpcell.00402.2001;
RA Tulk B.M., Kapadia S., Edwards J.C.;
RT "CLIC1 inserts from the aqueous phase into phospholipid membranes, where it
RT functions as an anion channel.";
RL Am. J. Physiol. 282:C1103-C1112(2002).
RN [16]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11978800; DOI=10.1074/jbc.m203666200;
RA Warton K., Tonini R., Fairlie W.D., Matthews J.M., Valenzuela S.M.,
RA Qiu M.R., Wu W.M., Pankhurst S., Bauskin A.R., Harrop S.J., Campbell T.J.,
RA Curmi P.M., Breit S.N., Mazzanti M.;
RT "Recombinant CLIC1 (NCC27) assembles in lipid bilayers via a pH-dependent
RT two-state process to form chloride ion channels with identical
RT characteristics to those observed in Chinese hamster ovary cells expressing
RT CLIC1.";
RL J. Biol. Chem. 277:26003-26011(2002).
RN [17]
RP INTERACTION WITH AKAP9.
RX PubMed=12163479; DOI=10.1074/jbc.m112277200;
RA Shanks R.A., Larocca M.C., Berryman M., Edwards J.C., Urushidani T.,
RA Navarre J., Goldenring J.R.;
RT "AKAP350 at the Golgi apparatus. II. Association of AKAP350 with a novel
RT chloride intracellular channel (CLIC) family member.";
RL J. Biol. Chem. 277:40973-40980(2002).
RN [18]
RP INTERACTION WITH TRAPPC2, AND SUBCELLULAR LOCATION.
RX PubMed=12681486; DOI=10.1016/s0014-5793(03)00228-x;
RA Fan L., Yu W., Zhu X.;
RT "Interaction of sedlin with chloride intracellular channel proteins.";
RL FEBS Lett. 540:77-80(2003).
RN [19]
RP DOMAIN.
RX PubMed=18850721; DOI=10.1021/bi801147r;
RA Fanucchi S., Adamson R.J., Dirr H.W.;
RT "Formation of an unfolding intermediate state of soluble chloride
RT intracellular channel protein CLIC1 at acidic pH.";
RL Biochemistry 47:11674-11681(2008).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-13; LYS-119 AND LYS-131, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121; SER-156 AND SER-211, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [26]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [27]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE,
RP FUNCTION, SUBCELLULAR LOCATION, PREDICTED MEMBRANE TOPOLOGY, AND PREDICTED
RP TRANSMEMBRANE DOMAIN.
RX PubMed=11551966; DOI=10.1074/jbc.m107804200;
RA Harrop S.J., DeMaere M.Z., Fairlie W.D., Reztsova T., Valenzuela S.M.,
RA Mazzanti M., Tonini R., Qiu M.R., Jankova L., Warton K., Bauskin A.R.,
RA Wu W.M., Pankhurst S., Campbell T.J., Breit S.N., Curmi P.M.G.;
RT "Crystal structure of a soluble form of the intracellular chloride ion
RT channel CLIC1 (NCC27) at 1.4-A resolution.";
RL J. Biol. Chem. 276:44993-45000(2001).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS), FUNCTION, SUBUNIT, SUBCELLULAR
RP LOCATION, DOMAIN, MUTAGENESIS OF CYS-24 AND CYS-59, GLUTATHIONYLATION AT
RP CYS-24, DISULFIDE BOND, PREDICTED MEMBRANE TOPOLOGY, AND PREDICTED
RP TRANSMEMBRANE DOMAIN.
RX PubMed=14613939; DOI=10.1074/jbc.m308444200;
RA Littler D.R., Harrop S.J., Fairlie W.D., Brown L.J., Pankhurst G.J.,
RA Pankhurst S., DeMaere M.Z., Campbell T.J., Bauskin A.R., Tonini R.,
RA Mazzanti M., Breit S.N., Curmi P.M.G.;
RT "The intracellular chloride ion channel protein CLIC1 undergoes a redox-
RT controlled structural transition.";
RL J. Biol. Chem. 279:9298-9305(2004).
CC -!- FUNCTION: Can insert into membranes and form chloride ion channels.
CC Channel activity depends on the pH. Membrane insertion seems to be
CC redox-regulated and may occur only under oxydizing conditions. Involved
CC in regulation of the cell cycle. {ECO:0000269|PubMed:10834939,
CC ECO:0000269|PubMed:11195932, ECO:0000269|PubMed:11551966,
CC ECO:0000269|PubMed:11940526, ECO:0000269|PubMed:11978800,
CC ECO:0000269|PubMed:14613939, ECO:0000269|PubMed:9139710}.
CC -!- SUBUNIT: Monomer. Homodimer (in vitro). Interacts with TRAPPC2.
CC Dimerization requires a conformation change that leads to the exposure
CC of a large hydrophobic surface. In vivo, this may lead to membrane
CC insertion. Interacts with AKAP9. {ECO:0000269|PubMed:11551966,
CC ECO:0000269|PubMed:12163479, ECO:0000269|PubMed:12681486,
CC ECO:0000269|PubMed:14613939}.
CC -!- INTERACTION:
CC O00299; O15116: LSM1; NbExp=4; IntAct=EBI-347404, EBI-347619;
CC O00299; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-347404, EBI-16439278;
CC O00299; Q5HYW2: NHSL2; NbExp=3; IntAct=EBI-347404, EBI-2859639;
CC O00299; O75832: PSMD10; NbExp=9; IntAct=EBI-347404, EBI-752185;
CC O00299; Q4KMQ1-2: TPRN; NbExp=8; IntAct=EBI-347404, EBI-11978969;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12681486,
CC ECO:0000269|PubMed:9139710}. Nucleus membrane
CC {ECO:0000269|PubMed:9139710}; Single-pass membrane protein
CC {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:10793131,
CC ECO:0000269|PubMed:11551966, ECO:0000269|PubMed:12681486,
CC ECO:0000269|PubMed:9139710, ECO:0000305|PubMed:11978800,
CC ECO:0000305|PubMed:14613939}. Cell membrane
CC {ECO:0000269|PubMed:11551966, ECO:0000269|PubMed:11940526,
CC ECO:0000269|PubMed:14613939, ECO:0000305|PubMed:11978800}; Single-pass
CC membrane protein {ECO:0000269|PubMed:11551966,
CC ECO:0000269|PubMed:14613939}. Note=Mostly in the nucleus including in
CC the nuclear membrane (PubMed:9139710, PubMed:12681486). Small amount in
CC the cytoplasm and the plasma membrane (PubMed:9139710). Exists both as
CC soluble cytoplasmic protein and as membrane protein with probably a
CC single transmembrane domain (PubMed:11940526, PubMed:11551966,
CC PubMed:14613939). {ECO:0000269|PubMed:11551966,
CC ECO:0000269|PubMed:11940526, ECO:0000269|PubMed:12681486,
CC ECO:0000269|PubMed:14613939, ECO:0000269|PubMed:9139710}.
CC -!- TISSUE SPECIFICITY: Expression is prominent in heart, placenta, liver,
CC kidney and pancreas. {ECO:0000269|PubMed:10793131}.
CC -!- DOMAIN: Members of this family may change from a globular, soluble
CC state to a state where the N-terminal domain is inserted into the
CC membrane and functions as chloride channel. A conformation change of
CC the N-terminal domain is thought to expose hydrophobic surfaces that
CC trigger membrane insertion. {ECO:0000269|PubMed:14613939,
CC ECO:0000269|PubMed:18850721}.
CC -!- PTM: Hydrogen peroxide treatment causes a conformation change, leading
CC to dimerization and formation of an intramolecular disulfide bond
CC between Cys-24 and Cys-59.
CC -!- MISCELLANEOUS: The protein seems to have very low affinity for
CC glutathione, even though glutathione binding was observed in protein
CC crystals.
CC -!- SIMILARITY: Belongs to the chloride channel CLIC family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CLIC1ID50543ch6p21.html";
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DR EMBL; U93205; AAC25675.1; -; mRNA.
DR EMBL; AF034607; AAD20437.1; -; mRNA.
DR EMBL; AF109197; AAD26137.1; -; mRNA.
DR EMBL; AJ012008; CAB46078.1; -; Genomic_DNA.
DR EMBL; CR542071; CAG46868.1; -; mRNA.
DR EMBL; AF129756; AAD18073.1; -; Genomic_DNA.
DR EMBL; BA000025; BAB63376.1; -; Genomic_DNA.
DR EMBL; AL662899; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC064527; AAH64527.1; -; mRNA.
DR EMBL; BC095469; AAH95469.1; -; mRNA.
DR EMBL; X87689; CAA61020.1; -; mRNA.
DR CCDS; CCDS4719.1; -.
DR RefSeq; NP_001274522.1; NM_001287593.1.
DR RefSeq; NP_001274523.1; NM_001287594.1.
DR RefSeq; NP_001279.2; NM_001288.4.
DR PDB; 1K0M; X-ray; 1.40 A; A/B=1-241.
DR PDB; 1K0N; X-ray; 1.80 A; A/B=1-241.
DR PDB; 1K0O; X-ray; 1.75 A; A/B=1-241.
DR PDB; 1RK4; X-ray; 1.79 A; A/B=1-241.
DR PDB; 3O3T; X-ray; 1.70 A; A=1-241.
DR PDB; 3P8W; X-ray; 2.00 A; A=1-241.
DR PDB; 3P90; X-ray; 2.30 A; A=1-241.
DR PDB; 3QR6; X-ray; 1.78 A; A=1-241.
DR PDB; 3SWL; X-ray; 2.35 A; A=6-241.
DR PDB; 3TGZ; X-ray; 2.30 A; A/B=1-241.
DR PDB; 3UVH; X-ray; 1.84 A; A/B=1-241.
DR PDB; 4IQA; X-ray; 2.49 A; A/B=6-241.
DR PDB; 4JZQ; X-ray; 1.35 A; A/B=1-241.
DR PDB; 4K0G; X-ray; 1.40 A; A=2-241.
DR PDB; 4K0N; X-ray; 1.25 A; A=1-241.
DR PDB; 7F8R; X-ray; 2.51 A; A/B=1-241.
DR PDBsum; 1K0M; -.
DR PDBsum; 1K0N; -.
DR PDBsum; 1K0O; -.
DR PDBsum; 1RK4; -.
DR PDBsum; 3O3T; -.
DR PDBsum; 3P8W; -.
DR PDBsum; 3P90; -.
DR PDBsum; 3QR6; -.
DR PDBsum; 3SWL; -.
DR PDBsum; 3TGZ; -.
DR PDBsum; 3UVH; -.
DR PDBsum; 4IQA; -.
DR PDBsum; 4JZQ; -.
DR PDBsum; 4K0G; -.
DR PDBsum; 4K0N; -.
DR PDBsum; 7F8R; -.
DR AlphaFoldDB; O00299; -.
DR SMR; O00299; -.
DR BioGRID; 107604; 128.
DR IntAct; O00299; 61.
DR MINT; O00299; -.
DR STRING; 9606.ENSP00000364935; -.
DR DrugBank; DB11638; Artenimol.
DR DrugBank; DB09130; Copper.
DR TCDB; 1.A.12.1.2; the intracellular chloride channel (clic) family.
DR GlyGen; O00299; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; O00299; -.
DR PhosphoSitePlus; O00299; -.
DR SwissPalm; O00299; -.
DR BioMuta; CLIC1; -.
DR OGP; O00299; -.
DR SWISS-2DPAGE; O00299; -.
DR CPTAC; CPTAC-1393; -.
DR CPTAC; CPTAC-1394; -.
DR CPTAC; CPTAC-1395; -.
DR CPTAC; CPTAC-1396; -.
DR CPTAC; CPTAC-1397; -.
DR EPD; O00299; -.
DR jPOST; O00299; -.
DR MassIVE; O00299; -.
DR PaxDb; O00299; -.
DR PeptideAtlas; O00299; -.
DR PRIDE; O00299; -.
DR ProteomicsDB; 47828; -.
DR TopDownProteomics; O00299; -.
DR Antibodypedia; 27604; 443 antibodies from 39 providers.
DR CPTC; O00299; 2 antibodies.
DR DNASU; 1192; -.
DR Ensembl; ENST00000375779.6; ENSP00000364934.2; ENSG00000213719.8.
DR Ensembl; ENST00000375780.6; ENSP00000364935.2; ENSG00000213719.8.
DR Ensembl; ENST00000375784.7; ENSP00000364940.3; ENSG00000213719.8.
DR Ensembl; ENST00000383404.6; ENSP00000372896.2; ENSG00000206394.8.
DR Ensembl; ENST00000383405.6; ENSP00000372897.2; ENSG00000206394.8.
DR Ensembl; ENST00000395892.5; ENSP00000379229.1; ENSG00000213719.8.
DR Ensembl; ENST00000400052.7; ENSP00000382926.3; ENSG00000206394.8.
DR Ensembl; ENST00000400058.5; ENSP00000382931.1; ENSG00000206394.8.
DR Ensembl; ENST00000415179.5; ENSP00000409247.1; ENSG00000226248.6.
DR Ensembl; ENST00000418285.6; ENSP00000407791.2; ENSG00000226417.6.
DR Ensembl; ENST00000420458.5; ENSP00000410965.1; ENSG00000226651.6.
DR Ensembl; ENST00000422167.6; ENSP00000407429.2; ENSG00000226248.6.
DR Ensembl; ENST00000423055.5; ENSP00000406968.1; ENSG00000226417.6.
DR Ensembl; ENST00000423143.5; ENSP00000404589.1; ENSG00000223639.6.
DR Ensembl; ENST00000423804.5; ENSP00000409979.1; ENSG00000230685.6.
DR Ensembl; ENST00000425464.6; ENSP00000401292.2; ENSG00000223639.6.
DR Ensembl; ENST00000431921.5; ENSP00000408357.1; ENSG00000226248.6.
DR Ensembl; ENST00000433916.5; ENSP00000391395.1; ENSG00000226651.6.
DR Ensembl; ENST00000434202.5; ENSP00000400532.1; ENSG00000226651.6.
DR Ensembl; ENST00000435242.5; ENSP00000412217.1; ENSG00000226417.6.
DR Ensembl; ENST00000438708.5; ENSP00000406088.1; ENSG00000226248.6.
DR Ensembl; ENST00000438750.5; ENSP00000404037.1; ENSG00000223639.6.
DR Ensembl; ENST00000442045.5; ENSP00000400280.1; ENSG00000226417.6.
DR Ensembl; ENST00000447338.5; ENSP00000413330.1; ENSG00000230685.6.
DR Ensembl; ENST00000447369.5; ENSP00000408094.1; ENSG00000230685.6.
DR Ensembl; ENST00000451546.5; ENSP00000416211.1; ENSG00000223639.6.
DR Ensembl; ENST00000456863.6; ENSP00000406335.2; ENSG00000226651.6.
DR Ensembl; ENST00000457485.6; ENSP00000398056.2; ENSG00000230685.6.
DR Ensembl; ENST00000614673.1; ENSP00000480256.1; ENSG00000230685.6.
DR Ensembl; ENST00000614982.1; ENSP00000477623.1; ENSG00000206394.8.
DR Ensembl; ENST00000616760.1; ENSP00000479808.1; ENSG00000213719.8.
DR Ensembl; ENST00000618288.1; ENSP00000479501.1; ENSG00000226417.6.
DR Ensembl; ENST00000619727.1; ENSP00000482255.1; ENSG00000226651.6.
DR Ensembl; ENST00000621055.1; ENSP00000478930.1; ENSG00000226248.6.
DR Ensembl; ENST00000622613.1; ENSP00000484581.1; ENSG00000223639.6.
DR GeneID; 1192; -.
DR KEGG; hsa:1192; -.
DR MANE-Select; ENST00000375784.8; ENSP00000364940.3; NM_001288.6; NP_001279.2.
DR CTD; 1192; -.
DR DisGeNET; 1192; -.
DR GeneCards; CLIC1; -.
DR HGNC; HGNC:2062; CLIC1.
DR HPA; ENSG00000213719; Low tissue specificity.
DR MIM; 602872; gene.
DR neXtProt; NX_O00299; -.
DR OpenTargets; ENSG00000213719; -.
DR PharmGKB; PA26588; -.
DR VEuPathDB; HostDB:ENSG00000213719; -.
DR eggNOG; KOG1422; Eukaryota.
DR GeneTree; ENSGT00940000154708; -.
DR HOGENOM; CLU_061051_1_0_1; -.
DR InParanoid; O00299; -.
DR OMA; EEIHIAY; -.
DR OrthoDB; 974249at2759; -.
DR PhylomeDB; O00299; -.
DR TreeFam; TF315438; -.
DR PathwayCommons; O00299; -.
DR SignaLink; O00299; -.
DR BioGRID-ORCS; 1192; 8 hits in 1077 CRISPR screens.
DR ChiTaRS; CLIC1; human.
DR EvolutionaryTrace; O00299; -.
DR GeneWiki; CLIC1; -.
DR GenomeRNAi; 1192; -.
DR Pharos; O00299; Tbio.
DR PRO; PR:O00299; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; O00299; protein.
DR Bgee; ENSG00000213719; Expressed in granulocyte and 95 other tissues.
DR ExpressionAtlas; O00299; baseline and differential.
DR Genevisible; O00299; HS.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0005903; C:brush border; TAS:UniProtKB.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005635; C:nuclear envelope; IDA:MGI.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031982; C:vesicle; HDA:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0005254; F:chloride channel activity; IDA:MGI.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0006821; P:chloride transport; IDA:MGI.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR GO; GO:0070527; P:platelet aggregation; HMP:UniProtKB.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:InterPro.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; TAS:UniProtKB.
DR InterPro; IPR002946; CLIC.
DR InterPro; IPR030259; CLIC-1.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR43920:SF2; PTHR43920:SF2; 1.
DR Pfam; PF13409; GST_N_2; 1.
DR PRINTS; PR01263; INTCLCHANNEL.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR00862; O-ClC; 1.
DR PROSITE; PS50405; GST_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell membrane; Chloride; Chloride channel;
KW Cytoplasm; Direct protein sequencing; Disulfide bond; Glutathionylation;
KW Ion channel; Ion transport; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.10, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..241
FT /note="Chloride intracellular channel protein 1"
FT /id="PRO_0000144201"
FT TRANSMEM 26..46
FT /note="Helical; Note=After insertion into the membrane"
FT /evidence="ECO:0000255"
FT DOMAIN 93..233
FT /note="GST C-terminal"
FT REGION 2..90
FT /note="Required for insertion into the membrane"
FT BINDING 64
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:11551966"
FT BINDING 77
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:11551966"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.10, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 13
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 24
FT /note="S-glutathionyl cysteine; alternate"
FT /evidence="ECO:0000269|PubMed:14613939"
FT MOD_RES 119
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 131
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 233
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1Q5"
FT DISULFID 24..59
FT /note="Alternate"
FT /evidence="ECO:0000269|PubMed:14613939"
FT MUTAGEN 24
FT /note="C->S: Loss of dimerization and of ion transport
FT activity."
FT /evidence="ECO:0000269|PubMed:14613939"
FT MUTAGEN 59
FT /note="C->S: Loss of dimerization and of ion transport
FT activity."
FT /evidence="ECO:0000269|PubMed:14613939"
FT CONFLICT 63
FT /note="Q -> E (in Ref. 1; AAC25675 and 3; AAD26137)"
FT /evidence="ECO:0000305"
FT STRAND 8..14
FT /evidence="ECO:0007829|PDB:4K0N"
FT STRAND 18..21
FT /evidence="ECO:0007829|PDB:4K0N"
FT HELIX 25..37
FT /evidence="ECO:0007829|PDB:4K0N"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:4K0N"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:1K0N"
FT HELIX 53..58
FT /evidence="ECO:0007829|PDB:4K0N"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:4K0N"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:4K0N"
FT HELIX 77..87
FT /evidence="ECO:0007829|PDB:4K0N"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:4K0N"
FT HELIX 101..104
FT /evidence="ECO:0007829|PDB:4K0N"
FT TURN 105..109
FT /evidence="ECO:0007829|PDB:4K0N"
FT HELIX 110..119
FT /evidence="ECO:0007829|PDB:4K0N"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:4K0N"
FT HELIX 126..145
FT /evidence="ECO:0007829|PDB:4K0N"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:4K0N"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:4JZQ"
FT STRAND 166..172
FT /evidence="ECO:0007829|PDB:4K0N"
FT HELIX 175..195
FT /evidence="ECO:0007829|PDB:4K0N"
FT HELIX 204..214
FT /evidence="ECO:0007829|PDB:4K0N"
FT HELIX 217..220
FT /evidence="ECO:0007829|PDB:4K0N"
FT HELIX 226..232
FT /evidence="ECO:0007829|PDB:4K0N"
FT HELIX 234..237
FT /evidence="ECO:0007829|PDB:4K0N"
SQ SEQUENCE 241 AA; 26923 MW; 163EEB7481826A0A CRC64;
MAEEQPQVEL FVKAGSDGAK IGNCPFSQRL FMVLWLKGVT FNVTTVDTKR RTETVQKLCP
GGQLPFLLYG TEVHTDTNKI EEFLEAVLCP PRYPKLAALN PESNTAGLDI FAKFSAYIKN
SNPALNDNLE KGLLKALKVL DNYLTSPLPE EVDETSAEDE GVSQRKFLDG NELTLADCNL
LPKLHIVQVV CKKYRGFTIP EAFRGVHRYL SNAYAREEFA STCPDDEEIE LAYEQVAKAL
K
