Full text data of CLIC1
CLIC1
(G6, NCC27)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Chloride intracellular channel protein 1 (Chloride channel ABP; Nuclear chloride ion channel 27; NCC27; Regulatory nuclear chloride ion channel protein; hRNCC)
Chloride intracellular channel protein 1 (Chloride channel ABP; Nuclear chloride ion channel 27; NCC27; Regulatory nuclear chloride ion channel protein; hRNCC)
hRBCD
IPI00010896
IPI00010896 Chloride intraCellular Channel 1 Seems to act as a chloride ion channel. soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a nuclear n/a expected molecular weight found in band found in band between 49 - 62 kdDa
IPI00010896 Chloride intraCellular Channel 1 Seems to act as a chloride ion channel. soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a nuclear n/a expected molecular weight found in band found in band between 49 - 62 kdDa
UniProt
O00299
ID CLIC1_HUMAN Reviewed; 241 AA.
AC O00299; Q15089; Q502X1;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 149.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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;
RA Chuang J.Z., Milner T.A., Zhu M., Sung C.H.;
RT "A 29 kDa intracellular chloride channel p64H1 is associated with
RT large 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
RT superfamily and a novel member of Ig superfamily, together with genes
RT encoding the regulatory nuclear chloride ion channel protein (hRNCC)
RT and an N omega-N omega-dimethylarginine dimethylaminohydrolase
RT homologue, are found in a 30-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.,
RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA Korn B., Zuo D., Hu Y., 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.,
RA Campbell R.D., 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.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA 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.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP PROTEIN SEQUENCE OF 2-13, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND 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;
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
RT the 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
RT channel gene family (CLIC5) that associates with the actin
RT cytoskeleton of 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,
RT where it functions as an anion channel.";
RL Am. J. Physiol. 282:C1103-C1112(2002).
RN [16]
RP FUNCTION.
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.,
RA Campbell T.J., Curmi P.M., Breit S.N., Mazzanti M.;
RT "Recombinant CLIC1 (NCC27) assembles in lipid bilayers via a pH-
RT dependent two-state process to form chloride ion channels with
RT identical characteristics to those observed in Chinese hamster ovary
RT cells expressing CLIC1.";
RL J. Biol. Chem. 277:26003-26011(2002).
RN [17]
RP INTERACTION WITH 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
RT novel 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, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; LYS-13; LYS-119; LYS-131
RP AND LYS-135, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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.,
RA Buerckstuemmer T., 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, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE,
RP FUNCTION, SUBCELLULAR LOCATION, PREDICTED MEMBRANE TOPOLOGY, AND
RP PREDICTED 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 [25]
RP X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS), FUNCTION, SUBUNIT, DOMAIN,
RP MUTAGENESIS OF CYS-24 AND CYS-59, DISULFIDE BOND, PREDICTED MEMBRANE
RP TOPOLOGY, AND PREDICTED 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
RT redox-controlled structural transition.";
RL J. Biol. Chem. 279:9298-9305(2004).
CC -!- FUNCTION: Can insert into membranes and form chloride ion
CC channels. Channel activity depends on the pH. Membrane insertion
CC seems to be redox-regulated and may occur only under oxydizing
CC conditions. Involved in regulation of the cell cycle.
CC -!- SUBUNIT: Monomer. Homodimer (in vitro). Interacts with TRAPPC2.
CC Dimerization requires a conformation change that leads to the
CC exposure of a large hydrophobic surface. In vivo, this may lead to
CC membrane insertion. Interacts with AKAP9.
CC -!- SUBCELLULAR LOCATION: Nucleus. Nucleus membrane; Single-pass
CC membrane protein (Probable). Cytoplasm. Cell membrane; Single-pass
CC membrane protein (Probable). Note=Mostly in the nucleus including
CC in the nuclear membrane. Small amount in the cytoplasm and the
CC plasma membrane. Exists both as soluble cytoplasmic protein and as
CC membrane protein with probably a single transmembrane domain.
CC -!- TISSUE SPECIFICITY: Expression is prominent in heart, placenta,
CC liver, kidney and pancreas.
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
CC of the N-terminal domain is thought to expose hydrophobic surfaces
CC that trigger membrane insertion.
CC -!- PTM: Hydrogen peroxide treatment causes a conformation change,
CC leading to dimerization and formation of an intramolecular
CC disulfide bond 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
CC protein crystals.
CC -!- SIMILARITY: Belongs to the chloride channel CLIC family.
CC -!- SIMILARITY: Contains 1 GST C-terminal domain.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and 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; CAI18417.1; -; Genomic_DNA.
DR EMBL; BC064527; AAH64527.1; -; mRNA.
DR EMBL; BC095469; AAH95469.1; -; mRNA.
DR EMBL; X87689; CAA61020.1; -; mRNA.
DR RefSeq; NP_001279.2; NM_001288.4.
DR RefSeq; XP_005248901.1; XM_005248844.1.
DR RefSeq; XP_005248902.1; XM_005248845.1.
DR RefSeq; XP_005272827.1; XM_005272770.1.
DR RefSeq; XP_005272828.1; XM_005272771.1.
DR RefSeq; XP_005274973.1; XM_005274916.1.
DR RefSeq; XP_005274974.1; XM_005274917.1.
DR RefSeq; XP_005275136.1; XM_005275079.1.
DR RefSeq; XP_005275137.1; XM_005275080.1.
DR RefSeq; XP_005275269.1; XM_005275212.1.
DR RefSeq; XP_005275270.1; XM_005275213.1.
DR RefSeq; XP_005275405.1; XM_005275348.1.
DR RefSeq; XP_005275406.1; XM_005275349.1.
DR RefSeq; XP_005275567.1; XM_005275510.1.
DR RefSeq; XP_005275568.1; XM_005275511.1.
DR UniGene; Hs.414565; -.
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 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 ProteinModelPortal; O00299; -.
DR SMR; O00299; 22-234.
DR IntAct; O00299; 26.
DR MINT; MINT-1033423; -.
DR STRING; 9606.ENSP00000406335; -.
DR TCDB; 1.A.12.1.2; the intracellular chloride channel (clic) family.
DR PhosphoSite; O00299; -.
DR OGP; O00299; -.
DR SWISS-2DPAGE; O00299; -.
DR PaxDb; O00299; -.
DR PRIDE; O00299; -.
DR DNASU; 1192; -.
DR Ensembl; ENST00000375779; ENSP00000364934; ENSG00000213719.
DR Ensembl; ENST00000375780; ENSP00000364935; ENSG00000213719.
DR Ensembl; ENST00000375784; ENSP00000364940; ENSG00000213719.
DR Ensembl; ENST00000383404; ENSP00000372896; ENSG00000206394.
DR Ensembl; ENST00000383405; ENSP00000372897; ENSG00000206394.
DR Ensembl; ENST00000395892; ENSP00000379229; ENSG00000213719.
DR Ensembl; ENST00000400052; ENSP00000382926; ENSG00000206394.
DR Ensembl; ENST00000400058; ENSP00000382931; ENSG00000206394.
DR Ensembl; ENST00000415179; ENSP00000409247; ENSG00000226248.
DR Ensembl; ENST00000418285; ENSP00000407791; ENSG00000226417.
DR Ensembl; ENST00000420458; ENSP00000410965; ENSG00000226651.
DR Ensembl; ENST00000422167; ENSP00000407429; ENSG00000226248.
DR Ensembl; ENST00000423055; ENSP00000406968; ENSG00000226417.
DR Ensembl; ENST00000423143; ENSP00000404589; ENSG00000223639.
DR Ensembl; ENST00000423804; ENSP00000409979; ENSG00000230685.
DR Ensembl; ENST00000425464; ENSP00000401292; ENSG00000223639.
DR Ensembl; ENST00000431921; ENSP00000408357; ENSG00000226248.
DR Ensembl; ENST00000433916; ENSP00000391395; ENSG00000226651.
DR Ensembl; ENST00000434202; ENSP00000400532; ENSG00000226651.
DR Ensembl; ENST00000435242; ENSP00000412217; ENSG00000226417.
DR Ensembl; ENST00000438708; ENSP00000406088; ENSG00000226248.
DR Ensembl; ENST00000438750; ENSP00000404037; ENSG00000223639.
DR Ensembl; ENST00000442045; ENSP00000400280; ENSG00000226417.
DR Ensembl; ENST00000447338; ENSP00000413330; ENSG00000230685.
DR Ensembl; ENST00000447369; ENSP00000408094; ENSG00000230685.
DR Ensembl; ENST00000451546; ENSP00000416211; ENSG00000223639.
DR Ensembl; ENST00000456863; ENSP00000406335; ENSG00000226651.
DR Ensembl; ENST00000457485; ENSP00000398056; ENSG00000230685.
DR GeneID; 1192; -.
DR KEGG; hsa:1192; -.
DR UCSC; uc003nwr.3; human.
DR CTD; 1192; -.
DR GeneCards; GC06M031698; -.
DR GeneCards; GC06Mj31685; -.
DR GeneCards; GC06Mk31680; -.
DR GeneCards; GC06Ml31737; -.
DR GeneCards; GC06Mm31774; -.
DR GeneCards; GC06Mn31688; -.
DR GeneCards; GC06Mo31688; -.
DR HGNC; HGNC:2062; CLIC1.
DR HPA; CAB020825; -.
DR HPA; CAB040557; -.
DR MIM; 602872; gene.
DR neXtProt; NX_O00299; -.
DR PharmGKB; PA26588; -.
DR eggNOG; NOG332015; -.
DR HOGENOM; HOG000231548; -.
DR HOVERGEN; HBG050994; -.
DR InParanoid; O00299; -.
DR KO; K05021; -.
DR OMA; LWRYLNA; -.
DR OrthoDB; EOG7X3QR3; -.
DR PhylomeDB; O00299; -.
DR SignaLink; O00299; -.
DR ChiTaRS; CLIC1; human.
DR EvolutionaryTrace; O00299; -.
DR GeneWiki; CLIC1; -.
DR GenomeRNAi; 1192; -.
DR NextBio; 4928; -.
DR PRO; PR:O00299; -.
DR ArrayExpress; O00299; -.
DR Bgee; O00299; -.
DR CleanEx; HS_CLIC1; -.
DR Genevestigator; O00299; -.
DR GO; GO:0005903; C:brush border; TAS:UniProtKB.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
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:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005254; F:chloride channel activity; IDA:MGI.
DR GO; GO:0005247; F:voltage-gated chloride channel activity; IEA:InterPro.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; TAS:UniProtKB.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.30.10; -; 1.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR002946; Int_Cl_channel.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR PANTHER; PTHR11260:SF1; PTHR11260:SF1; 1.
DR Pfam; PF13409; GST_N_2; 1.
DR PRINTS; PR01263; INTCLCHANNEL.
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 Complete proteome; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; Glutathionylation; Ion channel; Ion transport;
KW Membrane; Nucleus; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 241 Chloride intracellular channel protein 1.
FT /FTId=PRO_0000144201.
FT TRANSMEM 26 46 Helical; Note=After insertion into the
FT membrane; (Potential).
FT DOMAIN 93 233 GST C-terminal.
FT REGION 2 90 Required for insertion into the membrane.
FT BINDING 64 64 Glutathione; via carbonyl oxygen.
FT BINDING 77 77 Glutathione.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 13 13 N6-acetyllysine.
FT MOD_RES 24 24 S-glutathionyl cysteine.
FT MOD_RES 119 119 N6-acetyllysine.
FT MOD_RES 131 131 N6-acetyllysine.
FT MOD_RES 135 135 N6-acetyllysine.
FT MOD_RES 233 233 Phosphotyrosine (By similarity).
FT DISULFID 24 59
FT MUTAGEN 24 24 C->S: Loss of dimerization and of ion
FT transport activity.
FT MUTAGEN 59 59 C->S: Loss of dimerization and of ion
FT transport activity.
FT CONFLICT 63 63 Q -> E (in Ref. 1; AAC25675 and 3;
FT AAD26137).
FT STRAND 8 14
FT STRAND 18 21
FT HELIX 25 37
FT STRAND 42 46
FT STRAND 48 50
FT HELIX 53 58
FT STRAND 64 69
FT STRAND 72 75
FT HELIX 77 87
FT TURN 90 92
FT HELIX 101 104
FT TURN 105 109
FT HELIX 110 119
FT HELIX 123 145
FT HELIX 149 151
FT HELIX 156 160
FT STRAND 166 172
FT HELIX 175 195
FT HELIX 204 214
FT HELIX 217 220
FT HELIX 226 232
FT TURN 233 236
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
//
ID CLIC1_HUMAN Reviewed; 241 AA.
AC O00299; Q15089; Q502X1;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 149.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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;
RA Chuang J.Z., Milner T.A., Zhu M., Sung C.H.;
RT "A 29 kDa intracellular chloride channel p64H1 is associated with
RT large 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
RT superfamily and a novel member of Ig superfamily, together with genes
RT encoding the regulatory nuclear chloride ion channel protein (hRNCC)
RT and an N omega-N omega-dimethylarginine dimethylaminohydrolase
RT homologue, are found in a 30-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.,
RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA Korn B., Zuo D., Hu Y., 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.,
RA Campbell R.D., 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.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA 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.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP PROTEIN SEQUENCE OF 2-13, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND 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;
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
RT the 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
RT channel gene family (CLIC5) that associates with the actin
RT cytoskeleton of 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,
RT where it functions as an anion channel.";
RL Am. J. Physiol. 282:C1103-C1112(2002).
RN [16]
RP FUNCTION.
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.,
RA Campbell T.J., Curmi P.M., Breit S.N., Mazzanti M.;
RT "Recombinant CLIC1 (NCC27) assembles in lipid bilayers via a pH-
RT dependent two-state process to form chloride ion channels with
RT identical characteristics to those observed in Chinese hamster ovary
RT cells expressing CLIC1.";
RL J. Biol. Chem. 277:26003-26011(2002).
RN [17]
RP INTERACTION WITH 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
RT novel 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, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; LYS-13; LYS-119; LYS-131
RP AND LYS-135, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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.,
RA Buerckstuemmer T., 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, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE,
RP FUNCTION, SUBCELLULAR LOCATION, PREDICTED MEMBRANE TOPOLOGY, AND
RP PREDICTED 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 [25]
RP X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS), FUNCTION, SUBUNIT, DOMAIN,
RP MUTAGENESIS OF CYS-24 AND CYS-59, DISULFIDE BOND, PREDICTED MEMBRANE
RP TOPOLOGY, AND PREDICTED 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
RT redox-controlled structural transition.";
RL J. Biol. Chem. 279:9298-9305(2004).
CC -!- FUNCTION: Can insert into membranes and form chloride ion
CC channels. Channel activity depends on the pH. Membrane insertion
CC seems to be redox-regulated and may occur only under oxydizing
CC conditions. Involved in regulation of the cell cycle.
CC -!- SUBUNIT: Monomer. Homodimer (in vitro). Interacts with TRAPPC2.
CC Dimerization requires a conformation change that leads to the
CC exposure of a large hydrophobic surface. In vivo, this may lead to
CC membrane insertion. Interacts with AKAP9.
CC -!- SUBCELLULAR LOCATION: Nucleus. Nucleus membrane; Single-pass
CC membrane protein (Probable). Cytoplasm. Cell membrane; Single-pass
CC membrane protein (Probable). Note=Mostly in the nucleus including
CC in the nuclear membrane. Small amount in the cytoplasm and the
CC plasma membrane. Exists both as soluble cytoplasmic protein and as
CC membrane protein with probably a single transmembrane domain.
CC -!- TISSUE SPECIFICITY: Expression is prominent in heart, placenta,
CC liver, kidney and pancreas.
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
CC of the N-terminal domain is thought to expose hydrophobic surfaces
CC that trigger membrane insertion.
CC -!- PTM: Hydrogen peroxide treatment causes a conformation change,
CC leading to dimerization and formation of an intramolecular
CC disulfide bond 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
CC protein crystals.
CC -!- SIMILARITY: Belongs to the chloride channel CLIC family.
CC -!- SIMILARITY: Contains 1 GST C-terminal domain.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and 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; CAI18417.1; -; Genomic_DNA.
DR EMBL; BC064527; AAH64527.1; -; mRNA.
DR EMBL; BC095469; AAH95469.1; -; mRNA.
DR EMBL; X87689; CAA61020.1; -; mRNA.
DR RefSeq; NP_001279.2; NM_001288.4.
DR RefSeq; XP_005248901.1; XM_005248844.1.
DR RefSeq; XP_005248902.1; XM_005248845.1.
DR RefSeq; XP_005272827.1; XM_005272770.1.
DR RefSeq; XP_005272828.1; XM_005272771.1.
DR RefSeq; XP_005274973.1; XM_005274916.1.
DR RefSeq; XP_005274974.1; XM_005274917.1.
DR RefSeq; XP_005275136.1; XM_005275079.1.
DR RefSeq; XP_005275137.1; XM_005275080.1.
DR RefSeq; XP_005275269.1; XM_005275212.1.
DR RefSeq; XP_005275270.1; XM_005275213.1.
DR RefSeq; XP_005275405.1; XM_005275348.1.
DR RefSeq; XP_005275406.1; XM_005275349.1.
DR RefSeq; XP_005275567.1; XM_005275510.1.
DR RefSeq; XP_005275568.1; XM_005275511.1.
DR UniGene; Hs.414565; -.
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 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 ProteinModelPortal; O00299; -.
DR SMR; O00299; 22-234.
DR IntAct; O00299; 26.
DR MINT; MINT-1033423; -.
DR STRING; 9606.ENSP00000406335; -.
DR TCDB; 1.A.12.1.2; the intracellular chloride channel (clic) family.
DR PhosphoSite; O00299; -.
DR OGP; O00299; -.
DR SWISS-2DPAGE; O00299; -.
DR PaxDb; O00299; -.
DR PRIDE; O00299; -.
DR DNASU; 1192; -.
DR Ensembl; ENST00000375779; ENSP00000364934; ENSG00000213719.
DR Ensembl; ENST00000375780; ENSP00000364935; ENSG00000213719.
DR Ensembl; ENST00000375784; ENSP00000364940; ENSG00000213719.
DR Ensembl; ENST00000383404; ENSP00000372896; ENSG00000206394.
DR Ensembl; ENST00000383405; ENSP00000372897; ENSG00000206394.
DR Ensembl; ENST00000395892; ENSP00000379229; ENSG00000213719.
DR Ensembl; ENST00000400052; ENSP00000382926; ENSG00000206394.
DR Ensembl; ENST00000400058; ENSP00000382931; ENSG00000206394.
DR Ensembl; ENST00000415179; ENSP00000409247; ENSG00000226248.
DR Ensembl; ENST00000418285; ENSP00000407791; ENSG00000226417.
DR Ensembl; ENST00000420458; ENSP00000410965; ENSG00000226651.
DR Ensembl; ENST00000422167; ENSP00000407429; ENSG00000226248.
DR Ensembl; ENST00000423055; ENSP00000406968; ENSG00000226417.
DR Ensembl; ENST00000423143; ENSP00000404589; ENSG00000223639.
DR Ensembl; ENST00000423804; ENSP00000409979; ENSG00000230685.
DR Ensembl; ENST00000425464; ENSP00000401292; ENSG00000223639.
DR Ensembl; ENST00000431921; ENSP00000408357; ENSG00000226248.
DR Ensembl; ENST00000433916; ENSP00000391395; ENSG00000226651.
DR Ensembl; ENST00000434202; ENSP00000400532; ENSG00000226651.
DR Ensembl; ENST00000435242; ENSP00000412217; ENSG00000226417.
DR Ensembl; ENST00000438708; ENSP00000406088; ENSG00000226248.
DR Ensembl; ENST00000438750; ENSP00000404037; ENSG00000223639.
DR Ensembl; ENST00000442045; ENSP00000400280; ENSG00000226417.
DR Ensembl; ENST00000447338; ENSP00000413330; ENSG00000230685.
DR Ensembl; ENST00000447369; ENSP00000408094; ENSG00000230685.
DR Ensembl; ENST00000451546; ENSP00000416211; ENSG00000223639.
DR Ensembl; ENST00000456863; ENSP00000406335; ENSG00000226651.
DR Ensembl; ENST00000457485; ENSP00000398056; ENSG00000230685.
DR GeneID; 1192; -.
DR KEGG; hsa:1192; -.
DR UCSC; uc003nwr.3; human.
DR CTD; 1192; -.
DR GeneCards; GC06M031698; -.
DR GeneCards; GC06Mj31685; -.
DR GeneCards; GC06Mk31680; -.
DR GeneCards; GC06Ml31737; -.
DR GeneCards; GC06Mm31774; -.
DR GeneCards; GC06Mn31688; -.
DR GeneCards; GC06Mo31688; -.
DR HGNC; HGNC:2062; CLIC1.
DR HPA; CAB020825; -.
DR HPA; CAB040557; -.
DR MIM; 602872; gene.
DR neXtProt; NX_O00299; -.
DR PharmGKB; PA26588; -.
DR eggNOG; NOG332015; -.
DR HOGENOM; HOG000231548; -.
DR HOVERGEN; HBG050994; -.
DR InParanoid; O00299; -.
DR KO; K05021; -.
DR OMA; LWRYLNA; -.
DR OrthoDB; EOG7X3QR3; -.
DR PhylomeDB; O00299; -.
DR SignaLink; O00299; -.
DR ChiTaRS; CLIC1; human.
DR EvolutionaryTrace; O00299; -.
DR GeneWiki; CLIC1; -.
DR GenomeRNAi; 1192; -.
DR NextBio; 4928; -.
DR PRO; PR:O00299; -.
DR ArrayExpress; O00299; -.
DR Bgee; O00299; -.
DR CleanEx; HS_CLIC1; -.
DR Genevestigator; O00299; -.
DR GO; GO:0005903; C:brush border; TAS:UniProtKB.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
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:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005254; F:chloride channel activity; IDA:MGI.
DR GO; GO:0005247; F:voltage-gated chloride channel activity; IEA:InterPro.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; TAS:UniProtKB.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.30.10; -; 1.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR002946; Int_Cl_channel.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR PANTHER; PTHR11260:SF1; PTHR11260:SF1; 1.
DR Pfam; PF13409; GST_N_2; 1.
DR PRINTS; PR01263; INTCLCHANNEL.
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 Complete proteome; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; Glutathionylation; Ion channel; Ion transport;
KW Membrane; Nucleus; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 241 Chloride intracellular channel protein 1.
FT /FTId=PRO_0000144201.
FT TRANSMEM 26 46 Helical; Note=After insertion into the
FT membrane; (Potential).
FT DOMAIN 93 233 GST C-terminal.
FT REGION 2 90 Required for insertion into the membrane.
FT BINDING 64 64 Glutathione; via carbonyl oxygen.
FT BINDING 77 77 Glutathione.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 13 13 N6-acetyllysine.
FT MOD_RES 24 24 S-glutathionyl cysteine.
FT MOD_RES 119 119 N6-acetyllysine.
FT MOD_RES 131 131 N6-acetyllysine.
FT MOD_RES 135 135 N6-acetyllysine.
FT MOD_RES 233 233 Phosphotyrosine (By similarity).
FT DISULFID 24 59
FT MUTAGEN 24 24 C->S: Loss of dimerization and of ion
FT transport activity.
FT MUTAGEN 59 59 C->S: Loss of dimerization and of ion
FT transport activity.
FT CONFLICT 63 63 Q -> E (in Ref. 1; AAC25675 and 3;
FT AAD26137).
FT STRAND 8 14
FT STRAND 18 21
FT HELIX 25 37
FT STRAND 42 46
FT STRAND 48 50
FT HELIX 53 58
FT STRAND 64 69
FT STRAND 72 75
FT HELIX 77 87
FT TURN 90 92
FT HELIX 101 104
FT TURN 105 109
FT HELIX 110 119
FT HELIX 123 145
FT HELIX 149 151
FT HELIX 156 160
FT STRAND 166 172
FT HELIX 175 195
FT HELIX 204 214
FT HELIX 217 220
FT HELIX 226 232
FT TURN 233 236
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
//
MIM
602872
*RECORD*
*FIELD* NO
602872
*FIELD* TI
*602872 CHLORIDE INTRACELLULAR CHANNEL 1; CLIC1
;;NCC27
*FIELD* TX
CLONING
Ion channels are present on the plasma membrane of virtually all cells
read moreand 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.
*FIELD* RF
1. Singh, H.; Cousin, M. A.; Ashley, R. H.: Functional reconstitution
of mammalian 'chloride intracellular channels' CLIC1, CLIC4 and CLIC5
reveals differential regulation by cytoskeletal actin. FEBS J. 274:
6306-6316, 2007.
2. Valenzuela, S. M.; Martin, D. K.; Por, S. B.; Robbins, J. M.; Warton,
K.; Bootcov, M. R.; Schofield, P. R.; Campbell, T. J.; Breit, S. N.
: Molecular cloning and expression of a chloride ion channel of cell
nuclei. J. Biol. Chem. 272: 12575-12582, 1997.
*FIELD* CN
Patricia A. Hartz - updated: 10/28/2010
*FIELD* CD
Rebekah S. Rasooly: 7/21/1998
*FIELD* ED
mgross: 11/19/2010
terry: 10/28/2010
alopez: 7/21/1998
*RECORD*
*FIELD* NO
602872
*FIELD* TI
*602872 CHLORIDE INTRACELLULAR CHANNEL 1; CLIC1
;;NCC27
*FIELD* TX
CLONING
Ion channels are present on the plasma membrane of virtually all cells
read moreand 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.
*FIELD* RF
1. Singh, H.; Cousin, M. A.; Ashley, R. H.: Functional reconstitution
of mammalian 'chloride intracellular channels' CLIC1, CLIC4 and CLIC5
reveals differential regulation by cytoskeletal actin. FEBS J. 274:
6306-6316, 2007.
2. Valenzuela, S. M.; Martin, D. K.; Por, S. B.; Robbins, J. M.; Warton,
K.; Bootcov, M. R.; Schofield, P. R.; Campbell, T. J.; Breit, S. N.
: Molecular cloning and expression of a chloride ion channel of cell
nuclei. J. Biol. Chem. 272: 12575-12582, 1997.
*FIELD* CN
Patricia A. Hartz - updated: 10/28/2010
*FIELD* CD
Rebekah S. Rasooly: 7/21/1998
*FIELD* ED
mgross: 11/19/2010
terry: 10/28/2010
alopez: 7/21/1998