CLIC1_MOUSE
ID CLIC1_MOUSE Reviewed; 241 AA.
AC Q9Z1Q5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Chloride intracellular channel protein 1;
DE AltName: Full=Nuclear chloride ion channel 27;
DE Short=NCC27;
GN Name=Clic1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-233, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-131, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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 (By
CC similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus membrane
CC {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm
CC {ECO:0000250}. Cell membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}. Note=Mostly in the nucleus including in the
CC nuclear membrane. Small amount in the cytoplasm and the plasma
CC membrane. Exists both as soluble cytoplasmic protein and as membrane
CC protein with probably a single transmembrane domain (By similarity).
CC {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the chloride channel CLIC family. {ECO:0000305}.
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DR EMBL; AF109905; AAC84155.1; -; Genomic_DNA.
DR EMBL; BC004658; AAH04658.1; -; mRNA.
DR CCDS; CCDS28675.1; -.
DR RefSeq; NP_254279.1; NM_033444.2.
DR AlphaFoldDB; Q9Z1Q5; -.
DR SMR; Q9Z1Q5; -.
DR BioGRID; 227756; 8.
DR IntAct; Q9Z1Q5; 1.
DR STRING; 10090.ENSMUSP00000007257; -.
DR iPTMnet; Q9Z1Q5; -.
DR PhosphoSitePlus; Q9Z1Q5; -.
DR SwissPalm; Q9Z1Q5; -.
DR REPRODUCTION-2DPAGE; Q9Z1Q5; -.
DR CPTAC; non-CPTAC-3969; -.
DR EPD; Q9Z1Q5; -.
DR jPOST; Q9Z1Q5; -.
DR MaxQB; Q9Z1Q5; -.
DR PaxDb; Q9Z1Q5; -.
DR PRIDE; Q9Z1Q5; -.
DR ProteomicsDB; 283300; -.
DR TopDownProteomics; Q9Z1Q5; -.
DR Antibodypedia; 27604; 443 antibodies from 39 providers.
DR DNASU; 114584; -.
DR Ensembl; ENSMUST00000007257; ENSMUSP00000007257; ENSMUSG00000007041.
DR GeneID; 114584; -.
DR KEGG; mmu:114584; -.
DR UCSC; uc008cfg.1; mouse.
DR CTD; 1192; -.
DR MGI; MGI:2148924; Clic1.
DR VEuPathDB; HostDB:ENSMUSG00000007041; -.
DR eggNOG; KOG1422; Eukaryota.
DR GeneTree; ENSGT00940000154708; -.
DR HOGENOM; CLU_061051_1_0_1; -.
DR InParanoid; Q9Z1Q5; -.
DR OMA; EEIHIAY; -.
DR OrthoDB; 974249at2759; -.
DR PhylomeDB; Q9Z1Q5; -.
DR TreeFam; TF315438; -.
DR BioGRID-ORCS; 114584; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Clic1; mouse.
DR PRO; PR:Q9Z1Q5; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9Z1Q5; protein.
DR Bgee; ENSMUSG00000007041; Expressed in substantia propria of cornea and 245 other tissues.
DR ExpressionAtlas; Q9Z1Q5; baseline and differential.
DR Genevisible; Q9Z1Q5; MM.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0005635; C:nuclear envelope; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005254; F:chloride channel activity; ISO:MGI.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0006821; P:chloride transport; ISO:MGI.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IDA:MGI.
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; IDA:MGI.
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 Acetylation; Cell membrane; Chloride; Chloride channel; Cytoplasm;
KW Disulfide bond; Ion channel; Ion transport; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport; Voltage-gated channel.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O00299"
FT CHAIN 2..241
FT /note="Chloride intracellular channel protein 1"
FT /id="PRO_0000144202"
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 /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O00299"
FT MOD_RES 13
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O00299"
FT MOD_RES 119
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O00299"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00299"
FT MOD_RES 131
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00299"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00299"
FT MOD_RES 233
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT DISULFID 24..59
FT /evidence="ECO:0000250"
SQ SEQUENCE 241 AA; 27013 MW; 0260A9ECEDA51B1C CRC64;
MAEEQPQVEL FVKAGSDGAK IGNCPFSQRL FMVLWLKGVT FNVTTVDTKR RTETVQKLCP
GGQLPFLLYG TEVHTDTNKI EEFLEAMLCP PRYPKLAALN PESNTSGLDI FAKFSAYIKN
SNPALNDNLE KGLLKALKVL DNYLTSPLPE EVDETSAEDE GISQRKFLDG NELTLADCNL
LPKLHIVQVV CKKYRGFTIP EAFRGVHRYL SNAYAREEFA STCPDDEEIE LAYEQVARAL
K
