ID CLIC4_HUMAN Reviewed; 253 AA.
AC Q9Y696; Q9UFW9; Q9UQJ6;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 27-MAR-2024, entry version 206.
DE RecName: Full=Chloride intracellular channel protein 4;
DE AltName: Full=Intracellular chloride ion channel protein p64H1;
GN Name=CLIC4;
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].
RX PubMed=10070163; DOI=10.1152/ajprenal.1999.276.3.f398;
RA Edwards J.C.;
RT "A novel p64-related Cl- channel: subcellular distribution and nephron
RT segment-specific expression.";
RL Am. J. Physiol. 276:F398-F408(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
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 [5]
RP PROTEIN SEQUENCE OF 2-24; 41-60; 62-85 AND 125-130, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Platelet;
RA Bienvenut W.V., Claeys D.;
RL Submitted (FEB-2006) to UniProtKB.
RN [6]
RP SUBUNIT, AND TISSUE SPECIFICITY.
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 [7]
RP INDUCTION, AND FUNCTION.
RX PubMed=12163372; DOI=10.1016/s0002-9440(10)64203-4;
RA Ronnov-Jessen L., Villadsen R., Edwards J.C., Petersen O.W.;
RT "Differential expression of a chloride intracellular channel gene, CLIC4,
RT in transforming growth factor-beta1-mediated conversion of fibroblasts to
RT myofibroblasts.";
RL Am. J. Pathol. 161:471-480(2002).
RN [8]
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 [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14569596; DOI=10.1002/cm.10141;
RA Berryman M.A., Goldenring J.R.;
RT "CLIC4 is enriched at cell-cell junctions and colocalizes with AKAP350 at
RT the centrosome and midbody of cultured mammalian cells.";
RL Cell Motil. Cytoskeleton 56:159-172(2003).
RN [10]
RP FUNCTION.
RX PubMed=16239224; DOI=10.1074/jbc.m506724200;
RA Bohman S., Matsumoto T., Suh K., Dimberg A., Jakobsson L., Yuspa S.,
RA Claesson-Welsh L.;
RT "Proteomic analysis of vascular endothelial growth factor-induced
RT endothelial cell differentiation reveals a role for chloride intracellular
RT channel 4 (CLIC4) in tubular morphogenesis.";
RL J. Biol. Chem. 280:42397-42404(2005).
RN [11]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17200346; DOI=10.1158/1078-0432.ccr-06-1562;
RA Suh K.S., Crutchley J.M., Koochek A., Ryscavage A., Bhat K., Tanaka T.,
RA Oshima A., Fitzgerald P., Yuspa S.H.;
RT "Reciprocal modifications of CLIC4 in tumor epithelium and stroma mark
RT malignant progression of multiple human cancers.";
RL Clin. Cancer Res. 13:121-131(2007).
RN [12]
RP TISSUE SPECIFICITY, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17636002; DOI=10.1242/jcs.002741;
RA Suh K.S., Mutoh M., Mutoh T., Li L., Ryscavage A., Crutchley J.M.,
RA Dumont R.A., Cheng C., Yuspa S.H.;
RT "CLIC4 mediates and is required for Ca2+-induced keratinocyte
RT differentiation.";
RL J. Cell Sci. 120:2631-2640(2007).
RN [13]
RP INTERACTION WITH HRH3, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18302930; DOI=10.1016/j.bbrc.2008.02.071;
RA Maeda K., Haraguchi M., Kuramasu A., Sato T., Ariake K., Sakagami H.,
RA Kondo H., Yanai K., Fukunaga K., Yanagisawa T., Sukegawa J.;
RT "CLIC4 interacts with histamine H3 receptor and enhances the receptor cell
RT surface expression.";
RL Biochem. Biophys. Res. Commun. 369:603-608(2008).
RN [14]
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 [15]
RP FUNCTION.
RX PubMed=19247789; DOI=10.1007/s10456-009-9139-3;
RA Tung J.J., Hobert O., Berryman M., Kitajewski J.;
RT "Chloride intracellular channel 4 is involved in endothelial proliferation
RT and morphogenesis in vitro.";
RL Angiogenesis 12:209-220(2009).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-130, AND IDENTIFICATION BY MASS
RP 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 [17]
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 [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-4, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
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 [20]
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 [21]
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 [22]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), SUBUNIT, FUNCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=16176272; DOI=10.1111/j.1742-4658.2005.04909.x;
RA Littler D.R., Assaad N.N., Harrop S.J., Brown L.J., Pankhurst G.J.,
RA Luciani P., Aguilar M.-I., Mazzanti M., Berryman M.A., Breit S.N.,
RA Curmi P.M.G.;
RT "Crystal structure of the soluble form of the redox-regulated chloride ion
RT channel protein CLIC4.";
RL FEBS J. 272:4996-5007(2005).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), AND DOMAIN.
RX PubMed=16581025; DOI=10.1016/j.bbrc.2006.03.099;
RA Li Y., Li D., Zeng Z., Wang D.;
RT "Trimeric structure of the wild soluble chloride intracellular ion channel
RT CLIC4 observed in crystals.";
RL Biochem. Biophys. Res. Commun. 343:1272-1278(2006).
CC -!- FUNCTION: Can insert into membranes and form poorly selective ion
CC channels that may also transport chloride ions. Channel activity
CC depends on the pH. Membrane insertion seems to be redox-regulated and
CC may occur only under oxydizing conditions. Promotes cell-surface
CC expression of HRH3. Has alternate cellular functions like a potential
CC role in angiogenesis or in maintaining apical-basolateral membrane
CC polarity during mitosis and cytokinesis. Could also promote endothelial
CC cell proliferation and regulate endothelial morphogenesis
CC (tubulogenesis). {ECO:0000269|PubMed:12163372,
CC ECO:0000269|PubMed:14569596, ECO:0000269|PubMed:16176272,
CC ECO:0000269|PubMed:16239224, ECO:0000269|PubMed:18302930,
CC ECO:0000269|PubMed:19247789}.
CC -!- SUBUNIT: Component of a multimeric complex consisting of several
CC cytoskeletal proteins, including actin, ezrin, alpha-actinin, gelsolin,
CC IQGAP1 and CLIC5A. Binds directly to brain dynamin I in a complex
CC containing actin, tubulin and 14-3-3 isoforms. Monomer. Interacts with
CC HRH3. Interacts with AKAP9. {ECO:0000269|PubMed:10793131,
CC ECO:0000269|PubMed:12163479, ECO:0000269|PubMed:16176272,
CC ECO:0000269|PubMed:18302930}.
CC -!- INTERACTION:
CC Q9Y696; Q4KMQ1-2: TPRN; NbExp=4; IntAct=EBI-1057480, EBI-11978969;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:14569596}. Cytoplasmic vesicle
CC membrane {ECO:0000305|PubMed:17636002}; Single-pass membrane protein
CC {ECO:0000305}. Nucleus {ECO:0000305|PubMed:17636002}. Cell membrane
CC {ECO:0000269|PubMed:18302930}; Single-pass membrane protein
CC {ECO:0000305}. Mitochondrion {ECO:0000250|UniProtKB:Q9Z0W7}. Cell
CC junction {ECO:0000269|PubMed:14569596}. Note=Colocalized with AKAP9 at
CC the centrosome and midbody. Exists both as soluble cytoplasmic protein
CC and as membrane protein with probably a single transmembrane domain.
CC Present in an intracellular vesicular compartment that likely represent
CC trans-Golgi network vesicles. Might not be present in the nucleus of
CC cardiac cells. {ECO:0000250|UniProtKB:Q9Z0W7,
CC ECO:0000269|PubMed:14569596}.
CC -!- TISSUE SPECIFICITY: Detected in epithelial cells from colon, esophagus
CC and kidney (at protein level). Expression is prominent in heart,
CC kidney, placenta and skeletal muscle. {ECO:0000269|PubMed:10793131,
CC ECO:0000269|PubMed:17200346, ECO:0000269|PubMed:17636002}.
CC -!- INDUCTION: Up-regulated by calcium ions in differentiating
CC keratinocytes. Up-regulated in myofibroblasts.
CC {ECO:0000269|PubMed:12163372, ECO:0000269|PubMed:17636002}.
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 a 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:16581025}.
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="https://atlasgeneticsoncology.org/gene/40102/CLIC4";
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DR EMBL; AF097330; AAD38446.1; -; mRNA.
DR EMBL; AF109196; AAD26136.1; -; mRNA.
DR EMBL; AL117424; CAB55916.1; -; mRNA.
DR EMBL; BC012444; AAH12444.1; -; mRNA.
DR CCDS; CCDS256.1; -.
DR PIR; T17226; T17226.
DR RefSeq; NP_039234.1; NM_013943.2.
DR PDB; 2AHE; X-ray; 1.80 A; A=1-251.
DR PDB; 2D2Z; X-ray; 2.20 A; A/B/C=1-253.
DR PDB; 3OQS; X-ray; 2.00 A; B=198-207.
DR PDBsum; 2AHE; -.
DR PDBsum; 2D2Z; -.
DR PDBsum; 3OQS; -.
DR AlphaFoldDB; Q9Y696; -.
DR SMR; Q9Y696; -.
DR BioGRID; 117431; 131.
DR IntAct; Q9Y696; 15.
DR MINT; Q9Y696; -.
DR STRING; 9606.ENSP00000363500; -.
DR TCDB; 1.A.12.1.6; the intracellular chloride channel (clic) family.
DR GlyGen; Q9Y696; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y696; -.
DR MetOSite; Q9Y696; -.
DR PhosphoSitePlus; Q9Y696; -.
DR SwissPalm; Q9Y696; -.
DR BioMuta; CLIC4; -.
DR DMDM; 20141285; -.
DR OGP; Q9Y696; -.
DR REPRODUCTION-2DPAGE; IPI00001960; -.
DR EPD; Q9Y696; -.
DR jPOST; Q9Y696; -.
DR MassIVE; Q9Y696; -.
DR MaxQB; Q9Y696; -.
DR PaxDb; 9606-ENSP00000363500; -.
DR PeptideAtlas; Q9Y696; -.
DR ProteomicsDB; 86632; -.
DR Pumba; Q9Y696; -.
DR TopDownProteomics; Q9Y696; -.
DR Antibodypedia; 1956; 413 antibodies from 41 providers.
DR DNASU; 25932; -.
DR Ensembl; ENST00000374379.9; ENSP00000363500.4; ENSG00000169504.15.
DR Ensembl; ENST00000488683.1; ENSP00000436538.1; ENSG00000169504.15.
DR GeneID; 25932; -.
DR KEGG; hsa:25932; -.
DR MANE-Select; ENST00000374379.9; ENSP00000363500.4; NM_013943.3; NP_039234.1.
DR UCSC; uc001bjo.3; human.
DR AGR; HGNC:13518; -.
DR CTD; 25932; -.
DR DisGeNET; 25932; -.
DR GeneCards; CLIC4; -.
DR HGNC; HGNC:13518; CLIC4.
DR HPA; ENSG00000169504; Low tissue specificity.
DR MIM; 606536; gene.
DR neXtProt; NX_Q9Y696; -.
DR OpenTargets; ENSG00000169504; -.
DR PharmGKB; PA26591; -.
DR VEuPathDB; HostDB:ENSG00000169504; -.
DR eggNOG; KOG1422; Eukaryota.
DR GeneTree; ENSGT00940000155017; -.
DR HOGENOM; CLU_061051_1_0_1; -.
DR InParanoid; Q9Y696; -.
DR OMA; CHQIFMI; -.
DR OrthoDB; 103277at2759; -.
DR PhylomeDB; Q9Y696; -.
DR TreeFam; TF315438; -.
DR PathwayCommons; Q9Y696; -.
DR SignaLink; Q9Y696; -.
DR BioGRID-ORCS; 25932; 16 hits in 1129 CRISPR screens.
DR ChiTaRS; CLIC4; human.
DR EvolutionaryTrace; Q9Y696; -.
DR GeneWiki; CLIC4; -.
DR GenomeRNAi; 25932; -.
DR Pharos; Q9Y696; Tbio.
DR PRO; PR:Q9Y696; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9Y696; Protein.
DR Bgee; ENSG00000169504; Expressed in blood vessel layer and 214 other cell types or tissues.
DR ExpressionAtlas; Q9Y696; baseline and differential.
DR Genevisible; Q9Y696; HS.
DR GO; GO:0015629; C:actin cytoskeleton; TAS:UniProtKB.
DR GO; GO:0045177; C:apical part of cell; IDA:UniProtKB.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005902; C:microvillus; IDA:UniProtKB.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005254; F:chloride channel activity; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; TAS:UniProtKB.
DR GO; GO:0071277; P:cellular response to calcium ion; IMP:UniProtKB.
DR GO; GO:0006821; P:chloride transport; IBA:GO_Central.
DR GO; GO:0001886; P:endothelial cell morphogenesis; IEA:Ensembl.
DR GO; GO:0035088; P:establishment or maintenance of apical/basal cell polarity; NAS:UniProtKB.
DR GO; GO:0009566; P:fertilization; IEA:Ensembl.
DR GO; GO:0030216; P:keratinocyte differentiation; IMP:UniProtKB.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:0030336; P:negative regulation of cell migration; IDA:UniProtKB.
DR GO; GO:0051493; P:regulation of cytoskeleton organization; NAS:UniProtKB.
DR GO; GO:0061299; P:retina vasculature morphogenesis in camera-type eye; IEA:Ensembl.
DR GO; GO:0007035; P:vacuolar acidification; IEA:Ensembl.
DR CDD; cd10296; GST_C_CLIC4; 1.
DR CDD; cd03061; GST_N_CLIC; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR002946; CLIC.
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 NCBIfam; TIGR00862; O-ClC; 1.
DR PANTHER; PTHR45476:SF5; CHLORIDE INTRACELLULAR CHANNEL PROTEIN; 1.
DR PANTHER; PTHR45476; CHLORIDE INTRACELLULAR CHANNEL PROTEIN 6-RELATED; 1.
DR Pfam; PF13409; GST_N_2; 1.
DR PRINTS; PR01263; INTCLCHANNEL.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SFLD; SFLDG00358; Main_(cytGST); 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS50405; GST_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell junction; Cell membrane; Chloride;
KW Chloride channel; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW Direct protein sequencing; Ion channel; Ion transport; Membrane;
KW Mitochondrion; Nucleus; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895"
FT CHAIN 2..253
FT /note="Chloride intracellular channel protein 4"
FT /id="PRO_0000144210"
FT TRANSMEM 37..57
FT /note="Helical; Note=After insertion into the membrane"
FT /evidence="ECO:0000255"
FT DOMAIN 104..244
FT /note="GST C-terminal"
FT REGION 2..101
FT /note="Required for insertion into the membrane"
FT /evidence="ECO:0000305"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 24
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O00299"
FT MOD_RES 130
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00299"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00299"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYB1"
FT MOD_RES 244
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1Q5"
FT CONFLICT 14
FT /note="D -> Y (in Ref. 2; AAD26136)"
FT /evidence="ECO:0000305"
FT CONFLICT 133..134
FT /note="RP -> SA (in Ref. 1; AAD38446 and 2; AAD26136)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="Y -> S (in Ref. 2; AAD26136)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="T -> A (in Ref. 2; AAD26136)"
FT /evidence="ECO:0000305"
FT STRAND 19..25
FT /evidence="ECO:0007829|PDB:2AHE"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:2AHE"
FT HELIX 36..48
FT /evidence="ECO:0007829|PDB:2AHE"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:2AHE"
FT HELIX 64..69
FT /evidence="ECO:0007829|PDB:2AHE"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:2AHE"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:2AHE"
FT HELIX 88..98
FT /evidence="ECO:0007829|PDB:2AHE"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:2AHE"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:2AHE"
FT TURN 116..120
FT /evidence="ECO:0007829|PDB:2AHE"
FT HELIX 121..130
FT /evidence="ECO:0007829|PDB:2AHE"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:2AHE"
FT HELIX 137..156
FT /evidence="ECO:0007829|PDB:2AHE"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:2AHE"
FT HELIX 186..206
FT /evidence="ECO:0007829|PDB:2AHE"
FT HELIX 215..225
FT /evidence="ECO:0007829|PDB:2AHE"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:2AHE"
FT HELIX 237..243
FT /evidence="ECO:0007829|PDB:2AHE"
FT TURN 244..247
FT /evidence="ECO:0007829|PDB:2AHE"
SQ SEQUENCE 253 AA; 28772 MW; 3DD21A33C66626A5 CRC64;
MALSMPLNGL KEEDKEPLIE LFVKAGSDGE SIGNCPFSQR LFMILWLKGV VFSVTTVDLK
RKPADLQNLA PGTHPPFITF NSEVKTDVNK IEEFLEEVLC PPKYLKLSPK HPESNTAGMD
IFAKFSAYIK NSRPEANEAL ERGLLKTLQK LDEYLNSPLP DEIDENSMED IKFSTRKFLD
GNEMTLADCN LLPKLHIVKV VAKKYRNFDI PKEMTGIWRY LTNAYSRDEF TNTCPSDKEV
EIAYSDVAKR LTK
//
