CLIC5_HUMAN
ID CLIC5_HUMAN Reviewed; 410 AA.
AC Q9NZA1; B3KUF1; Q5T4Z0; Q8NBY3; Q96JT5; Q9BWZ0;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 3.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Chloride intracellular channel protein 5;
GN Name=CLIC5;
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] (ISOFORM 1), AND SUBCELLULAR LOCATION (ISOFORM
RP 1).
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH AKAP9, AND
RP SUBCELLULAR LOCATION (ISOFORM 2).
RC TISSUE=Colon adenocarcinoma;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta, and Small intestine;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Placenta;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
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 [8]
RP FUNCTION, AND SUBCELLULAR LOCATION (ISOFORM 1).
RX PubMed=15184393; DOI=10.1074/jbc.m402835200;
RA Berryman M., Bruno J., Price J., Edwards J.C.;
RT "CLIC-5A functions as a chloride channel in vitro and associates with the
RT cortical actin cytoskeleton in vitro and in vivo.";
RL J. Biol. Chem. 279:34794-34801(2004).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION (ISOFORM 1), AND INTERACTION WITH F-ACTIN.
RX PubMed=18028448; DOI=10.1111/j.1742-4658.2007.06145.x;
RA Singh H., Cousin M.A., Ashley R.H.;
RT "Functional reconstitution of mammalian 'chloride intracellular channels'
RT CLIC1, CLIC4 and CLIC5 reveals differential regulation by cytoskeletal
RT actin.";
RL FEBS J. 274:6306-6316(2007).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION (ISOFORM 1), AND TISSUE SPECIFICITY (ISOFORM
RP 1).
RX PubMed=20335315; DOI=10.1152/ajprenal.00030.2010;
RA Wegner B., Al-Momany A., Kulak S.C., Kozlowski K., Obeidat M., Jahroudi N.,
RA Paes J., Berryman M., Ballermann B.J.;
RT "CLIC5A, a component of the ezrin-podocalyxin complex in glomeruli, is a
RT determinant of podocyte integrity.";
RL Am. J. Physiol. 298:F1492-F1503(2010).
RN [11]
RP FUNCTION, TISSUE SPECIFICITY, AND INVOLVEMENT IN DFNB103.
RX PubMed=24781754; DOI=10.1038/ejhg.2014.83;
RA Seco C.Z., Oonk A.M., Dominguez-Ruiz M., Draaisma J.M., Gandia M.,
RA Oostrik J., Neveling K., Kunst H.P., Hoefsloot L.H., Del Castillo I.,
RA Pennings R.J., Kremer H., Admiraal R.J., Schraders M.;
RT "Progressive hearing loss and vestibular dysfunction caused by a homozygous
RT nonsense mutation in CLIC5.";
RL Eur. J. Hum. Genet. 23:189-194(2015).
CC -!- FUNCTION: Required for normal hearing (PubMed:24781754). It is
CC necessary for the formation of stereocilia in the inner ear and normal
CC development of the organ of Corti (By similarity). Can insert into
CC membranes and form poorly selective ion channels that may also
CC transport chloride ions. May play a role in the regulation of
CC transepithelial ion absorption and secretion. Is required for the
CC development and/or maintenance of the proper glomerular endothelial
CC cell and podocyte architecture (PubMed:15184393, PubMed:18028448,
CC PubMed:20335315). Plays a role in formation of the lens suture in the
CC eye, which is important for normal optical properties of the lens (By
CC similarity). {ECO:0000250|UniProtKB:Q8BXK9,
CC ECO:0000269|PubMed:15184393, ECO:0000269|PubMed:18028448,
CC ECO:0000269|PubMed:20335315, ECO:0000269|PubMed:24781754}.
CC -!- SUBUNIT: Component of a multimeric complex consisting of several
CC cytoskeletal proteins, including actin, ezrin, alpha-actinin, gelsolin,
CC and IQGAP1. Interacts with AKAP9. {ECO:0000269|PubMed:12163479,
CC ECO:0000269|PubMed:18028448}.
CC -!- INTERACTION:
CC Q9NZA1; P00523: SRC; Xeno; NbExp=2; IntAct=EBI-5658997, EBI-848039;
CC Q9NZA1-2; Q4KMQ1-2: TPRN; NbExp=6; IntAct=EBI-13076412, EBI-11978969;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:10793131, ECO:0000269|PubMed:15184393}. Cytoplasm,
CC cell cortex {ECO:0000269|PubMed:15184393}. Membrane
CC {ECO:0000269|PubMed:15184393, ECO:0000305|PubMed:18028448}; Single-pass
CC membrane protein {ECO:0000255}. Apical cell membrane
CC {ECO:0000269|PubMed:20335315}; Single-pass membrane protein
CC {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:O00299}.
CC Note=Associates with the cortical actin cytoskeleton (PubMed:10793131,
CC PubMed:15184393). Localizes to the apical region of cochlear hair
CC cells, at the base of the actin-rich hair bundle (By similarity).
CC Colocalizes with podocalyxin at the apical cell membrane in renal
CC glomeruli (PubMed:20335315). May localize to the centrosome in lens
CC epithelial cells (By similarity). Exists both as soluble cytoplasmic
CC protein and as membrane protein with probably a single transmembrane
CC domain (By similarity). {ECO:0000250|UniProtKB:O00299,
CC ECO:0000250|UniProtKB:Q8BXK9, ECO:0000250|UniProtKB:Q9EPT8,
CC ECO:0000269|PubMed:10793131, ECO:0000269|PubMed:15184393,
CC ECO:0000269|PubMed:20335315}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Golgi apparatus
CC {ECO:0000269|PubMed:12163479}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:12163479}.
CC Note=Colocalizes with AKAP9 at the Golgi apparatus as well as, to a
CC lesser extent, the centrosome. {ECO:0000269|PubMed:12163479}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=2; Synonyms=CLIC5B;
CC IsoId=Q9NZA1-1; Sequence=Displayed;
CC Name=1; Synonyms=CLIC5A;
CC IsoId=Q9NZA1-2; Sequence=VSP_000869, VSP_000870;
CC Name=3;
CC IsoId=Q9NZA1-3; Sequence=VSP_044889, VSP_044890, VSP_044891;
CC -!- TISSUE SPECIFICITY: Widely expressed in both fetal and adult human
CC tissues (PubMed:24781754). Isoform 1 is expressed in renal glomeruli
CC endothelial cells and podocytes (at protein level).
CC {ECO:0000269|PubMed:20335315, ECO:0000269|PubMed:24781754}.
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 -!- DISEASE: Deafness, autosomal recessive, 103 (DFNB103) [MIM:616042]: A
CC form of sensorineural deafness with onset in early childhood. Hearing
CC impairment progresses from mild to severe or even profound before the
CC second decade, and is accompanied by vestibular areflexia.
CC {ECO:0000269|PubMed:24781754}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the chloride channel CLIC family. {ECO:0000305}.
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DR EMBL; AF216941; AAF66928.1; -; mRNA.
DR EMBL; AY032602; AAK52083.1; -; mRNA.
DR EMBL; AK075163; BAC11444.1; -; mRNA.
DR EMBL; AK097048; BAG53413.1; -; mRNA.
DR EMBL; AK075144; BAC11432.1; -; mRNA.
DR EMBL; AL050336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL357057; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355522; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL591211; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX04286.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX04287.1; -; Genomic_DNA.
DR EMBL; BC035968; AAH35968.1; -; mRNA.
DR CCDS; CCDS47438.1; -. [Q9NZA1-1]
DR CCDS; CCDS4914.1; -. [Q9NZA1-2]
DR CCDS; CCDS59022.1; -. [Q9NZA1-3]
DR RefSeq; NP_001107558.1; NM_001114086.1. [Q9NZA1-1]
DR RefSeq; NP_001242952.1; NM_001256023.1. [Q9NZA1-3]
DR RefSeq; NP_058625.2; NM_016929.4. [Q9NZA1-2]
DR RefSeq; XP_016866442.1; XM_017010953.1.
DR PDB; 6Y2H; X-ray; 2.15 A; A/B/C/D=175-410.
DR PDBsum; 6Y2H; -.
DR AlphaFoldDB; Q9NZA1; -.
DR SMR; Q9NZA1; -.
DR BioGRID; 119781; 17.
DR CORUM; Q9NZA1; -.
DR IntAct; Q9NZA1; 9.
DR MINT; Q9NZA1; -.
DR STRING; 9606.ENSP00000185206; -.
DR iPTMnet; Q9NZA1; -.
DR PhosphoSitePlus; Q9NZA1; -.
DR BioMuta; CLIC5; -.
DR DMDM; 215274174; -.
DR OGP; Q9NZA1; -.
DR EPD; Q9NZA1; -.
DR jPOST; Q9NZA1; -.
DR MassIVE; Q9NZA1; -.
DR MaxQB; Q9NZA1; -.
DR PaxDb; Q9NZA1; -.
DR PeptideAtlas; Q9NZA1; -.
DR PRIDE; Q9NZA1; -.
DR ProteomicsDB; 72834; -.
DR ProteomicsDB; 83343; -. [Q9NZA1-1]
DR ProteomicsDB; 83344; -. [Q9NZA1-2]
DR Antibodypedia; 16850; 247 antibodies from 27 providers.
DR DNASU; 53405; -.
DR Ensembl; ENST00000185206.12; ENSP00000185206.6; ENSG00000112782.19. [Q9NZA1-1]
DR Ensembl; ENST00000339561.12; ENSP00000344165.6; ENSG00000112782.19. [Q9NZA1-2]
DR Ensembl; ENST00000544153.3; ENSP00000439195.1; ENSG00000112782.19. [Q9NZA1-3]
DR GeneID; 53405; -.
DR KEGG; hsa:53405; -.
DR MANE-Select; ENST00000339561.12; ENSP00000344165.6; NM_016929.5; NP_058625.2. [Q9NZA1-2]
DR UCSC; uc003oxu.5; human. [Q9NZA1-1]
DR CTD; 53405; -.
DR DisGeNET; 53405; -.
DR GeneCards; CLIC5; -.
DR HGNC; HGNC:13517; CLIC5.
DR HPA; ENSG00000112782; Tissue enhanced (heart muscle, skeletal muscle, tongue).
DR MalaCards; CLIC5; -.
DR MIM; 607293; gene.
DR MIM; 616042; phenotype.
DR neXtProt; NX_Q9NZA1; -.
DR OpenTargets; ENSG00000112782; -.
DR Orphanet; 90636; Autosomal recessive non-syndromic sensorineural deafness type DFNB.
DR PharmGKB; PA26592; -.
DR VEuPathDB; HostDB:ENSG00000112782; -.
DR eggNOG; KOG1422; Eukaryota.
DR GeneTree; ENSGT00940000156406; -.
DR HOGENOM; CLU_048291_0_0_1; -.
DR InParanoid; Q9NZA1; -.
DR OMA; YRNYEFP; -.
DR OrthoDB; 974249at2759; -.
DR PhylomeDB; Q9NZA1; -.
DR TreeFam; TF315438; -.
DR PathwayCommons; Q9NZA1; -.
DR Reactome; R-HSA-9662360; Sensory processing of sound by inner hair cells of the cochlea.
DR Reactome; R-HSA-9662361; Sensory processing of sound by outer hair cells of the cochlea.
DR SignaLink; Q9NZA1; -.
DR BioGRID-ORCS; 53405; 12 hits in 1068 CRISPR screens.
DR ChiTaRS; CLIC5; human.
DR GeneWiki; CLIC5; -.
DR GenomeRNAi; 53405; -.
DR Pharos; Q9NZA1; Tbio.
DR PRO; PR:Q9NZA1; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9NZA1; protein.
DR Bgee; ENSG00000112782; Expressed in renal glomerulus and 192 other tissues.
DR ExpressionAtlas; Q9NZA1; baseline and differential.
DR Genevisible; Q9NZA1; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0032421; C:stereocilium bundle; IEA:Ensembl.
DR GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0006821; P:chloride transport; IDA:UniProtKB.
DR GO; GO:0007565; P:female pregnancy; TAS:ProtInc.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007605; P:sensory perception of sound; IMP:UniProtKB.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR CDD; cd10297; GST_C_CLIC5; 1.
DR InterPro; IPR002946; CLIC.
DR InterPro; IPR030264; CLIC-5.
DR InterPro; IPR042069; CLIC5_C_GST.
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; PTHR45476:SF4; PTHR45476:SF4; 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; Alternative splicing; Cell membrane; Chloride;
KW Chloride channel; Cytoplasm; Cytoskeleton; Deafness; Golgi apparatus;
KW Hearing; Ion channel; Ion transport; Membrane; Non-syndromic deafness;
KW Reference proteome; Sensory transduction; Transmembrane;
KW Transmembrane helix; Transport; Vision; Voltage-gated channel.
FT CHAIN 1..410
FT /note="Chloride intracellular channel protein 5"
FT /id="PRO_0000144214"
FT TRANSMEM 193..213
FT /note="Helical; Note=After insertion into the membrane"
FT /evidence="ECO:0000255"
FT DOMAIN 260..400
FT /note="GST C-terminal"
FT VAR_SEQ 1..159
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:10793131,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_000869"
FT VAR_SEQ 1..17
FT /note="MNDEDYSTIYDTIQNER -> MTDSATANGDDRDPEIE (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:16303743"
FT /id="VSP_044889"
FT VAR_SEQ 18..176
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16303743"
FT /id="VSP_044890"
FT VAR_SEQ 160..180
FT /note="AEGLEEKEGAHMNPEIYLFVK -> MTDSATANGDDRDPEIELFVK (in
FT isoform 1)"
FT /evidence="ECO:0000303|PubMed:10793131,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_000870"
FT VAR_SEQ 356..410
FT /note="IVAKKYRNYDIPAEMTGLWRYLKNAYARDEFTNTCAADSEIELAYADVAKRL
FT SRS -> EQVPLKGMI (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16303743"
FT /id="VSP_044891"
FT VARIANT 114
FT /note="T -> A (in dbSNP:rs723580)"
FT /id="VAR_059208"
FT VARIANT 257
FT /note="P -> H (in dbSNP:rs35822882)"
FT /id="VAR_047541"
FT CONFLICT 201
FT /note="L -> F (in Ref. 2; AAK52083)"
FT /evidence="ECO:0000305"
FT STRAND 175..181
FT /evidence="ECO:0007829|PDB:6Y2H"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:6Y2H"
FT HELIX 192..204
FT /evidence="ECO:0007829|PDB:6Y2H"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:6Y2H"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:6Y2H"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:6Y2H"
FT HELIX 244..254
FT /evidence="ECO:0007829|PDB:6Y2H"
FT TURN 257..259
FT /evidence="ECO:0007829|PDB:6Y2H"
FT HELIX 268..271
FT /evidence="ECO:0007829|PDB:6Y2H"
FT TURN 272..276
FT /evidence="ECO:0007829|PDB:6Y2H"
FT HELIX 277..286
FT /evidence="ECO:0007829|PDB:6Y2H"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:6Y2H"
FT HELIX 293..312
FT /evidence="ECO:0007829|PDB:6Y2H"
FT HELIX 316..319
FT /evidence="ECO:0007829|PDB:6Y2H"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:6Y2H"
FT HELIX 342..362
FT /evidence="ECO:0007829|PDB:6Y2H"
FT HELIX 371..381
FT /evidence="ECO:0007829|PDB:6Y2H"
FT HELIX 384..387
FT /evidence="ECO:0007829|PDB:6Y2H"
FT HELIX 393..399
FT /evidence="ECO:0007829|PDB:6Y2H"
FT TURN 400..403
FT /evidence="ECO:0007829|PDB:6Y2H"
FT CONFLICT Q9NZA1-2:12
FT /note="R -> S (in Ref. 1; AAF66928)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 410 AA; 46503 MW; E26D307775F8354C CRC64;
MNDEDYSTIY DTIQNERTYE VPDQPEENES PHYDDVHEYL RPENDLYATQ LNTHEYDFVS
VYTIKGEETS LASVQSEDRG YLLPDEIYSE LQEAHPGEPQ EDRGISMEGL YSSTQDQQLC
AAELQENGSV MKEDLPSPSS FTIQHSKAFS TTKYSCYSDA EGLEEKEGAH MNPEIYLFVK
AGIDGESIGN CPFSQRLFMI LWLKGVVFNV TTVDLKRKPA DLHNLAPGTH PPFLTFNGDV
KTDVNKIEEF LEETLTPEKY PKLAAKHRES NTAGIDIFSK FSAYIKNTKQ QNNAALERGL
TKALKKLDDY LNTPLPEEID ANTCGEDKGS RRKFLDGDEL TLADCNLLPK LHVVKIVAKK
YRNYDIPAEM TGLWRYLKNA YARDEFTNTC AADSEIELAY ADVAKRLSRS
