CLIC5_MOUSE
ID CLIC5_MOUSE Reviewed; 251 AA.
AC Q8BXK9; Q3U0H8;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Chloride intracellular channel protein 5;
GN Name=Clic5;
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 MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Adrenal gland, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISEASE.
RX PubMed=17021174; DOI=10.1523/jneurosci.2166-06.2006;
RA Gagnon L.H., Longo-Guess C.M., Berryman M., Shin J.-B., Saylor K.W., Yu H.,
RA Gillespie P.G., Johnson K.R.;
RT "The chloride intracellular channel protein CLIC5 is expressed at high
RT levels in hair cell stereocilia and is essential for normal inner ear
RT function.";
RL J. Neurosci. 26:10188-10198(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Lung, and Spleen;
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 FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISEASE.
RX PubMed=29425878; DOI=10.1016/j.exer.2018.02.001;
RA Fan J., Lerner J., Wyatt M.K., Cai P., Peterson K., Dong L., Wistow G.;
RT "The klotho-related protein KLPH (lctl) has preferred expression in lens
RT and is essential for expression of clic5 and normal lens suture
RT formation.";
RL Exp. Eye Res. 169:111-121(2018).
CC -!- FUNCTION: Required for normal hearing (By similarity). It is necessary
CC for the formation of stereocilia in the inner ear and normal
CC development of the organ of Corti. Can insert into membranes and form
CC poorly selective ion channels that may also transport chloride ions.
CC May play a role in the regulation of transepithelial ion absorption and
CC secretion. Is required for the development and/or maintenance of the
CC proper glomerular endothelial cell and podocyte architecture
CC (PubMed:17021174). Plays a role in formation of the lens suture in the
CC eye, which is important for normal optical properties of the lens
CC (PubMed:29425878). {ECO:0000250|UniProtKB:Q9NZA1,
CC ECO:0000269|PubMed:17021174, ECO:0000269|PubMed:29425878}.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:Q9NZA1}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:29425878}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q9NZA1}. Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:Q9NZA1}. Membrane
CC {ECO:0000250|UniProtKB:Q9NZA1}; Single-pass membrane protein
CC {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:17021174};
CC Single-pass membrane protein {ECO:0000255}. Cytoplasm
CC {ECO:0000250|UniProtKB:O00299}. Note=Colocalized with AKAP9 at the
CC Golgi apparatus as well as, to a lesser extent, the centrosome (By
CC similarity). Associates with the cortical actin cytoskeleton (By
CC similarity). Localizes to the apical region of cochlear hair cells, at
CC the base of the actin-rich hair bundle (PubMed:17021174). Colocalizes
CC with podocalyxin at the apical cell membrane in renal glomeruli (By
CC similarity). May localize to the centrosome in lens epithelial cells
CC (PubMed:29425878). Exists both as soluble cytoplasmic protein and as
CC membrane protein with probably a single transmembrane domain (By
CC similarity). {ECO:0000250|UniProtKB:O00299,
CC ECO:0000250|UniProtKB:Q9NZA1, ECO:0000269|PubMed:17021174,
CC ECO:0000269|PubMed:29425878}.
CC -!- TISSUE SPECIFICITY: Detected in lung and inner ear. Detected in
CC embryonic cochlea, on microvilli-covered apical surfaces of interdental
CC cells, columnar cells of Kolliker's organ, and on stereocilia of inner
CC and outer hair cells (at protein level) (PubMed:17021174). Also
CC detected in the eye, where it localizes to lens fiber cells in the lens
CC epithelium (at protein level) (PubMed:29425878).
CC {ECO:0000269|PubMed:17021174, ECO:0000269|PubMed:29425878}.
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: Note=Defects in Clic5 are a cause of the jitterbug (jbg)
CC phenotype. Jbg is the result of a spontaneous mutation that leads to
CC severe degeneration of the organ of Corti in the inner ear. Jbg leads
CC to progressive degeneration of inner ear hair cells. Affected mice are
CC identified by head bobbing, circling behavior and their inability to
CC swim. They cannot hear well when young, and become completely deaf
CC after 5 months (PubMed:17021174). In addition, there are eye defects
CC with aberrant development of the lens suture and formation of lens
CC opacities (PubMed:29425878). {ECO:0000269|PubMed:17021174,
CC ECO:0000269|PubMed:29425878}.
CC -!- SIMILARITY: Belongs to the chloride channel CLIC family. {ECO:0000305}.
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DR EMBL; AK046522; BAC32769.1; -; mRNA.
DR EMBL; AK156849; BAE33875.1; -; mRNA.
DR EMBL; BC064037; AAH64037.1; -; mRNA.
DR CCDS; CCDS28804.1; -.
DR RefSeq; NP_766209.1; NM_172621.2.
DR AlphaFoldDB; Q8BXK9; -.
DR SMR; Q8BXK9; -.
DR IntAct; Q8BXK9; 1.
DR STRING; 10090.ENSMUSP00000024755; -.
DR iPTMnet; Q8BXK9; -.
DR PhosphoSitePlus; Q8BXK9; -.
DR EPD; Q8BXK9; -.
DR jPOST; Q8BXK9; -.
DR MaxQB; Q8BXK9; -.
DR PaxDb; Q8BXK9; -.
DR PeptideAtlas; Q8BXK9; -.
DR PRIDE; Q8BXK9; -.
DR ProteomicsDB; 283385; -.
DR Antibodypedia; 16850; 247 antibodies from 27 providers.
DR DNASU; 224796; -.
DR Ensembl; ENSMUST00000024755; ENSMUSP00000024755; ENSMUSG00000023959.
DR GeneID; 224796; -.
DR KEGG; mmu:224796; -.
DR UCSC; uc008cpw.1; mouse.
DR CTD; 53405; -.
DR MGI; MGI:1917912; Clic5.
DR VEuPathDB; HostDB:ENSMUSG00000023959; -.
DR eggNOG; KOG1422; Eukaryota.
DR GeneTree; ENSGT00940000156406; -.
DR HOGENOM; CLU_061051_1_0_1; -.
DR InParanoid; Q8BXK9; -.
DR OMA; YRNYEFP; -.
DR OrthoDB; 974249at2759; -.
DR PhylomeDB; Q8BXK9; -.
DR TreeFam; TF315438; -.
DR BioGRID-ORCS; 224796; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Clic5; mouse.
DR PRO; PR:Q8BXK9; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8BXK9; protein.
DR Bgee; ENSMUSG00000023959; Expressed in right lung and 134 other tissues.
DR ExpressionAtlas; Q8BXK9; baseline and differential.
DR Genevisible; Q8BXK9; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISS: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:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0032420; C:stereocilium; IDA:MGI.
DR GO; GO:0032421; C:stereocilium bundle; ISO:MGI.
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:0060088; P:auditory receptor cell stereocilium organization; IMP:MGI.
DR GO; GO:0006821; P:chloride transport; ISO:MGI.
DR GO; GO:0002024; P:diet induced thermogenesis; IMP:MGI.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI.
DR GO; GO:0008104; P:protein localization; IMP:MGI.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0002021; P:response to dietary excess; IMP:MGI.
DR GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
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 Cell membrane; Chloride; Chloride channel; Cytoplasm; Cytoskeleton;
KW Golgi apparatus; Hearing; Ion channel; Ion transport; Membrane;
KW Reference proteome; Sensory transduction; Transmembrane;
KW Transmembrane helix; Transport; Vision; Voltage-gated channel.
FT CHAIN 1..251
FT /note="Chloride intracellular channel protein 5"
FT /id="PRO_0000144215"
FT TRANSMEM 34..54
FT /note="Helical; Note=After insertion into the membrane"
FT /evidence="ECO:0000255"
FT DOMAIN 101..241
FT /note="GST C-terminal"
FT REGION 1..98
FT /note="Required for insertion into the membrane"
FT /evidence="ECO:0000250"
SQ SEQUENCE 251 AA; 28287 MW; 7055A17D22977974 CRC64;
MTDSATTNGD DRDPEIELFV KAGIDGESIG NCPFSQRLFM ILWLKGVVFN VTTVDLKRKP
ADLHNLAPGT HPPFLTFNGD VKTDVNKIEE FLEETLTPEK YPKLAAKHRE SNTAGIDIFS
KFSAYIKNTK QQNNAALERG LTKALRKLDD YLNSPLPEEI DTNTHGDEKG SQRKFLDGDE
LTLADCNLLP KLHVVKIVAK KYRNYDIPAE MTGLWRYLKN AYARDEFTNT CAADSEIELA
YADVARRLSR S
