CLIC5_RAT
ID CLIC5_RAT Reviewed; 251 AA.
AC Q9EPT8;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Chloride intracellular channel protein 5;
GN Name=Clic5;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Lung;
RA Vanderbilt J., Mager E., Dobbs L.;
RT "Identification of a rat homolog of the human chloride intracellular
RT channel (CLIC5).";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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).
CC -!- FUNCTION: Required for normal hearing. It is necessary for the
CC formation of stereocilia in the inner ear and normal development of the
CC organ of Corti. Can insert into membranes and form poorly selective ion
CC channels that may also transport chloride ions. May play a role in the
CC regulation of transepithelial ion absorption and secretion. Is required
CC for the development and/or maintenance of the proper glomerular
CC endothelial cell and podocyte architecture. Plays a role in formation
CC of the lens suture in the eye, which is important for normal optical
CC properties of the lens. {ECO:0000250|UniProtKB:Q8BXK9,
CC ECO:0000250|UniProtKB:Q9NZA1}.
CC -!- SUBUNIT: Component of a multimeric complex consisting of several
CC cytoskeletal proteins, including actin, ezrin, alpha-actinin, gelsolin,
CC and IQGAP1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:Q9NZA1}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q9NZA1}. 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=Colocalizes 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 (By similarity). 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:Q8BXK9, ECO:0000250|UniProtKB:Q9NZA1,
CC ECO:0000269|PubMed:17021174}.
CC -!- TISSUE SPECIFICITY: Detected in cochlea, in cochlear and vestibular
CC hair cell bundles in the organ of Corti (at protein level).
CC {ECO:0000269|PubMed:17021174}.
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; AF323174; AAG49367.1; -; mRNA.
DR RefSeq; NP_446055.1; NM_053603.2.
DR AlphaFoldDB; Q9EPT8; -.
DR SMR; Q9EPT8; -.
DR BioGRID; 250191; 1.
DR STRING; 10116.ENSRNOP00000067890; -.
DR iPTMnet; Q9EPT8; -.
DR PhosphoSitePlus; Q9EPT8; -.
DR jPOST; Q9EPT8; -.
DR PaxDb; Q9EPT8; -.
DR PRIDE; Q9EPT8; -.
DR Ensembl; ENSRNOT00000079517; ENSRNOP00000072035; ENSRNOG00000047218.
DR GeneID; 94272; -.
DR KEGG; rno:94272; -.
DR UCSC; RGD:620659; rat.
DR CTD; 53405; -.
DR RGD; 620659; Clic5.
DR eggNOG; KOG1422; Eukaryota.
DR GeneTree; ENSGT00940000156406; -.
DR HOGENOM; CLU_061051_1_0_1; -.
DR InParanoid; Q9EPT8; -.
DR OMA; YRNYEFP; -.
DR OrthoDB; 974249at2759; -.
DR PhylomeDB; Q9EPT8; -.
DR TreeFam; TF315438; -.
DR PRO; PR:Q9EPT8; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000047218; Expressed in lung and 18 other tissues.
DR Genevisible; Q9EPT8; RN.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0032420; C:stereocilium; ISO:RGD.
DR GO; GO:0032421; C:stereocilium bundle; IDA:MGI.
DR GO; GO:0005254; F:chloride channel activity; IDA:RGD.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0060088; P:auditory receptor cell stereocilium organization; ISO:RGD.
DR GO; GO:0006821; P:chloride transport; ISO:RGD.
DR GO; GO:0002024; P:diet induced thermogenesis; ISO:RGD.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR GO; GO:0050885; P:neuromuscular process controlling balance; ISO:RGD.
DR GO; GO:0008104; P:protein localization; ISO:RGD.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0002021; P:response to dietary excess; ISO:RGD.
DR GO; GO:0007605; P:sensory perception of sound; ISS: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 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_0000144216"
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; 28299 MW; 11079FDE8508D53C CRC64;
MTDSATANGD DRDPEIELFV KAGIDGESIG NCPFSQRLFM ILWLKGVVFN VTTVDLKRKP
ADLHNLAPGT HPPFLTFNGD VKTDVNKIEE FLEETLTPEK YPKLAARHRE SNTAGIDIFS
KFSAYIKNTK QQNNAALERG LTKALRKLDD YLNTPLPEEI DTNTHGDEKG SQRKFLDGDE
LTLADCNLLP KLHVVKIVAK KYRNYDIPAE MTGLWRYLKN AYARDEFTNT CAADSEIELA
YADVARRLSR S
