CLIC5_BOVIN
ID CLIC5_BOVIN Reviewed; 437 AA.
AC P35526;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 25-MAY-2022, entry version 143.
DE RecName: Full=Chloride intracellular channel protein 5;
DE AltName: Full=Chlorine channel protein p64;
GN Name=CLIC5;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=7686908; DOI=10.1016/s0021-9258(18)82424-3;
RA Landry D.W., Sullivan S., Nicolaides M., Redhead C., Edelman A., Field M.,
RA Al-Awqati Q., Edwards J.F.;
RT "Molecular cloning and characterization of p64, a chloride channel protein
RT from kidney microsomes.";
RL J. Biol. Chem. 268:14948-14955(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina;
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).
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 {ECO:0000305|PubMed:7686908};
CC Single-pass membrane protein {ECO:0000255}. Apical cell membrane
CC {ECO:0000250|UniProtKB:Q9NZA1}; Single-pass membrane protein
CC {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:O00299}.
CC Note=Colocalizes with AKAP9 at the Golgi apparatus as well as, to a
CC lesser extent, the centrosome (By similarity). Associates with the
CC cortical actin cytoskeleton (By similarity). Localizes to the apical
CC region of cochlear hair cells, at the base of the actin-rich hair
CC bundle (By similarity). Colocalizes with podocalyxin at the apical cell
CC membrane in renal glomeruli (By similarity). May localize to the
CC centrosome in lens epithelial cells (By similarity). Exists both as
CC soluble cytoplasmic protein and as membrane protein with probably a
CC single transmembrane domain (By similarity).
CC {ECO:0000250|UniProtKB:O00299, ECO:0000250|UniProtKB:Q8BXK9,
CC ECO:0000250|UniProtKB:Q9EPT8, ECO:0000250|UniProtKB:Q9NZA1}.
CC -!- TISSUE SPECIFICITY: Expressed in most tissues. Higher levels found in
CC kidney, heart, skeletal muscle, T84 and PANC-1 cells.
CC {ECO:0000269|PubMed:7686908}.
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 -!- PTM: Phosphorylated. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the chloride channel CLIC family. {ECO:0000305}.
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DR EMBL; L16547; AAA02561.1; -; mRNA.
DR EMBL; AF109199; AAD26139.1; -; mRNA.
DR PIR; A47104; A47104.
DR RefSeq; NP_776701.1; NM_174276.3.
DR AlphaFoldDB; P35526; -.
DR SMR; P35526; -.
DR BioGRID; 159015; 1.
DR STRING; 9913.ENSBTAP00000013537; -.
DR TCDB; 1.A.12.1.1; the intracellular chloride channel (clic) family.
DR PaxDb; P35526; -.
DR GeneID; 281696; -.
DR KEGG; bta:281696; -.
DR CTD; 53405; -.
DR eggNOG; KOG1422; Eukaryota.
DR InParanoid; P35526; -.
DR OrthoDB; 974249at2759; -.
DR Proteomes; UP000009136; Unplaced.
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:0031410; C:cytoplasmic vesicle; TAS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; TAS:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; TAS:UniProtKB.
DR GO; GO:0005254; F:chloride channel activity; TAS:UniProtKB.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0006821; P:chloride transport; TAS:UniProtKB.
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; 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 2: Evidence at transcript level;
KW Cell membrane; Chloride; Chloride channel; Cytoplasm; Cytoskeleton;
KW Golgi apparatus; Hearing; Ion channel; Ion transport; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; Sensory transduction;
KW Transmembrane; Transmembrane helix; Transport; Vision;
KW Voltage-gated channel.
FT CHAIN 1..437
FT /note="Chloride intracellular channel protein 5"
FT /id="PRO_0000144213"
FT TRANSMEM 219..239
FT /note="Helical; Note=After insertion into the membrane"
FT /evidence="ECO:0000255"
FT REPEAT 118..125
FT /note="1"
FT REPEAT 126..133
FT /note="2"
FT REPEAT 134..141
FT /note="3"
FT REPEAT 142..149
FT /note="4"
FT DOMAIN 286..427
FT /note="GST C-terminal"
FT REGION 1..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..149
FT /note="4 X 8 AA tandem repeats of [AGQ]-[SP]-D-[PS]-E-E-P-
FT Q"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..153
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 437 AA; 48959 MW; FE5522856BBE799F CRC64;
MNDENYSTTI YNRVQTERVY EDSDPAENGG PLYDEVHEDV RREDNLYVNE LENQEYDSVA
VYPVGRQGRT SASLQPETGE YVLPDEPYSK AQDPHPGEPT ADEDISLEEL LSPTKDHQSD
SEEPQASDPE EPQASDPEEP QGPDPEEPQE NGNEMEADLP SPSSFTIQNS RAFSTREISP
TSYSADDVSE GNESASASPE INLFVKAGID GESIGNCPFS QRLFMILWLK GVVFNVTTVD
LKRKPADLHN LAPGTHPPFL TFNGDVKTDV NKIEEFLEET LTPEKYPRLA AKHRESNTAG
IDIFVKFSAY IKNTKQQSNA ALERGLTKAL KKLDDYLNTP LPEEIDADTR GDDEKGSRRK
FLDGDELTLA DCNLLPKLHV VKIVAKKYRN YDFPAEMTGL WRYLKNAYAR DEFTNTCAAD
SEIELAYADV AKRLSRS
