CLIC4_RAT
ID CLIC4_RAT Reviewed; 253 AA.
AC Q9Z0W7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Chloride intracellular channel protein 4;
DE AltName: Full=Intracellular chloride ion channel protein p64H1;
GN Name=Clic4;
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 TISSUE=Brain;
RX PubMed=9295337; DOI=10.1074/jbc.272.38.23880;
RA Duncan R.R., Westwood P.K., Boyd A., Ashley R.H.;
RT "Rat brain p64H1, expression of a new member of the p64 chloride channel
RT protein family in endoplasmic reticulum.";
RL J. Biol. Chem. 272:23880-23886(1997).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=17453412; DOI=10.1080/09687860600927907;
RA Singh H., Ashley R.H.;
RT "CLIC4 (p64H1) and its putative transmembrane domain form poorly selective,
RT redox-regulated ion channels.";
RL Mol. Membr. Biol. 24:41-52(2007).
RN [3]
RP FUNCTION, INTERACTION WITH HRH3, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
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).
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. May play a role in angiogenesis (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:17453412,
CC ECO:0000269|PubMed:18302930}.
CC -!- SUBUNIT: Monomer (By similarity). Interacts with HRH3. {ECO:0000250,
CC ECO:0000269|PubMed:18302930}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum. Membrane {ECO:0000305};
CC Single-pass membrane protein {ECO:0000305}. Cytoplasm {ECO:0000250}.
CC Cytoplasmic vesicle membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}. Nucleus {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=Exists
CC both as soluble cytoplasmic protein and as membrane protein with
CC probably a single transmembrane domain. Present in an intracellular
CC vesicular compartment that likely represent trans-Golgi network
CC vesicles (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in brain, in cell bodies and dendrites of
CC Purkinje cells in cerebellar neurons (at protein level). Marked
CC expression was found in hippocampus and cerebellum, and in many other
CC tissues. {ECO:0000269|PubMed:18302930}.
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; AF104119; AAD16875.1; -; mRNA.
DR PIR; S70484; S70484.
DR RefSeq; NP_114006.1; NM_031818.1.
DR AlphaFoldDB; Q9Z0W7; -.
DR SMR; Q9Z0W7; -.
DR BioGRID; 249813; 6.
DR CORUM; Q9Z0W7; -.
DR STRING; 10116.ENSRNOP00000024464; -.
DR iPTMnet; Q9Z0W7; -.
DR PhosphoSitePlus; Q9Z0W7; -.
DR SwissPalm; Q9Z0W7; -.
DR World-2DPAGE; 0004:Q9Z0W7; -.
DR jPOST; Q9Z0W7; -.
DR PaxDb; Q9Z0W7; -.
DR PRIDE; Q9Z0W7; -.
DR GeneID; 83718; -.
DR KEGG; rno:83718; -.
DR CTD; 25932; -.
DR RGD; 61857; Clic4.
DR eggNOG; KOG1422; Eukaryota.
DR InParanoid; Q9Z0W7; -.
DR OrthoDB; 974249at2759; -.
DR PhylomeDB; Q9Z0W7; -.
DR PRO; PR:Q9Z0W7; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0045177; C:apical part of cell; ISO:RGD.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0005813; C:centrosome; ISO:RGD.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; TAS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; TAS:RGD.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005902; C:microvillus; ISO:RGD.
DR GO; GO:0030496; C:midbody; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0016363; C:nuclear matrix; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0031982; C:vesicle; TAS:UniProtKB.
DR GO; GO:0005254; F:chloride channel activity; IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0001525; P:angiogenesis; ISO:RGD.
DR GO; GO:0048754; P:branching morphogenesis of an epithelial tube; ISO:RGD.
DR GO; GO:0071277; P:cellular response to calcium ion; ISO:RGD.
DR GO; GO:0006821; P:chloride transport; IBA:GO_Central.
DR GO; GO:0001886; P:endothelial cell morphogenesis; ISO:RGD.
DR GO; GO:0009566; P:fertilization; ISO:RGD.
DR GO; GO:0030216; P:keratinocyte differentiation; ISO:RGD.
DR GO; GO:0035264; P:multicellular organism growth; ISO:RGD.
DR GO; GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0061299; P:retina vasculature morphogenesis in camera-type eye; ISO:RGD.
DR GO; GO:0007035; P:vacuolar acidification; ISO:RGD.
DR InterPro; IPR002946; CLIC.
DR InterPro; IPR030257; CLIC-4/6.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR45476:SF1; PTHR45476:SF1; 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 Acetylation; Cell membrane; Chloride; Chloride channel; Cytoplasm;
KW Cytoplasmic vesicle; Endoplasmic reticulum; Ion channel; Ion transport;
KW Membrane; Nucleus; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9Y696"
FT CHAIN 2..253
FT /note="Chloride intracellular channel protein 4"
FT /id="PRO_0000144212"
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:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y696"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y696"
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:0000250|UniProtKB:Q9Y696"
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"
SQ SEQUENCE 253 AA; 28633 MW; DC2A66C3258AAFCF CRC64;
MALSMPLNGL KEEDKEPLIE LFVKAGSDGE SIGNCPFSQR LFMILWLKGV VFSVTTVDLK
RKPAHLQNLA PGTHPPFITF NSEVKTDVNK IEEFLEEVLC PPKYLKLSPK HPESNTAGMD
IFAKFSAYIK NSRPEANEAL ERGLLKTLQK LDEYLNSPLP GEIDENSMED IKSSTRRFLD
GDEMTLADCN LLPKLHIVKV VAKKYRNFDI PKGMTGIWRY LTNAYSRDEF TNTCPSDKEV
EIAYSDVAKR LTK
