ID CLIC6_RAT Reviewed; 612 AA.
AC Q811Q2;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 24-JAN-2024, entry version 140.
DE RecName: Full=Chloride intracellular channel protein 6;
GN Name=Clic6; Synonyms=Clic6b;
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], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH DRD2; DRD3 AND DRD4.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=14499480; DOI=10.1016/s0169-328x(03)00283-3;
RA Griffon N., Jeanneteau F., Prieur F., Diaz J., Sokoloff P.;
RT "CLIC6, a member of the intracellular chloride channel family, interacts
RT with dopamine D(2)-like receptors.";
RL Brain Res. Mol. Brain Res. 117:47-57(2003).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40; SER-264; SER-303; SER-321
RP AND SER-368, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: May insert into membranes and form chloride ion channels. May
CC play a critical role in water-secreting cells, possibly through the
CC regulation of chloride ion transport (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with dopamine receptors DRD2, DRD3 and DRD4.
CC {ECO:0000269|PubMed:14499480}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000305|PubMed:14499480}; Single-pass membrane protein
CC {ECO:0000305|PubMed:14499480}. Note=Predominantly cytoplasmic. Upon
CC chloride ion efflux from the cell, it is translocated to the plasma
CC membrane (By similarity). Colocalizes with DRD3 at the plasma membrane.
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in brain, pituitary and
CC stomach. In adult brain, it is restricted to the choroid plexus, the
CC striatal proliferative subventricular zone and the cerebellum where it
CC colocalizes with the D(3)R in the Purkinje cells of the lobules IX and
CC X. {ECO:0000269|PubMed:14499480}.
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 a 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:0000250}.
CC -!- SIMILARITY: Belongs to the chloride channel CLIC family. {ECO:0000305}.
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DR EMBL; AY191249; AAO38057.1; -; mRNA.
DR RefSeq; NP_788267.1; NM_176078.2.
DR AlphaFoldDB; Q811Q2; -.
DR SMR; Q811Q2; -.
DR STRING; 10116.ENSRNOP00000068644; -.
DR iPTMnet; Q811Q2; -.
DR PhosphoSitePlus; Q811Q2; -.
DR jPOST; Q811Q2; -.
DR PaxDb; 10116-ENSRNOP00000033206; -.
DR GeneID; 304081; -.
DR KEGG; rno:304081; -.
DR UCSC; RGD:727938; rat.
DR AGR; RGD:727938; -.
DR CTD; 54102; -.
DR RGD; 727938; Clic6.
DR eggNOG; KOG1422; Eukaryota.
DR InParanoid; Q811Q2; -.
DR OrthoDB; 4829736at2759; -.
DR PhylomeDB; Q811Q2; -.
DR PRO; PR:Q811Q2; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
DR GO; GO:0031749; F:D2 dopamine receptor binding; IPI:RGD.
DR GO; GO:0031750; F:D3 dopamine receptor binding; IPI:RGD.
DR GO; GO:0031751; F:D4 dopamine receptor binding; IPI:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR CDD; cd10301; GST_C_CLIC6; 1.
DR CDD; cd03061; GST_N_CLIC; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR002946; CLIC.
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 NCBIfam; TIGR00862; O-ClC; 1.
DR PANTHER; PTHR45476:SF1; CHLORIDE INTRACELLULAR CHANNEL PROTEIN 6; 1.
DR PANTHER; PTHR45476; CHLORIDE INTRACELLULAR CHANNEL PROTEIN 6-RELATED; 1.
DR Pfam; PF13410; GST_C_2; 1.
DR Pfam; PF13409; GST_N_2; 1.
DR PRINTS; PR01263; INTCLCHANNEL.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SFLD; SFLDG00358; Main_(cytGST); 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS50405; GST_CTER; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Chloride; Chloride channel; Cytoplasm; Ion channel;
KW Ion transport; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..612
FT /note="Chloride intracellular channel protein 6"
FT /id="PRO_0000144220"
FT TRANSMEM 397..417
FT /note="Helical; Note=After insertion into the membrane"
FT /evidence="ECO:0000255"
FT DOMAIN 464..612
FT /note="GST C-terminal"
FT REGION 1..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..373
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 612 AA; 64687 MW; E9868AB4BDEF58D0 CRC64;
MAEATEPKEV SSGSQGQPEG AVIEGPGEPG AADLEGREAS EGAAEAPRDL GEGAEAMASG
KEEGGCGQDG EIGEVQAQDP RPGPGTETPG TSGAPGEAEA AECDSEGALI PQSGGGAKRQ
QVQGTSSGLD AQGEAPEVPE DARREPEDPK ASEAGEEAES GQEALGGSAP ESQINPEVQG
PVGDNMDTEA PAGEPQGSEG EPQGGGESSP QPQDEAIEIA AAEVGGHEPG ELAGASAADA
KGEGETLRKD GFEEAAPEEA RVDSGENGFE EAAPEEARVD SGENRDQGRL QEETGEEEAR
PESGLKGPCE EAIQEKAPDG SLDGEEAKST GHEESQVELS NHLAEETSAQ GGEELGRVNG
RRENGPASEE GDLGQEHDIT LFVKAGSDGE SIGNCPFSQR LFMILWLKGV IFNVTTVDLK
RKPADLQNLA PGTNPPFMTF DGEVKTDVNK IEEFLEEKLV PPRYPKLGTQ HPESNSAGND
VFAKFSAFIK NTKKDANDIY EKNLLRALKK LDSYLNSPLP DEIDAYSTED VTVSQRKFLD
GDELTLADCN LLPKLHIIKI VAKKYRGFEF PSEMTGIWRY LNNAYARDEF TNTCPADQEI
EHAYSDAAKR MK
//
