CLIC6_MOUSE
ID CLIC6_MOUSE Reviewed; 596 AA.
AC Q8BHB9;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Chloride intracellular channel protein 6;
GN Name=Clic6;
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 [MRNA].
RX PubMed=14597386; DOI=10.1016/s0378-1119(03)00830-8;
RA Friedli M., Guipponi M., Bertrand S., Bertrand D., Neerman-Arbez M.,
RA Scott H.S., Antonarakis S.E., Reymond A.;
RT "Identification of a novel member of the CLIC family, CLIC6, mapping to
RT 21q22.12.";
RL Gene 320:31-40(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
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:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
CC Note=Predominantly cytoplasmic. Upon chloride ion efflux from the cell,
CC it is translocated to the plasma membrane (By similarity).
CC {ECO:0000250}.
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:0000250}.
CC -!- SIMILARITY: Belongs to the chloride channel CLIC family. {ECO:0000305}.
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DR EMBL; AF448440; AAN76731.1; -; mRNA.
DR EMBL; AK077599; BAC36890.1; -; mRNA.
DR EMBL; BC075706; AAH75706.1; -; mRNA.
DR CCDS; CCDS28338.1; -.
DR RefSeq; NP_766057.1; NM_172469.3.
DR PDB; 6ERY; X-ray; 1.79 A; A/B=363-596.
DR PDB; 6ERZ; X-ray; 1.92 A; A/B=363-596.
DR PDBsum; 6ERY; -.
DR PDBsum; 6ERZ; -.
DR AlphaFoldDB; Q8BHB9; -.
DR SMR; Q8BHB9; -.
DR STRING; 10090.ENSMUSP00000023670; -.
DR iPTMnet; Q8BHB9; -.
DR PhosphoSitePlus; Q8BHB9; -.
DR EPD; Q8BHB9; -.
DR jPOST; Q8BHB9; -.
DR MaxQB; Q8BHB9; -.
DR PaxDb; Q8BHB9; -.
DR PeptideAtlas; Q8BHB9; -.
DR PRIDE; Q8BHB9; -.
DR ProteomicsDB; 279106; -.
DR Antibodypedia; 8114; 197 antibodies from 26 providers.
DR DNASU; 209195; -.
DR Ensembl; ENSMUST00000023670; ENSMUSP00000023670; ENSMUSG00000022949.
DR GeneID; 209195; -.
DR KEGG; mmu:209195; -.
DR UCSC; uc007zzg.1; mouse.
DR CTD; 54102; -.
DR MGI; MGI:2146607; Clic6.
DR VEuPathDB; HostDB:ENSMUSG00000022949; -.
DR eggNOG; KOG1422; Eukaryota.
DR GeneTree; ENSGT00940000159602; -.
DR HOGENOM; CLU_023994_0_0_1; -.
DR InParanoid; Q8BHB9; -.
DR OMA; QGASMEA; -.
DR OrthoDB; 974249at2759; -.
DR PhylomeDB; Q8BHB9; -.
DR TreeFam; TF315438; -.
DR BioGRID-ORCS; 209195; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Clic6; mouse.
DR PRO; PR:Q8BHB9; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q8BHB9; protein.
DR Bgee; ENSMUSG00000022949; Expressed in choroid plexus epithelium and 177 other tissues.
DR ExpressionAtlas; Q8BHB9; baseline and differential.
DR Genevisible; Q8BHB9; MM.
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; ISO:MGI.
DR GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
DR GO; GO:0031749; F:D2 dopamine receptor binding; ISO:MGI.
DR GO; GO:0031750; F:D3 dopamine receptor binding; ISO:MGI.
DR GO; GO:0031751; F:D4 dopamine receptor binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
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; 2.
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 3D-structure; Cell membrane; Chloride; Chloride channel; Cytoplasm;
KW Ion channel; Ion transport; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel.
FT CHAIN 1..596
FT /note="Chloride intracellular channel protein 6"
FT /id="PRO_0000144218"
FT TRANSMEM 381..401
FT /note="Helical; Note=After insertion into the membrane"
FT /evidence="ECO:0000255"
FT DOMAIN 448..596
FT /note="GST C-terminal"
FT REGION 1..360
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 137..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q811Q2"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q811Q2"
FT STRAND 363..369
FT /evidence="ECO:0007829|PDB:6ERY"
FT STRAND 373..376
FT /evidence="ECO:0007829|PDB:6ERY"
FT HELIX 380..392
FT /evidence="ECO:0007829|PDB:6ERY"
FT STRAND 396..401
FT /evidence="ECO:0007829|PDB:6ERY"
FT STRAND 421..424
FT /evidence="ECO:0007829|PDB:6ERY"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:6ERY"
FT HELIX 432..442
FT /evidence="ECO:0007829|PDB:6ERY"
FT TURN 445..447
FT /evidence="ECO:0007829|PDB:6ERY"
FT HELIX 457..460
FT /evidence="ECO:0007829|PDB:6ERY"
FT TURN 461..464
FT /evidence="ECO:0007829|PDB:6ERY"
FT HELIX 465..474
FT /evidence="ECO:0007829|PDB:6ERY"
FT HELIX 478..480
FT /evidence="ECO:0007829|PDB:6ERY"
FT HELIX 481..500
FT /evidence="ECO:0007829|PDB:6ERY"
FT STRAND 521..527
FT /evidence="ECO:0007829|PDB:6ERY"
FT HELIX 530..550
FT /evidence="ECO:0007829|PDB:6ERY"
FT HELIX 559..569
FT /evidence="ECO:0007829|PDB:6ERY"
FT HELIX 572..575
FT /evidence="ECO:0007829|PDB:6ERY"
FT HELIX 581..587
FT /evidence="ECO:0007829|PDB:6ERY"
FT HELIX 589..592
FT /evidence="ECO:0007829|PDB:6ERY"
SQ SEQUENCE 596 AA; 62886 MW; 34B57EDC543841DA CRC64;
MAEATEPKEV APGSQGQPEG ATIEGPGEPG AADLEGREAS EEAAEAPRDL GAGVEARASG
KEEGGCGQDE GTGGAQAQDP RTGPEAETPG ASGAPGEAEA AERDPEGAIP QGAEEAPSAQ
QVQGMSSGLD SQGEAPEVPG DSRREPEDPT ASEAGEEAES GQEAQGGGAL GLQINPEVQG
LAGDNMDTEA PAGGPLGSES EPQGGGESSP QPQDEAIEIV TTEIGGNESG ELAGASAADA
AGEGETLGKD GSEEAASEDA RVDAHENGDQ GKLQEETGEE EARPEPELKG PCEGAIQEKP
PDGSLDGEEA KSTEHEEESQ AELSNHLAEE PSVQGGEELG RVNGRRENGP ALEEGDPGQE
HDITLFVKAG YDGESIGNCP FSQRLFMILW LKGVIFNVTT VDLKRKPADL QNLAPGTNPP
FMTFDGEVKT DVNKIEEFLE EKLVPPRYPK LGTQHPESNS AGNDVFAKFS AFIKNTKKDA
NEIYEKNLLR ALKKLDSYLN SPLPDEIDAD SSEDVTVSQR KFLDGDELTL ADCNLLPKLH
IIKIVAKKYR DFEFPSEMTG IWRYLNNAYA RDEFTNTCPA DREIEHAYSD AAKRMK
