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Database: UniProt
Entry: F6VJL1_MONDO
LinkDB: F6VJL1_MONDO
Original site: F6VJL1_MONDO 
ID   F6VJL1_MONDO            Unreviewed;       710 AA.
AC   F6VJL1;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 2.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=Chloride intracellular channel protein {ECO:0000256|RuleBase:RU362009};
GN   Name=CLIC6 {ECO:0000313|Ensembl:ENSMODP00000026323.2};
OS   Monodelphis domestica (Gray short-tailed opossum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX   NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000026323.2, ECO:0000313|Proteomes:UP000002280};
RN   [1] {ECO:0000313|Ensembl:ENSMODP00000026323.2, ECO:0000313|Proteomes:UP000002280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17495919; DOI=10.1038/nature05805;
RA   Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L., Duke S.,
RA   Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J., Kamal M.,
RA   Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A., Benos P.V.,
RA   Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L., Deakin J.E.,
RA   Fazzari M.J., Glass J.L., Grabherr M., Greally J.M., Gu W., Hore T.A.,
RA   Huttley G.A., Kleber M., Jirtle R.L., Koina E., Lee J.T., Mahony S.,
RA   Marra M.A., Miller R.D., Nicholls R.D., Oda M., Papenfuss A.T., Parra Z.E.,
RA   Pollock D.D., Ray D.A., Schein J.E., Speed T.P., Thompson K.,
RA   VandeBerg J.L., Wade C.M., Walker J.A., Waters P.D., Webber C.,
RA   Weidman J.R., Xie X., Zody M.C., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Bloom T., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M.,
RA   Samollow P.B., Lander E.S., Lindblad-Toh K.;
RT   "Genome of the marsupial Monodelphis domestica reveals innovation in non-
RT   coding sequences.";
RL   Nature 447:167-177(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMODP00000026323.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362009}; Single-
CC       pass membrane protein {ECO:0000256|RuleBase:RU362009}. Cytoplasm
CC       {ECO:0000256|RuleBase:RU362009}.
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. {ECO:0000256|RuleBase:RU362009}.
CC   -!- SIMILARITY: Belongs to the chloride channel CLIC family.
CC       {ECO:0000256|ARBA:ARBA00007655, ECO:0000256|RuleBase:RU362009}.
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DR   RefSeq; XP_001376468.1; XM_001376431.3.
DR   AlphaFoldDB; F6VJL1; -.
DR   SMR; F6VJL1; -.
DR   STRING; 13616.ENSMODP00000026323; -.
DR   Ensembl; ENSMODT00000026791.3; ENSMODP00000026323.2; ENSMODG00000021052.3.
DR   KEGG; mdo:100025586; -.
DR   CTD; 54102; -.
DR   eggNOG; KOG1422; Eukaryota.
DR   GeneTree; ENSGT00940000159602; -.
DR   HOGENOM; CLU_023994_0_0_1; -.
DR   InParanoid; F6VJL1; -.
DR   OMA; ERRENWG; -.
DR   OrthoDB; 103277at2759; -.
DR   TreeFam; TF315438; -.
DR   Proteomes; UP000002280; Chromosome 4.
DR   Bgee; ENSMODG00000021052; Expressed in placenta and 12 other cell types or tissues.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0031749; F:D2 dopamine receptor binding; IBA:GO_Central.
DR   GO; GO:0031750; F:D3 dopamine receptor binding; IBA:GO_Central.
DR   GO; GO:0031751; F:D4 dopamine receptor binding; IBA:GO_Central.
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; 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   3: Inferred from homology;
KW   Chloride {ECO:0000256|ARBA:ARBA00023214, ECO:0000256|RuleBase:RU362009};
KW   Chloride channel {ECO:0000256|ARBA:ARBA00023173,
KW   ECO:0000256|RuleBase:RU362009}; Cytoplasm {ECO:0000256|RuleBase:RU362009};
KW   Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000256|RuleBase:RU362009};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU362009}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002280};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Transport {ECO:0000256|RuleBase:RU362009};
KW   Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882,
KW   ECO:0000256|RuleBase:RU362009}.
FT   DOMAIN          539..710
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
FT   REGION          1..463
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..59
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..164
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        237..259
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        260..275
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        276..305
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        361..388
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        389..408
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        421..443
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   710 AA;  78540 MW;  81332222D9F52AB1 CRC64;
     MTEAAEPVVR LPAPKENADL PGLLEKGIGE LGPDTVAKEE EQETEVKYNE KKQSSEEDAT
     GDGEGAVTPA ESLKEAREEA GATIVQIDQR VGEERKTLTQ NDWEKDSLKK QEDKARESPR
     NAEEQIEQQK WEKEERNELL HDVEVEGISR EGRRELEGSS STEHQRQQEE SQGAAKGTED
     PGDPETQTVV GAEHSVGGEA AVETTAAARV ASQETVQEGV KLLQPEGQLT EPAAGMEAEG
     LDREREKRLE DRDSENGESS GGEENSSVQQ TEFEGTSARE QKEGEVDDQP SLEESPTRDS
     LTDEAQENEA PQGVRYPESA EVEAAVGPAQ EESGGLEDVK ADATGGDPEE AVQAEYASLR
     AKTDVQEEAI EEGKENWGKE KGNIEVMTEG EEENFDGSPQ EEDEEENEKT IPERNLDTEL
     SNHLSESSSE DAPAEAETNK QGTRLNGAEE EGEASEEEAS VERTSAPVLA AGNEHDISLF
     VKAGYDGESI GNCPFSQRLF MILWLKGVIF NVTTVDLKRK PADLQDLAPG TNPPFMTFDG
     EVKTDVNKIE EFLEEKLAPP RYPKLGTQHM ESNSAGNDVF AKFSAFIKNT RKDANENLEK
     NLIKALKKLD NYLNTPLPDE IDAYSTEDIT VSNRKFLDGN ELSLADCNLL PKLHIIKIVA
     KKYRNFEFPT EMTGLWRYLN NAYTRDEFTN TCPADREIEY AYSDVAKRMK
//
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