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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
 
 
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