CLCC1_HUMAN
ID CLCC1_HUMAN Reviewed; 551 AA.
AC Q96S66; O94861; Q8WYP8; Q8WYP9; Q9BU25;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Chloride channel CLIC-like protein 1;
DE AltName: Full=Mid-1-related chloride channel protein 1;
DE Flags: Precursor;
GN Name=CLCC1; Synonyms=KIAA0761, MCLC;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4).
RX PubMed=11279057; DOI=10.1074/jbc.m100366200;
RA Nagasawa M., Kanzaki M., Iino Y., Morishita Y., Kojima I.;
RT "Identification of a novel chloride channel expressed in the endoplasmic
RT reticulum, Golgi apparatus, and nucleus.";
RL J. Biol. Chem. 276:20413-20418(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Skin;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438; SER-464; SER-509;
RP SER-524 AND SER-532, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-482; SER-524 AND SER-532, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-509, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438; THR-482; SER-509;
RP SER-524 AND SER-532, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH PIGBOS1.
RX PubMed=31653868; DOI=10.1038/s41467-019-12816-z;
RA Chu Q., Martinez T.F., Novak S.W., Donaldson C.J., Tan D., Vaughan J.M.,
RA Chang T., Diedrich J.K., Andrade L., Kim A., Zhang T., Manor U.,
RA Saghatelian A.;
RT "Regulation of the ER stress response by a mitochondrial microprotein.";
RL Nat. Commun. 10:4883-4883(2019).
RN [16]
RP INVOLVEMENT IN RP32.
RX PubMed=16189710; DOI=10.1007/s00439-005-0054-4;
RA Zhang Q., Zulfiqar F., Xiao X., Riazuddin S.A., Ayyagari R., Sabar F.,
RA Caruso R., Sieving P.A., Riazuddin S., Hejtmancik J.F.;
RT "Severe autosomal recessive retinitis pigmentosa maps to chromosome 1p13.3-
RT p21.2 between D1S2896 and D1S457 but outside ABCA4.";
RL Hum. Genet. 118:356-365(2005).
RN [17]
RP INVOLVEMENT IN RP32, VARIANT RP32 GLU-25, FUNCTION, INTERACTION WITH CALR,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND CHARACTERIZATION OF VARIANT
RP RP32 GLU-25.
RX PubMed=30157172; DOI=10.1371/journal.pgen.1007504;
RA Li L., Jiao X., D'Atri I., Ono F., Nelson R., Chan C.C., Nakaya N., Ma Z.,
RA Ma Y., Cai X., Zhang L., Lin S., Hameed A., Chioza B.A., Hardy H., Arno G.,
RA Hull S., Khan M.I., Fasham J., Harlalka G.V., Michaelides M., Moore A.T.,
RA Coban Akdemir Z.H., Jhangiani S., Lupski J.R., Cremers F.P.M., Qamar R.,
RA Salman A., Chilton J., Self J., Ayyagari R., Kabir F., Naeem M.A., Ali M.,
RA Akram J., Sieving P.A., Riazuddin S., Baple E.L., Riazuddin S.A.,
RA Crosby A.H., Hejtmancik J.F.;
RT "Mutation in the intracellular chloride channel CLCC1 associated with
RT autosomal recessive retinitis pigmentosa.";
RL PLoS Genet. 14:E1007504-E1007504(2018).
CC -!- FUNCTION: Seems to act as a chloride ion channel (PubMed:30157172).
CC Plays a role in retina development (PubMed:30157172).
CC {ECO:0000269|PubMed:30157172}.
CC -!- SUBUNIT: Interacts with mitochondrial protein PIGBOS1 (via C-terminus);
CC the interaction occurs at the mitochondria-associated endoplasmic
CC reticulum (ER) membrane, a zone of contact between the ER and
CC mitochondrial membranes, but does not appear to play a role in ER-
CC mitochondria tethering and is not affected by ER stress
CC (PubMed:31653868). Interacts with CALR (PubMed:30157172).
CC {ECO:0000269|PubMed:30157172, ECO:0000269|PubMed:31653868}.
CC -!- INTERACTION:
CC Q96S66; A0A0B4J2F0: PIGBOS1; NbExp=11; IntAct=EBI-2836109, EBI-26657479;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:30157172, ECO:0000269|PubMed:31653868}; Multi-pass
CC membrane protein {ECO:0000255}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9WU61}; Multi-pass membrane protein
CC {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:Q9WU61}; Multi-
CC pass membrane protein {ECO:0000255}. Note=Within the endoplasmic
CC reticulum (ER), localizes to the mitochondria-associated ER membrane, a
CC zone of contact between the ER and mitochondrial membranes.
CC {ECO:0000269|PubMed:31653868}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=hMCLC-1;
CC IsoId=Q96S66-1; Sequence=Displayed;
CC Name=2; Synonyms=hMCLC-2;
CC IsoId=Q96S66-2; Sequence=VSP_027349;
CC Name=3; Synonyms=hMCLC-3;
CC IsoId=Q96S66-3; Sequence=VSP_027348;
CC Name=4; Synonyms=hMCLC-4;
CC IsoId=Q96S66-4; Sequence=VSP_027347;
CC -!- TISSUE SPECIFICITY: Expressed in the retina of the eye, with extensive
CC expression in the lamina cribrosa, optic nerve, ganglion cell layer,
CC inner nuclear layer, outer nuclear layer and retinal pigment
CC epithelium. {ECO:0000269|PubMed:30157172}.
CC -!- DISEASE: Retinitis pigmentosa 32 (RP32) [MIM:609913]: A form of
CC retinitis pigmentosa, a retinal dystrophy belonging to the group of
CC pigmentary retinopathies. Retinitis pigmentosa is characterized by
CC retinal pigment deposits visible on fundus examination and primary loss
CC of rod photoreceptor cells followed by secondary loss of cone
CC photoreceptors. Patients typically have night vision blindness and loss
CC of midperipheral visual field. RP32 inheritance is autosomal recessive.
CC {ECO:0000269|PubMed:16189710, ECO:0000269|PubMed:30157172}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the chloride channel MCLC family. {ECO:0000305}.
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DR EMBL; AB052915; BAB59018.1; -; mRNA.
DR EMBL; AB052916; BAB79261.1; -; mRNA.
DR EMBL; AB052917; BAB79262.1; -; mRNA.
DR EMBL; AB052918; BAB79263.1; -; mRNA.
DR EMBL; AB018304; BAA34481.2; -; mRNA.
DR EMBL; AL449266; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471122; EAW56345.1; -; Genomic_DNA.
DR EMBL; CH471122; EAW56346.1; -; Genomic_DNA.
DR EMBL; BC002939; AAH02939.1; -; mRNA.
DR CCDS; CCDS41362.1; -. [Q96S66-1]
DR CCDS; CCDS60214.1; -. [Q96S66-4]
DR CCDS; CCDS60215.1; -. [Q96S66-3]
DR CCDS; CCDS793.1; -. [Q96S66-2]
DR RefSeq; NP_001041675.1; NM_001048210.2. [Q96S66-1]
DR RefSeq; NP_001265131.1; NM_001278202.1. [Q96S66-3]
DR RefSeq; NP_001265132.1; NM_001278203.1. [Q96S66-4]
DR RefSeq; NP_055942.1; NM_015127.4. [Q96S66-2]
DR AlphaFoldDB; Q96S66; -.
DR BioGRID; 116769; 170.
DR IntAct; Q96S66; 48.
DR MINT; Q96S66; -.
DR STRING; 9606.ENSP00000349456; -.
DR TCDB; 1.A.36.1.1; the intracellular chloride channel (icc) family.
DR iPTMnet; Q96S66; -.
DR MetOSite; Q96S66; -.
DR PhosphoSitePlus; Q96S66; -.
DR SwissPalm; Q96S66; -.
DR BioMuta; CLCC1; -.
DR DMDM; 74752121; -.
DR EPD; Q96S66; -.
DR jPOST; Q96S66; -.
DR MassIVE; Q96S66; -.
DR MaxQB; Q96S66; -.
DR PaxDb; Q96S66; -.
DR PeptideAtlas; Q96S66; -.
DR PRIDE; Q96S66; -.
DR ProteomicsDB; 78077; -. [Q96S66-1]
DR ProteomicsDB; 78078; -. [Q96S66-2]
DR ProteomicsDB; 78079; -. [Q96S66-3]
DR ProteomicsDB; 78080; -. [Q96S66-4]
DR Antibodypedia; 2391; 151 antibodies from 28 providers.
DR DNASU; 23155; -.
DR Ensembl; ENST00000302500.5; ENSP00000306552.4; ENSG00000121940.17. [Q96S66-3]
DR Ensembl; ENST00000348264.6; ENSP00000337243.2; ENSG00000121940.17. [Q96S66-4]
DR Ensembl; ENST00000356970.6; ENSP00000349456.2; ENSG00000121940.17. [Q96S66-1]
DR Ensembl; ENST00000369969.7; ENSP00000358986.3; ENSG00000121940.17. [Q96S66-1]
DR Ensembl; ENST00000369970.8; ENSP00000358987.3; ENSG00000121940.17. [Q96S66-2]
DR Ensembl; ENST00000674849.1; ENSP00000502251.1; ENSG00000121940.17. [Q96S66-1]
DR Ensembl; ENST00000675508.1; ENSP00000502836.1; ENSG00000121940.17. [Q96S66-1]
DR Ensembl; ENST00000675654.1; ENSP00000502648.1; ENSG00000121940.17. [Q96S66-1]
DR Ensembl; ENST00000675956.1; ENSP00000502457.1; ENSG00000121940.17. [Q96S66-1]
DR Ensembl; ENST00000685014.1; ENSP00000510582.1; ENSG00000121940.17. [Q96S66-1]
DR Ensembl; ENST00000685104.1; ENSP00000508473.1; ENSG00000121940.17. [Q96S66-1]
DR Ensembl; ENST00000685497.1; ENSP00000509420.1; ENSG00000121940.17. [Q96S66-1]
DR Ensembl; ENST00000685540.1; ENSP00000510352.1; ENSG00000121940.17. [Q96S66-1]
DR Ensembl; ENST00000685628.1; ENSP00000509075.1; ENSG00000121940.17. [Q96S66-2]
DR Ensembl; ENST00000686078.1; ENSP00000510291.1; ENSG00000121940.17. [Q96S66-1]
DR Ensembl; ENST00000686434.1; ENSP00000508570.1; ENSG00000121940.17. [Q96S66-2]
DR Ensembl; ENST00000686776.1; ENSP00000509013.1; ENSG00000121940.17. [Q96S66-1]
DR Ensembl; ENST00000686821.1; ENSP00000508563.1; ENSG00000121940.17. [Q96S66-1]
DR Ensembl; ENST00000687226.1; ENSP00000509162.1; ENSG00000121940.17. [Q96S66-2]
DR Ensembl; ENST00000687328.1; ENSP00000508816.1; ENSG00000121940.17. [Q96S66-1]
DR Ensembl; ENST00000687449.1; ENSP00000508982.1; ENSG00000121940.17. [Q96S66-1]
DR Ensembl; ENST00000687591.1; ENSP00000509036.1; ENSG00000121940.17. [Q96S66-1]
DR Ensembl; ENST00000687734.1; ENSP00000510543.1; ENSG00000121940.17. [Q96S66-2]
DR Ensembl; ENST00000687865.1; ENSP00000509218.1; ENSG00000121940.17. [Q96S66-1]
DR Ensembl; ENST00000688285.1; ENSP00000509990.1; ENSG00000121940.17. [Q96S66-1]
DR Ensembl; ENST00000688610.1; ENSP00000510524.1; ENSG00000121940.17. [Q96S66-3]
DR Ensembl; ENST00000688778.1; ENSP00000510715.1; ENSG00000121940.17. [Q96S66-1]
DR Ensembl; ENST00000689189.1; ENSP00000510675.1; ENSG00000121940.17. [Q96S66-1]
DR Ensembl; ENST00000689351.1; ENSP00000508607.1; ENSG00000121940.17. [Q96S66-1]
DR Ensembl; ENST00000689359.1; ENSP00000508884.1; ENSG00000121940.17. [Q96S66-1]
DR Ensembl; ENST00000689991.1; ENSP00000508952.1; ENSG00000121940.17. [Q96S66-1]
DR Ensembl; ENST00000690509.1; ENSP00000510142.1; ENSG00000121940.17. [Q96S66-1]
DR Ensembl; ENST00000690756.1; ENSP00000509544.1; ENSG00000121940.17. [Q96S66-1]
DR Ensembl; ENST00000690781.1; ENSP00000510137.1; ENSG00000121940.17. [Q96S66-1]
DR Ensembl; ENST00000690874.1; ENSP00000510602.1; ENSG00000121940.17. [Q96S66-1]
DR Ensembl; ENST00000691513.1; ENSP00000509584.1; ENSG00000121940.17. [Q96S66-1]
DR Ensembl; ENST00000691556.1; ENSP00000509451.1; ENSG00000121940.17. [Q96S66-1]
DR Ensembl; ENST00000691731.1; ENSP00000509533.1; ENSG00000121940.17. [Q96S66-1]
DR Ensembl; ENST00000692404.1; ENSP00000510666.1; ENSG00000121940.17. [Q96S66-1]
DR Ensembl; ENST00000692511.1; ENSP00000510067.1; ENSG00000121940.17. [Q96S66-1]
DR Ensembl; ENST00000692795.1; ENSP00000509960.1; ENSG00000121940.17. [Q96S66-1]
DR Ensembl; ENST00000693089.1; ENSP00000509330.1; ENSG00000121940.17. [Q96S66-1]
DR Ensembl; ENST00000693336.1; ENSP00000509936.1; ENSG00000121940.17. [Q96S66-1]
DR Ensembl; ENST00000693673.1; ENSP00000509782.1; ENSG00000121940.17. [Q96S66-1]
DR GeneID; 23155; -.
DR KEGG; hsa:23155; -.
DR MANE-Select; ENST00000369969.7; ENSP00000358986.3; NM_001377458.1; NP_001364387.1.
DR UCSC; uc009wes.2; human. [Q96S66-1]
DR CTD; 23155; -.
DR DisGeNET; 23155; -.
DR GeneCards; CLCC1; -.
DR HGNC; HGNC:29675; CLCC1.
DR HPA; ENSG00000121940; Low tissue specificity.
DR MalaCards; CLCC1; -.
DR MIM; 609913; phenotype.
DR MIM; 617539; gene.
DR neXtProt; NX_Q96S66; -.
DR OpenTargets; ENSG00000121940; -.
DR PharmGKB; PA142672105; -.
DR VEuPathDB; HostDB:ENSG00000121940; -.
DR eggNOG; ENOG502QSP7; Eukaryota.
DR GeneTree; ENSGT00390000016611; -.
DR HOGENOM; CLU_034552_1_1_1; -.
DR InParanoid; Q96S66; -.
DR OMA; ELWTYVH; -.
DR PhylomeDB; Q96S66; -.
DR TreeFam; TF328890; -.
DR PathwayCommons; Q96S66; -.
DR SignaLink; Q96S66; -.
DR SIGNOR; Q96S66; -.
DR BioGRID-ORCS; 23155; 88 hits in 1082 CRISPR screens.
DR ChiTaRS; CLCC1; human.
DR GeneWiki; CLCC1; -.
DR GenomeRNAi; 23155; -.
DR Pharos; Q96S66; Tbio.
DR PRO; PR:Q96S66; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q96S66; protein.
DR Bgee; ENSG00000121940; Expressed in tendon of biceps brachii and 200 other tissues.
DR ExpressionAtlas; Q96S66; baseline and differential.
DR Genevisible; Q96S66; HS.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005254; F:chloride channel activity; IBA:GO_Central.
DR InterPro; IPR009231; Chloride_chnl_CLIC-like.
DR PANTHER; PTHR34093; PTHR34093; 1.
DR Pfam; PF05934; MCLC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloride; Chloride channel; Endoplasmic reticulum;
KW Golgi apparatus; Ion channel; Ion transport; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Retinitis pigmentosa; Signal;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..551
FT /note="Chloride channel CLIC-like protein 1"
FT /id="PRO_0000297682"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 363..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 464
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 482
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 532
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 114..298
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11279057"
FT /id="VSP_027347"
FT VAR_SEQ 114..234
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11279057"
FT /id="VSP_027348"
FT VAR_SEQ 114..163
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11279057,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_027349"
FT VARIANT 25
FT /note="D -> E (in RP32; reduces ion channel activity; no
FT impact on interaction with CALR; no impact on ER
FT localization; dbSNP:rs750180668)"
FT /evidence="ECO:0000269|PubMed:30157172"
FT /id="VAR_083125"
FT VARIANT 368
FT /note="S -> R (in dbSNP:rs168107)"
FT /id="VAR_034673"
SQ SEQUENCE 551 AA; 62023 MW; 08709A80E99F2E15 CRC64;
MLCSLLLCEC LLLVAGYAHD DDWIDPTDML NYDAASGTMR KSQAKYGISG EKDVSPDLSC
ADEISECYHK LDSLTYKIDE CEKKKREDYE SQSNPVFRRY LNKILIEAGK LGLPDENKGD
MHYDAEIILK RETLLEIQKF LNGEDWKPGA LDDALSDILI NFKFHDFETW KWRFEDSFGV
DPYNVLMVLL CLLCIVVLVA TELWTYVRWY TQLRRVLIIS FLFSLGWNWM YLYKLAFAQH
QAEVAKMEPL NNVCAKKMDW TGSIWEWFRS SWTYKDDPCQ KYYELLLVNP IWLVPPTKAL
AVTFTTFVTE PLKHIGKGTG EFIKALMKEI PALLHLPVLI IMALAILSFC YGAGKSVHVL
RHIGGPESEP PQALRPRDRR RQEEIDYRPD GGAGDADFHY RGQMGPTEQG PYAKTYEGRR
EILRERDVDL RFQTGNKSPE VLRAFDVPDA EAREHPTVVP SHKSPVLDTK PKETGGILGE
GTPKESSTES SQSAKPVSGQ DTSGNTEGSP AAEKAQLKSE AAGSPDQGST YSPARGVAGP
RGQDPVSSPC G
