CLCC1_DANRE
ID CLCC1_DANRE Reviewed; 609 AA.
AC A0A2R8Q3S9;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2018, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=Chloride channel CLIC-like protein 1 {ECO:0000305};
DE Flags: Precursor;
GN Name=clcc1 {ECO:0000303|PubMed:30157172};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000312|Proteomes:UP000000437};
RN [1] {ECO:0000312|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000312|Proteomes:UP000000437};
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 207-526.
RA Mathavan S., Yao F., Wong E., Thoreau H., Nayudu M., Govindarajan K.R.,
RA Ruan Y., Wei C.;
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
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 (By similarity). Plays
CC a role in retina development (PubMed:30157172).
CC {ECO:0000250|UniProtKB:Q9WU61, ECO:0000269|PubMed:30157172}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9WU61}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9WU61};
CC Multi-pass membrane protein {ECO:0000255}. Nucleus membrane
CC {ECO:0000250|UniProtKB:Q9WU61}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Within the endoplasmic reticulum (ER), localizes to
CC the mitochondria-associated ER membrane, a zone of contact between the
CC ER and mitochondrial membranes. {ECO:0000250|UniProtKB:Q96S66}.
CC -!- TISSUE SPECIFICITY: Expressed in the hindbrain, swim bladder and the
CC eye at 1 day post fertilization (dpf) with increased expression at 3
CC dpf (PubMed:30157172). At 3 dpf, most prominent expression in the
CC retina, with strong exxpression in the ganglion cell layer, outer
CC nuclear layer and the retinal pigmented epithelium (PubMed:30157172).
CC {ECO:0000269|PubMed:30157172}.
CC -!- DISRUPTION PHENOTYPE: Knockout leads to lethality at 11 dpf, with
CC knockout larvae exhibiting abnormalities in various retinal layers
CC including the inner plexiform layer, the outer nuclear layer and the
CC rod photoreceptor layer and decreased function of the photoreceptor
CC cone cells (PubMed:30157172). Morpholino knockdown results in reduced
CC eye size with proportionately decreased lens size, thinner inner
CC plexiform layer and outer nuclear layer after 36 hours post
CC fertilization (hpf) (PubMed:30157172). No change in the inner nuclear
CC layer, but increased apparent thickness of the ganglion cell layer
CC (PubMed:30157172). Reduced number of rod cells, with existing rod cells
CC exhibiting an abnormal morphology or pyknotic appearance, decreased
CC opsin levels and disrupted photoreceptor cell bodies (PubMed:30157172).
CC {ECO:0000269|PubMed:30157172}.
CC -!- SIMILARITY: Belongs to the chloride channel MCLC family. {ECO:0000305}.
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DR EMBL; CU655842; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU693480; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; EH475966; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_009294671.1; XM_009296396.2.
DR AlphaFoldDB; A0A2R8Q3S9; -.
DR STRING; 7955.ENSDARP00000107966; -.
DR Ensembl; ENSDART00000180240; ENSDARP00000147377; ENSDARG00000100186.
DR GeneID; 100332460; -.
DR KEGG; dre:100332460; -.
DR CTD; 23155; -.
DR GeneTree; ENSGT00940000165672; -.
DR PRO; PR:A0A2R8Q3S9; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 22.
DR Bgee; ENSDARG00000100186; Expressed in mature ovarian follicle and 19 other tissues.
DR ExpressionAtlas; A0A2R8Q3S9; baseline.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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 2: Evidence at transcript level;
KW Chloride; Chloride channel; Endoplasmic reticulum; Golgi apparatus;
KW Ion channel; Ion transport; Membrane; Nucleus; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..609
FT /note="Chloride channel CLIC-like protein 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000449248"
FT TRANSMEM 212..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 358..380
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 398..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..470
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..536
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 212
FT /note="V -> G (in Ref. 2; EH475966)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="Y -> C (in Ref. 2; EH475966)"
FT /evidence="ECO:0000305"
FT CONFLICT 515
FT /note="E -> G (in Ref. 2; EH475966)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 609 AA; 69946 MW; 766E33298E667131 CRC64;
MKLSSSSSFG LCILVVFFCF VVIESAKIRI DGYNDEAWID PYDMLNYDPT TKRMRKSTES
ESYQNVPTKR REFNSESCDV PKCPDEHECI KKLHILQKEF DEQKSKSTAT LSKPVCLPVF
KRFLSKLLKE TSKLGLPDDG ITAMHYDAEV KLSKQSLAEI QKLLNDEDGW TTGAMDEALS
QILVQFKLHD YEAWKWRFED TFHVDVDTVL KVSLIVLIIV AIICTQLWSV VSWFVQFRRM
FAVSFFISLI WNWFHLYMLA FAEHKKNIVQ VESFNAKCTG LKQLNWQDSL SEWYRRTWTL
QDDPCKKYYE VLVVNPILLV PPTKAITITI TNFITDPLKH IGEGISEFLR ALLKDLPVTL
QIPVLIIIIL AILIFVYGSA QAAIHQVARF PRLGWRQEQP PPAVGQRQNP QLRAHEEPWE
GGDARQPLPM RQDNRGNHVG NRGDQGFRDA NAPENREEDR SMDIRQEFST KRTPVETLQA
TGNTFPDDET DSQQRTQELD SGANVEEEVK VEEKEKKESF SVDNKEQKET KSPDRSEPIT
SEPPSSIDVK TVGADQGNEH LMCTKRKWAA QNGFKLQVIL CEINSEASAD LPEEEECFSF
KHPVQETQS
