CLCC1_MOUSE
ID CLCC1_MOUSE Reviewed; 539 AA.
AC Q99LI2; A2AEK9;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Chloride channel CLIC-like protein 1;
DE Flags: Precursor;
GN Name=Clcc1;
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 [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Thymus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-429 AND SER-498, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, Spleen, and Testis;
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).
RN [7]
RP FUNCTION, 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 -!- 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 (By
CC similarity). Interacts with CALR (By similarity).
CC {ECO:0000250|UniProtKB:Q96S66}.
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 -!- DISRUPTION PHENOTYPE: Embryonic lethal. {ECO:0000269|PubMed:30157172}.
CC -!- SIMILARITY: Belongs to the chloride channel MCLC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAM17753.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AK169803; BAE41377.1; -; mRNA.
DR EMBL; AK171296; BAE42376.1; -; mRNA.
DR EMBL; AL671917; CAM17753.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL671917; CAM17754.1; -; Genomic_DNA.
DR EMBL; BC003247; AAH03247.1; -; mRNA.
DR CCDS; CCDS17766.1; -.
DR RefSeq; NP_001171242.1; NM_001177771.1.
DR RefSeq; NP_663518.1; NM_145543.2.
DR RefSeq; XP_006501479.1; XM_006501416.3.
DR RefSeq; XP_017175050.1; XM_017319561.1.
DR AlphaFoldDB; Q99LI2; -.
DR BioGRID; 230895; 2.
DR IntAct; Q99LI2; 3.
DR MINT; Q99LI2; -.
DR STRING; 10090.ENSMUSP00000102224; -.
DR iPTMnet; Q99LI2; -.
DR PhosphoSitePlus; Q99LI2; -.
DR SwissPalm; Q99LI2; -.
DR EPD; Q99LI2; -.
DR jPOST; Q99LI2; -.
DR MaxQB; Q99LI2; -.
DR PaxDb; Q99LI2; -.
DR PeptideAtlas; Q99LI2; -.
DR PRIDE; Q99LI2; -.
DR ProteomicsDB; 283375; -.
DR Antibodypedia; 2391; 151 antibodies from 28 providers.
DR DNASU; 229725; -.
DR Ensembl; ENSMUST00000029483; ENSMUSP00000029483; ENSMUSG00000027884.
DR Ensembl; ENSMUST00000106609; ENSMUSP00000102220; ENSMUSG00000027884.
DR GeneID; 229725; -.
DR KEGG; mmu:229725; -.
DR UCSC; uc008qzk.2; mouse.
DR CTD; 23155; -.
DR MGI; MGI:2385186; Clcc1.
DR VEuPathDB; HostDB:ENSMUSG00000027884; -.
DR eggNOG; ENOG502QSP7; Eukaryota.
DR GeneTree; ENSGT00390000016611; -.
DR HOGENOM; CLU_034552_1_1_1; -.
DR InParanoid; Q99LI2; -.
DR OMA; ELWTYVH; -.
DR BioGRID-ORCS; 229725; 8 hits in 71 CRISPR screens.
DR ChiTaRS; Clcc1; mouse.
DR PRO; PR:Q99LI2; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q99LI2; protein.
DR Bgee; ENSMUSG00000027884; Expressed in spermatocyte and 237 other tissues.
DR ExpressionAtlas; Q99LI2; baseline and differential.
DR Genevisible; Q99LI2; MM.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005254; F:chloride channel activity; ISO:MGI.
DR GO; GO:0006821; P:chloride transport; ISO:MGI.
DR InterPro; IPR009231; Chloride_chnl_CLIC-like.
DR PANTHER; PTHR34093; PTHR34093; 1.
DR Pfam; PF05934; MCLC; 1.
PE 1: Evidence at protein level;
KW Chloride; Chloride channel; Endoplasmic reticulum; Golgi apparatus;
KW Ion channel; Ion transport; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..539
FT /note="Chloride channel CLIC-like protein 1"
FT /id="PRO_0000297683"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 41..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 429
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96S66"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96S66"
FT MOD_RES 476
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96S66"
FT MOD_RES 498
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 513
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96S66"
FT MOD_RES 521
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96S66"
SQ SEQUENCE 539 AA; 60621 MW; 252A3E095B56C1C4 CRC64;
MLCRLLLCEC LLLITGYAHD DDWIDPTDML NYDAASGTMR KSQVRSGTSE KKEVSPDSSE
AEELSDCLHR LDSLTHKVDS CEKKKMKDYE SQSNPVFRRY LNKILIEAGK LGLPDENKVE
MRYDAEILLS RQTLLEIQKF LSGEEWKPGA LDDALSDILI NFKCHDSEAW KWQFEDYFGV
DPYNVFMVLL CLLCLVVLVA TELWTYVRWY TQMKRIFIIS FLLSLAWNWI YLYKMAFAQH
QANIAGMEPF DNLCAKKMDW TGSLWEWFTS SWTYKDDPCQ KYYELLIVNP IWLVPPTKAL
AITFTNFVTE PLKHIGKGAG EFIKALMKEI PVLLQIPVLA ILALAVLSFC YGAGRSVPML
RHFGGPDREP PRALEPDDRR RQKGLDYRLH GGAGDADFSY RGPAGSIEQG PYDKMHASKR
DALRQRFHSG NKSPEVLRAF DLPDTEAQEH PEVVPSHKSP IMNTNLETGE LPGESTPTEY
SQSAKDVSGQ VPSAGKSSPT VDKAQLKTDS ECSPPGGCPP SKEAAVAAHG TEPVSSPCG
