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 27-MAR-2024, entry version 131. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 3. 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; 10090-ENSMUSP00000102224; -. DR PeptideAtlas; Q99LI2; -. DR ProteomicsDB; 283375; -. DR Pumba; Q99LI2; -. DR Antibodypedia; 2391; 172 antibodies from 29 providers. DR DNASU; 229725; -. DR Ensembl; ENSMUST00000029483.15; ENSMUSP00000029483.9; ENSMUSG00000027884.17. DR Ensembl; ENSMUST00000106609.8; ENSMUSP00000102220.2; ENSMUSG00000027884.17. DR GeneID; 229725; -. DR KEGG; mmu:229725; -. DR UCSC; uc008qzk.2; mouse. DR AGR; MGI:2385186; -. 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; TELWTYI; -. DR OrthoDB; 3823720at2759; -. DR BioGRID-ORCS; 229725; 8 hits in 76 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 240 other cell types or 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; CHLORIDE CHANNEL CLIC-LIKE PROTEIN 1; 1. DR PANTHER; PTHR34093:SF1; CHLORIDE CHANNEL CLIC-LIKE PROTEIN 1; 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 //