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 11-DEC-2019, entry version 111. 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). CC -!- FUNCTION: Seems to act as a chloride ion channel. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane CC protein {ECO:0000305}. Endoplasmic reticulum {ECO:0000250}. Golgi CC apparatus {ECO:0000250}. Nucleus {ECO:0000250}. 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 IntAct; Q99LI2; 2. 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 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 eggNOG; ENOG410IJAP; Eukaryota. DR eggNOG; ENOG41108E0; LUCA. DR GeneTree; ENSGT00390000016611; -. DR HOGENOM; HOG000231351; -. DR InParanoid; Q99LI2; -. DR KO; K22188; -. DR OrthoDB; 1001950at2759; -. DR ChiTaRS; Clcc1; mouse. DR PRO; PR:Q99LI2; -. DR Proteomes; UP000000589; Chromosome 3. DR RNAct; Q99LI2; protein. DR Bgee; ENSMUSG00000027884; Expressed in 271 organ(s), highest expression level in primary oocyte. 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:0005794; C:Golgi apparatus; ISO:MGI. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI. 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 MOD_RES 429 FT /note="Phosphoserine" FT /evidence="ECO:0000244|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:0000244|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 //