CLIC3_MOUSE
ID CLIC3_MOUSE Reviewed; 237 AA.
AC Q9D7P7;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Chloride intracellular channel protein 3;
GN Name=Clic3;
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=C57BL/6J; TISSUE=Tongue;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
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: Can insert into membranes and form chloride ion channels. May
CC participate in cellular growth control (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Associated with the C-terminal of MAPK15.
CC {ECO:0000250|UniProtKB:O95833}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Note=Predominantly nuclear. Some protein was found in the cytoplasm.
CC Exists both as soluble cytoplasmic protein and as membrane protein with
CC probably a single transmembrane domain (By similarity). {ECO:0000250}.
CC -!- DOMAIN: Members of this family may change from a globular, soluble
CC state to a state where the N-terminal domain is inserted into the
CC membrane and functions as chloride channel. A conformation change of
CC the N-terminal domain is thought to expose hydrophobic surfaces that
CC trigger membrane insertion (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the chloride channel CLIC family. {ECO:0000305}.
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DR EMBL; AK009020; BAB26030.2; -; mRNA.
DR CCDS; CCDS15774.1; -.
DR RefSeq; NP_081361.1; NM_027085.3.
DR AlphaFoldDB; Q9D7P7; -.
DR SMR; Q9D7P7; -.
DR STRING; 10090.ENSMUSP00000109904; -.
DR PhosphoSitePlus; Q9D7P7; -.
DR MaxQB; Q9D7P7; -.
DR PaxDb; Q9D7P7; -.
DR PRIDE; Q9D7P7; -.
DR ProteomicsDB; 283384; -.
DR Antibodypedia; 991; 233 antibodies from 31 providers.
DR DNASU; 69454; -.
DR Ensembl; ENSMUST00000114265; ENSMUSP00000109904; ENSMUSG00000015093.
DR GeneID; 69454; -.
DR KEGG; mmu:69454; -.
DR UCSC; uc008isd.1; mouse.
DR CTD; 9022; -.
DR MGI; MGI:1916704; Clic3.
DR VEuPathDB; HostDB:ENSMUSG00000015093; -.
DR eggNOG; KOG1422; Eukaryota.
DR GeneTree; ENSGT00940000161243; -.
DR HOGENOM; CLU_061051_1_0_1; -.
DR InParanoid; Q9D7P7; -.
DR OMA; HYRRFGI; -.
DR OrthoDB; 1347811at2759; -.
DR PhylomeDB; Q9D7P7; -.
DR TreeFam; TF315438; -.
DR BioGRID-ORCS; 69454; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Clic3; mouse.
DR PRO; PR:Q9D7P7; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9D7P7; protein.
DR Bgee; ENSMUSG00000015093; Expressed in lip and 93 other tissues.
DR ExpressionAtlas; Q9D7P7; baseline and differential.
DR Genevisible; Q9D7P7; MM.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005254; F:chloride channel activity; ISS:UniProtKB.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0006821; P:chloride transport; ISS:UniProtKB.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR InterPro; IPR002946; CLIC.
DR InterPro; IPR030261; CLIC-3.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR43920:SF3; PTHR43920:SF3; 1.
DR Pfam; PF13409; GST_N_2; 1.
DR PRINTS; PR01263; INTCLCHANNEL.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 1: Evidence at protein level;
KW Chloride; Chloride channel; Cytoplasm; Disulfide bond; Ion channel;
KW Ion transport; Membrane; Nucleus; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..237
FT /note="Chloride intracellular channel protein 3"
FT /id="PRO_0000144208"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 13..91
FT /note="GST N-terminal"
FT DOMAIN 92..236
FT /note="GST C-terminal"
FT REGION 1..89
FT /note="Required for insertion into the membrane"
FT /evidence="ECO:0000250"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95833"
FT DISULFID 23..26
FT /note="In soluble form"
FT /evidence="ECO:0000250"
SQ SEQUENCE 237 AA; 26846 MW; E1C3BA1754654191 CRC64;
MAETTKLQLF VKASEDGESV GHCPSCQRLF MVLLLKGVPF TLTTVDTRRA LDVLKDFAPG
SQLPILLYDG DVKTDTLQIE EFLEETLGPP DFPSLAPRYR ESNTAGNDIF HKFSAFIKNP
VPTQDNALYQ QLLRALTRLD SYLRAPLDHE LAQEPHLRES HRRFLDGDQF TLADCSLLPK
LHIVDTVCAH FRQLPIPAEL SCVRRYLDSA LQKKEFKYTC PHSAEILAAY QPAVHPR
