CLIC2_HUMAN
ID CLIC2_HUMAN Reviewed; 247 AA.
AC O15247; A8K9S0; O15174; Q5JT80; Q8TCE3;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 3.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Chloride intracellular channel protein 2;
DE AltName: Full=XAP121;
GN Name=CLIC2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=9339381; DOI=10.1006/geno.1997.4922;
RA Heiss N.S., Poustka A.;
RT "Genomic structure of a novel chloride channel gene, CLIC2, in Xq28.";
RL Genomics 45:224-228(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [6]
RP INTERACTION WITH TRAPPC2.
RX PubMed=12681486; DOI=10.1016/s0014-5793(03)00228-x;
RA Fan L., Yu W., Zhu X.;
RT "Interaction of sedlin with chloride intracellular channel proteins.";
RL FEBS Lett. 540:77-80(2003).
RN [7]
RP FUNCTION, SUBUNIT, 3D-STRUCTURE MODELING, TISSUE SPECIFICITY, AND
RP INTERACTION WITH RYR2.
RX PubMed=15147738; DOI=10.1016/j.biocel.2004.01.026;
RA Board P.G., Coggan M., Watson S., Gage P.W., Dulhunty A.F.;
RT "CLIC-2 modulates cardiac ryanodine receptor Ca2+ release channels.";
RL Int. J. Biochem. Cell Biol. 36:1599-1612(2004).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RYR2.
RX PubMed=15916532; DOI=10.1042/bj20042113;
RA Dulhunty A.F., Pouliquin P., Coggan M., Gage P.W., Board P.G.;
RT "A recently identified member of the glutathione transferase structural
RT family modifies cardiac RyR2 substate activity, coupled gating and
RT activation by Ca2+ and ATP.";
RL Biochem. J. 390:333-343(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP TISSUE SPECIFICITY, VARIANT MRXS32 GLN-101, AND CHARACTERIZATION OF VARIANT
RP MRXS32 GLN-101.
RX PubMed=22814392; DOI=10.1093/hmg/dds292;
RA Takano K., Liu D., Tarpey P., Gallant E., Lam A., Witham S., Alexov E.,
RA Chaubey A., Stevenson R.E., Schwartz C.E., Board P.G., Dulhunty A.F.;
RT "An X-linked channelopathy with cardiomegaly due to a CLIC2 mutation
RT enhancing ryanodine receptor channel activity.";
RL Hum. Mol. Genet. 21:4497-4507(2012).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE,
RP SUBUNIT, FUNCTION, PH DEPENDENCE, AND DISULFIDE BOND.
RX PubMed=17945253; DOI=10.1016/j.jmb.2007.09.041;
RA Cromer B.A., Gorman M.A., Hansen G., Adams J.J., Coggan M., Littler D.R.,
RA Brown L.J., Mazzanti M., Breit S.N., Curmi P.M.G., Dulhunty A.F.,
RA Board P.G., Parker M.W.;
RT "Structure of the Janus protein human CLIC2.";
RL J. Mol. Biol. 374:719-731(2007).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND DISULFIDE BOND.
RX PubMed=18186468; DOI=10.1002/prot.21922;
RA Mi W., Liang Y.-H., Li L., Su X.-D.;
RT "The crystal structure of human chloride intracellular channel protein 2: a
RT disulfide bond with functional implications.";
RL Proteins 71:509-513(2008).
CC -!- FUNCTION: Can insert into membranes and form chloride ion channels.
CC Channel activity depends on the pH. Membrane insertion seems to be
CC redox-regulated and may occur only under oxydizing conditions.
CC Modulates the activity of RYR2 and inhibits calcium influx.
CC {ECO:0000269|PubMed:15147738, ECO:0000269|PubMed:15916532,
CC ECO:0000269|PubMed:17945253}.
CC -!- SUBUNIT: Monomer. Interacts with TRAPPC2 and RYR2.
CC {ECO:0000269|PubMed:12681486, ECO:0000269|PubMed:15147738,
CC ECO:0000269|PubMed:15916532, ECO:0000269|PubMed:17945253}.
CC -!- INTERACTION:
CC O15247; Q4KMQ1-2: TPRN; NbExp=3; IntAct=EBI-6286019, EBI-11978969;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15916532}. Membrane
CC {ECO:0000305|PubMed:15916532}; Single-pass membrane protein
CC {ECO:0000305|PubMed:15916532}. Note=Exists both as soluble cytoplasmic
CC protein and as membrane protein with probably a single transmembrane
CC domain.
CC -!- TISSUE SPECIFICITY: Expressed in adult and fetal brain, heart, skeletal
CC muscle, liver, lung, and spleen. Detected in adult stomach and testis.
CC Expressed in fetal thymus and kidney. {ECO:0000269|PubMed:15147738,
CC ECO:0000269|PubMed:22814392}.
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.
CC -!- DISEASE: Intellectual developmental disorder, X-linked, syndromic 32
CC (MRXS32) [MIM:300886]: A syndrome characterized by profound
CC intellectual deficit, delayed psychomotor development beginning in
CC infancy and little or no speech development. Additional features
CC include seizures, large joint contractures, and abnormal positioning of
CC the thumbs. {ECO:0000269|PubMed:22814392}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the chloride channel CLIC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA73228.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Y12696; CAA73228.1; ALT_FRAME; mRNA.
DR EMBL; AJ000217; CAA03948.1; -; Genomic_DNA.
DR EMBL; AJ000218; CAA03948.1; JOINED; Genomic_DNA.
DR EMBL; AJ000219; CAA03948.1; JOINED; Genomic_DNA.
DR EMBL; AK292785; BAF85474.1; -; mRNA.
DR EMBL; AL356738; CAI41464.1; -; Genomic_DNA.
DR EMBL; CH471172; EAW72624.1; -; Genomic_DNA.
DR EMBL; BC022305; AAH22305.1; -; mRNA.
DR CCDS; CCDS14767.1; -.
DR RefSeq; NP_001280.3; NM_001289.5.
DR PDB; 2PER; X-ray; 2.00 A; A=1-247.
DR PDB; 2R4V; X-ray; 1.85 A; A=1-247.
DR PDB; 2R5G; X-ray; 1.86 A; A=1-247.
DR PDBsum; 2PER; -.
DR PDBsum; 2R4V; -.
DR PDBsum; 2R5G; -.
DR AlphaFoldDB; O15247; -.
DR SMR; O15247; -.
DR BioGRID; 107605; 17.
DR IntAct; O15247; 4.
DR STRING; 9606.ENSP00000358460; -.
DR TCDB; 1.A.12.1.5; the intracellular chloride channel (clic) family.
DR iPTMnet; O15247; -.
DR PhosphoSitePlus; O15247; -.
DR BioMuta; CLIC2; -.
DR EPD; O15247; -.
DR jPOST; O15247; -.
DR MassIVE; O15247; -.
DR MaxQB; O15247; -.
DR PaxDb; O15247; -.
DR PeptideAtlas; O15247; -.
DR PRIDE; O15247; -.
DR ProteomicsDB; 48540; -.
DR Antibodypedia; 17894; 159 antibodies from 26 providers.
DR DNASU; 1193; -.
DR Ensembl; ENST00000369449.7; ENSP00000358460.2; ENSG00000155962.13.
DR GeneID; 1193; -.
DR KEGG; hsa:1193; -.
DR MANE-Select; ENST00000369449.7; ENSP00000358460.2; NM_001289.6; NP_001280.3.
DR UCSC; uc004fnf.5; human.
DR CTD; 1193; -.
DR DisGeNET; 1193; -.
DR GeneCards; CLIC2; -.
DR GeneReviews; CLIC2; -.
DR HGNC; HGNC:2063; CLIC2.
DR HPA; ENSG00000155962; Low tissue specificity.
DR MalaCards; CLIC2; -.
DR MIM; 300138; gene.
DR MIM; 300886; phenotype.
DR neXtProt; NX_O15247; -.
DR OpenTargets; ENSG00000155962; -.
DR Orphanet; 324410; X-linked intellectual disability-cardiomegaly-congestive heart failure syndrome.
DR PharmGKB; PA26589; -.
DR VEuPathDB; HostDB:ENSG00000155962; -.
DR eggNOG; KOG1422; Eukaryota.
DR GeneTree; ENSGT00940000161397; -.
DR HOGENOM; CLU_061051_1_0_1; -.
DR InParanoid; O15247; -.
DR OMA; IHTCPED; -.
DR OrthoDB; 974249at2759; -.
DR PhylomeDB; O15247; -.
DR TreeFam; TF315438; -.
DR PathwayCommons; O15247; -.
DR Reactome; R-HSA-2672351; Stimuli-sensing channels.
DR Reactome; R-HSA-5578775; Ion homeostasis.
DR SignaLink; O15247; -.
DR BioGRID-ORCS; 1193; 9 hits in 705 CRISPR screens.
DR ChiTaRS; CLIC2; human.
DR EvolutionaryTrace; O15247; -.
DR GeneWiki; CLIC2; -.
DR GenomeRNAi; 1193; -.
DR Pharos; O15247; Tbio.
DR PRO; PR:O15247; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; O15247; protein.
DR Bgee; ENSG00000155962; Expressed in calcaneal tendon and 154 other tissues.
DR ExpressionAtlas; O15247; baseline and differential.
DR Genevisible; O15247; HS.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; TAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005254; F:chloride channel activity; IBA:GO_Central.
DR GO; GO:0004602; F:glutathione peroxidase activity; IDA:BHF-UCL.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0006821; P:chloride transport; IBA:GO_Central.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR GO; GO:0060315; P:negative regulation of ryanodine-sensitive calcium-release channel activity; IDA:BHF-UCL.
DR GO; GO:0051099; P:positive regulation of binding; IDA:BHF-UCL.
DR GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; IC:BHF-UCL.
DR GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IDA:BHF-UCL.
DR GO; GO:0007165; P:signal transduction; TAS:UniProtKB.
DR InterPro; IPR002946; CLIC.
DR InterPro; IPR030253; CLIC-2.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
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:SF4; PTHR43920:SF4; 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 TIGRFAMs; TIGR00862; O-ClC; 1.
DR PROSITE; PS50405; GST_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloride; Chloride channel; Cytoplasm; Disease variant;
KW Disulfide bond; Intellectual disability; Ion channel; Ion transport;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport; Voltage-gated channel.
FT CHAIN 1..247
FT /note="Chloride intracellular channel protein 2"
FT /id="PRO_0000144205"
FT TRANSMEM 32..52
FT /note="Helical; Note=After insertion into the membrane"
FT /evidence="ECO:0000255"
FT DOMAIN 99..239
FT /note="GST C-terminal"
FT REGION 1..96
FT /note="Required for insertion into the membrane"
FT /evidence="ECO:0000250"
FT REGION 1..94
FT /note="N-terminal"
FT REGION 95..106
FT /note="Joint loop"
FT REGION 107..247
FT /note="C-terminal"
FT REGION 151..171
FT /note="Foot loop"
FT DISULFID 30..33
FT /note="In soluble form"
FT /evidence="ECO:0000269|PubMed:17945253,
FT ECO:0000269|PubMed:18186468"
FT VARIANT 101
FT /note="H -> Q (in MRXS32; results in stimulation of RYR
FT channels activity with channels remaining open for longer
FT times; the mutation may impair insertion of the protein
FT into the membrane to form a functioning ion channel;
FT dbSNP:rs398122917)"
FT /evidence="ECO:0000269|PubMed:22814392"
FT /id="VAR_068898"
FT CONFLICT 109
FT /note="S -> C (in Ref. 1; CAA03948)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="E -> G (in Ref. 1; CAA73228)"
FT /evidence="ECO:0000305"
FT STRAND 14..20
FT /evidence="ECO:0007829|PDB:2R4V"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:2R4V"
FT HELIX 31..43
FT /evidence="ECO:0007829|PDB:2R4V"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:2R4V"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:2R5G"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:2R4V"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:2R4V"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:2R4V"
FT HELIX 83..93
FT /evidence="ECO:0007829|PDB:2R4V"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:2R4V"
FT HELIX 108..111
FT /evidence="ECO:0007829|PDB:2R4V"
FT TURN 112..115
FT /evidence="ECO:0007829|PDB:2R4V"
FT HELIX 116..125
FT /evidence="ECO:0007829|PDB:2R4V"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:2R4V"
FT HELIX 132..151
FT /evidence="ECO:0007829|PDB:2R4V"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:2R4V"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:2R5G"
FT STRAND 172..178
FT /evidence="ECO:0007829|PDB:2R4V"
FT HELIX 181..201
FT /evidence="ECO:0007829|PDB:2R4V"
FT HELIX 210..220
FT /evidence="ECO:0007829|PDB:2R4V"
FT HELIX 223..226
FT /evidence="ECO:0007829|PDB:2R4V"
FT HELIX 232..239
FT /evidence="ECO:0007829|PDB:2R4V"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:2R4V"
SQ SEQUENCE 247 AA; 28356 MW; 9DB896034DD103E8 CRC64;
MSGLRPGTQV DPEIELFVKA GSDGESIGNC PFCQRLFMIL WLKGVKFNVT TVDMTRKPEE
LKDLAPGTNP PFLVYNKELK TDFIKIEEFL EQTLAPPRYP HLSPKYKESF DVGCNLFAKF
SAYIKNTQKE ANKNFEKSLL KEFKRLDDYL NTPLLDEIDP DSAEEPPVSR RLFLDGDQLT
LADCSLLPKL NIIKVAAKKY RDFDIPAEFS GVWRYLHNAY AREEFTHTCP EDKEIENTYA
NVAKQKS
