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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
 
 
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