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Database: UniProt
Entry: I3NES9_ICTTR
LinkDB: I3NES9_ICTTR
Original site: I3NES9_ICTTR 
ID   I3NES9_ICTTR            Unreviewed;       253 AA.
AC   I3NES9;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   RecName: Full=Chloride intracellular channel protein {ECO:0000256|RuleBase:RU362009};
GN   Name=LOC101964462 {ECO:0000313|Ensembl:ENSSTOP00000022876.1};
OS   Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS   tridecemlineatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC   Xerinae; Marmotini; Ictidomys.
OX   NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000022876.1, ECO:0000313|Proteomes:UP000005215};
RN   [1] {ECO:0000313|Proteomes:UP000005215}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Assembly & Analysis Group;
RG   Computational R&D Group;
RG   and Sequencing Platform;
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT   "The Draft Genome of Spermophilus tridecemlineatus.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSTOP00000022876.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000256|ARBA:ARBA00004282}.
CC       Cell membrane {ECO:0000256|ARBA:ARBA00004162}; Single-pass membrane
CC       protein {ECO:0000256|ARBA:ARBA00004162}. Cytoplasm, cytoskeleton,
CC       microtubule organizing center, centrosome
CC       {ECO:0000256|ARBA:ARBA00004300}. Cytoplasmic vesicle membrane
CC       {ECO:0000256|ARBA:ARBA00037855}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00037855}. Membrane
CC       {ECO:0000256|RuleBase:RU362009}; Single-pass membrane protein
CC       {ECO:0000256|RuleBase:RU362009}. Cytoplasm
CC       {ECO:0000256|RuleBase:RU362009}. Mitochondrion
CC       {ECO:0000256|ARBA:ARBA00004173}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123}.
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. {ECO:0000256|RuleBase:RU362009}.
CC   -!- SIMILARITY: Belongs to the chloride channel CLIC family.
CC       {ECO:0000256|ARBA:ARBA00007655, ECO:0000256|RuleBase:RU362009}.
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DR   EMBL; AGTP01031270; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_005324008.1; XM_005323951.2.
DR   AlphaFoldDB; I3NES9; -.
DR   SMR; I3NES9; -.
DR   STRING; 43179.ENSSTOP00000022876; -.
DR   Ensembl; ENSSTOT00000019947.1; ENSSTOP00000022876.1; ENSSTOG00000023266.1.
DR   GeneID; 101964462; -.
DR   eggNOG; KOG1422; Eukaryota.
DR   GeneTree; ENSGT00940000155017; -.
DR   HOGENOM; CLU_061051_1_0_1; -.
DR   InParanoid; I3NES9; -.
DR   OMA; PEANEXV; -.
DR   OrthoDB; 103277at2759; -.
DR   TreeFam; TF315438; -.
DR   Proteomes; UP000005215; Unassembled WGS sequence.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
DR   CDD; cd03061; GST_N_CLIC; 1.
DR   Gene3D; 1.20.1050.10; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR002946; CLIC.
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   NCBIfam; TIGR00862; O-ClC; 1.
DR   PANTHER; PTHR45476:SF5; CHLORIDE INTRACELLULAR CHANNEL PROTEIN; 1.
DR   PANTHER; PTHR45476; CHLORIDE INTRACELLULAR CHANNEL PROTEIN 6-RELATED; 1.
DR   Pfam; PF13410; GST_C_2; 1.
DR   Pfam; PF13409; GST_N_2; 1.
DR   PRINTS; PR01263; INTCLCHANNEL.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG00358; Main_(cytGST); 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
PE   3: Inferred from homology;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Chloride {ECO:0000256|ARBA:ARBA00023214, ECO:0000256|RuleBase:RU362009};
KW   Chloride channel {ECO:0000256|ARBA:ARBA00023173,
KW   ECO:0000256|RuleBase:RU362009}; Cytoplasm {ECO:0000256|RuleBase:RU362009};
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000256|RuleBase:RU362009};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU362009}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362009};
KW   Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882,
KW   ECO:0000256|RuleBase:RU362009}.
FT   DOMAIN          81..244
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   253 AA;  28807 MW;  2BF412F1E1EB86CE CRC64;
     MALSLPLNGL KEEDREPLIE LFVKAGSDGE SIGNCPFSQR LFMILWLKGV VFSVTTVDLK
     RKPADLQNLA PGTHPPFITF NSEVKTDVNK IEEFLEEVLC PPKYLKLSPK HSESNTAGMD
     IFAKFSAYIK NSRPEANEML ERGLLKTLHK LDQYLNSPLP DEIEENNMEN IKFSTRKFLD
     GNEMTLADCN LLPKLHIVKV VAKKYRNFDI PEGMTGIWRY LTNVYGRDEF TNTCPSDKEV
     EIAYSDVAKR LTK
//
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