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Database: UniProt
Entry: A0A2K5N8B4_CERAT
LinkDB: A0A2K5N8B4_CERAT
Original site: A0A2K5N8B4_CERAT 
ID   A0A2K5N8B4_CERAT        Unreviewed;       230 AA.
AC   A0A2K5N8B4;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Chloride intracellular channel protein {ECO:0000256|RuleBase:RU362009};
GN   Name=CLIC1 {ECO:0000313|Ensembl:ENSCATP00000033742.1};
OS   Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Cercocebus.
OX   NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000033742.1, ECO:0000313|Proteomes:UP000233060};
RN   [1] {ECO:0000313|Ensembl:ENSCATP00000033742.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004162};
CC       Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}.
CC       Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}. Membrane
CC       {ECO:0000256|RuleBase:RU362009}; Single-pass membrane protein
CC       {ECO:0000256|RuleBase:RU362009}. Cytoplasm
CC       {ECO:0000256|RuleBase:RU362009}. Nucleus membrane
CC       {ECO:0000256|ARBA:ARBA00004590}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004590}.
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   AlphaFoldDB; A0A2K5N8B4; -.
DR   Ensembl; ENSCATT00000058016.1; ENSCATP00000033742.1; ENSCATG00000039844.1.
DR   GeneTree; ENSGT00940000154708; -.
DR   Proteomes; UP000233060; Unplaced.
DR   Bgee; ENSCATG00000039844; Expressed in spleen and 12 other cell types or tissues.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
DR   CDD; cd10300; GST_C_CLIC1; 1.
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; IPR030259; CLIC-1_C.
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:SF2; 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 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   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
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   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233060};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Transport {ECO:0000256|RuleBase:RU362009};
KW   Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882,
KW   ECO:0000256|RuleBase:RU362009}.
FT   DOMAIN          82..222
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   230 AA;  25681 MW;  09D430B1EF348DC0 CRC64;
     LFAGSDGAKI GNCPFSQRLF MVLWLKGVTF NVTTVDTKRR TETVQKLCPG GQLPFLLYGT
     EVHTDTNKIE EFLEAVLCPP RYPKLAALNP ESNTAGLDIF AKFSAYIKNS NPALNDNLEK
     GLLKALKVLD NYLTSPLPEE VDETSAEDEG VSQRKFLDGN ELTLADCNLL PKLHIVQVVC
     KKYRGFTIPE VFRGVHRYLS NAYAREEFAS TCPDDEEIEL AYEQVAKALK
//
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