ID A0A2U9CPZ0_SCOMX Unreviewed; 298 AA.
AC A0A2U9CPZ0;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Chloride intracellular channel protein {ECO:0000256|RuleBase:RU362009};
GN ORFNames=SMAX5B_003497 {ECO:0000313|EMBL:AWP16752.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP16752.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP16752.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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; CP026259; AWP16752.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9CPZ0; -.
DR STRING; 52904.ENSSMAP00000015966; -.
DR Proteomes; UP000246464; Chromosome 17.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; 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; 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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464};
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 126..289
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 298 AA; 33759 MW; 996970C443D4BFE7 CRC64;
MVKRKSRDFF SRSDDKQKRK HEATSVAPSL KKFLLTLRQQ LGRLMEGKVL RQGDSPLLVS
SYLSVYKGLA GSDGESIGNC PFSQRLFMIL WLKGVVFNVT TVDLKRKPAD LQNLAPGTHP
PFITFNGEVK TDVNKIEEFL EDVLCPPKFI KLGARHPESN TAGMDIFAKF SAFIKNSKPD
ANEALERGLL KTLQKLDEYL RSPLPDEIDH NSTEDVKVSK RKFLDGDEMT LADCNLLPKL
HIVKVVAKKH RGFDIPKEMT AIWKYLNVAY TREEFTNTCP SDKEIEIAYG DVAKRLVK
//