ID A0A3B3RJC9_9TELE Unreviewed; 445 AA.
AC A0A3B3RJC9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Chloride intracellular channel protein {ECO:0000256|RuleBase:RU362009};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000018732.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000018732.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362009}; Single-
CC pass membrane protein {ECO:0000256|RuleBase:RU362009}. Cytoplasm
CC {ECO:0000256|RuleBase:RU362009}.
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; A0A3B3RJC9; -.
DR STRING; 1676925.ENSPKIP00000018732; -.
DR Ensembl; ENSPKIT00000035562.1; ENSPKIP00000018732.1; ENSPKIG00000004188.1.
DR GeneTree; ENSGT00940000156406; -.
DR OrthoDB; 103277at2759; -.
DR Proteomes; UP000261540; Unplaced.
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; cd10297; GST_C_CLIC5; 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; IPR042069; CLIC5_C_GST.
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; 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 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 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 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 274..445
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT REGION 1..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..164
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 445 AA; 49809 MW; 85E340611C21ACD4 CRC64;
MNDGHQNIYE SIDDGNLYAT PHKNASSETE SHYENQGAIY EEPNVAKEAA HGEIKLHELD
EGDERREDRA SPDYINIRPE SQNGDSDSSD LDERKAFEGN KLSASSEDEG VQESPRLAAK
ANGVKGEPPS LTSSEDGEPV RGDPYDDPSA DMAEEEEEEE EKEVDRIDEG MLMAYSLESS
KISEPEEVVD YSLHTPINSN EEKIADPDQP EVVLFVKAGS DGESIGNCPF SQRIFMILWL
KGVVFNVTTV DLKRKPADLH NLAPGTHPPF LTFNGEVKTD VNKIEEFLEE VLAPPKYPRL
ASKHRESNTA GNDIFAKFSA YIKNTKPEAN PGLEKSLVKA LKRLDDYLNT PLPDEIDADS
MEDEKTSNRK FLDGDELTLA DCNLLPKLHI VKVVAKKYRN YEIPAELTAV WRYLQNAYSR
DEVTNTCAAD REIELAYLDV AKRLK
//
