ID A0A091LAB2_9GRUI Unreviewed; 228 AA.
AC A0A091LAB2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Chloride intracellular channel protein {ECO:0000256|RuleBase:RU362009};
DE Flags: Fragment;
GN ORFNames=N324_01333 {ECO:0000313|EMBL:KFP39926.1};
OS Chlamydotis macqueenii (Macqueen's bustard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Otididae; Chlamydotis.
OX NCBI_TaxID=187382 {ECO:0000313|EMBL:KFP39926.1, ECO:0000313|Proteomes:UP000053330};
RN [1] {ECO:0000313|EMBL:KFP39926.1, ECO:0000313|Proteomes:UP000053330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N324 {ECO:0000313|EMBL:KFP39926.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KK744961; KFP39926.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091LAB2; -.
DR SMR; A0A091LAB2; -.
DR Proteomes; UP000053330; 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:SF1; CHLORIDE INTRACELLULAR CHANNEL PROTEIN 6; 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 Reference proteome {ECO:0000313|Proteomes:UP000053330};
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 57..228
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP39926.1"
FT NON_TER 228
FT /evidence="ECO:0000313|EMBL:KFP39926.1"
SQ SEQUENCE 228 AA; 25799 MW; 22F7214912664C86 CRC64;
AGSDGESIGN CPFSQRLFMI LWLKGVIFNV TTVDLKRKPA DLQNLAPGTN PPFMTFDGEV
KTDVNKIEEF LEEKLAPPRY PKLAPNHPES NSAGNDVFAK FSAFIKNPRK DANENLEKSL
LKALRKLDNY LNSPLPDEID AYSTEEITVS SRKFLDGDEL TLADCNLLPK LHIIKVVAKK
YRNFDFPPEM TGISRYLNNA YARDEFTNTC PADQEIEYAY LDVAKRMK
//
