ID A0A3B4Y6W1_SERLL Unreviewed; 952 AA.
AC A0A3B4Y6W1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Chloride intracellular channel protein 4-like {ECO:0000313|Ensembl:ENSSLDP00000018998.1};
OS Seriola lalandi dorsalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000018998.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000018998.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the chloride channel CLIC family.
CC {ECO:0000256|ARBA:ARBA00007655}.
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DR AlphaFoldDB; A0A3B4Y6W1; -.
DR STRING; 1841481.ENSSLDP00000018998; -.
DR Ensembl; ENSSLDT00000019640.1; ENSSLDP00000018998.1; ENSSLDG00000014919.1.
DR GeneTree; ENSGT00940000159602; -.
DR Proteomes; UP000261360; 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; 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; 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; 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.
PE 3: Inferred from homology;
KW Chloride {ECO:0000256|ARBA:ARBA00023214};
KW Chloride channel {ECO:0000256|ARBA:ARBA00023173};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Transport {ECO:0000256|ARBA:ARBA00022882};
KW Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882}.
FT DOMAIN 735..797
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13409"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..54
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..507
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..547
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..602
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 952 AA; 107658 MW; FF605D2963F8DB29 CRC64;
MAQSGSCQNP DLSNAVIAHS REGTGSDLDT QRGREDEEGA EEDEDVELAE EVGEDVLLTS
EAGNAQAKRE CREQGEREEL RIIQVALLAN GVIREGEGKV EKPEENSEGG VEMVDEEQEK
IVEETREEED MIKVEKSQDQ ILDKQEALTA SSKREEKINE GDNELEEHQI VSTTDYTETL
QESSILVEES GKPSLSSPDD TTKTEVVPLI NSEVTETTED PTTDETTGIE QVNIQNDLCQ
TIGTIEMVGN QTNQLTNDNQ DEMKNTDEMK ESESSKQDVE PTNNNITWKQ KESVVANIEE
EGAKELMKDA MSDIDIEGEA KVEQPELAFV PSEELSQTEG GVKETMLGGI NQKDLEEEQV
DEVKSLDEGQ TTMRELMGEE EHRERESIIK FENQAVVGPP EPEVDQVEEA FELEEVGEVE
LDQPGGEVTS EENGSSTQGG GDLQEHPSQL FVEAGADWGD KLREQPTRMA LVEDRREEGV
EEEEMVGEVE MAEEPVTVLD DEIEEVEMVE IGKEKDENEK DEKGEEEKDN NNDNREVELD
TNGRVKGLKK AMENGILSPE PQPLRKEGWG TARMLSPRRK DTDWIKNDQP EEDRAPEMKD
WRKELKPLKK NIWETERGRK EGVRTETLPE KKSPPMKEDW IKELKSVIKD ESLPKKKDEQ
VKRKRVVLLE DGHSYIPQRE EMTEGKREEV KLISHRRVES PLPPVHRNSR TPQDQDYEIS
LYVKAGSDGE SIGNCPFSQR LFMILWLKGV IFNVTTVDLK RKPADLQDLA PGTNPPFVTF
NGEVKVDVNM IEEFLEAKLT PPSYPRLAPK HREANTAGID VFAKFSAYIK NPRKDTNDAL
EKALLKSLYR LDDFLRTPLS DEIDAYASGD LPESSRSFLD GSDLTLADCN LLPKLHILKV
VAKKYRGFEI PVEMAGVWRY LNCAYQREEF TSTCPAEREI EFAYLDVAKR IK
//
