ID A0A3Q3ADD9_KRYMA Unreviewed; 976 AA.
AC A0A3Q3ADD9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Chloride voltage-gated channel 1 {ECO:0000313|Ensembl:ENSKMAP00000009214.1};
GN Name=CLCN1 {ECO:0000313|Ensembl:ENSKMAP00000009214.1};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000009214.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000009214.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR AlphaFoldDB; A0A3Q3ADD9; -.
DR SMR; A0A3Q3ADD9; -.
DR Ensembl; ENSKMAT00000009349.1; ENSKMAP00000009214.1; ENSKMAG00000006908.1.
DR GeneTree; ENSGT00940000157383; -.
DR OMA; QPYYYAD; -.
DR OrthoDB; 1194at2759; -.
DR Proteomes; UP000264800; Unplaced.
DR GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005247; F:voltage-gated chloride channel activity; IEA:InterPro.
DR CDD; cd04591; CBS_pair_voltage-gated_CLC_euk_bac; 1.
DR CDD; cd03683; ClC_1_like; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 2.
DR Gene3D; 1.10.3080.10; Clc chloride channel; 1.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR014743; Cl-channel_core.
DR InterPro; IPR001807; Cl-channel_volt-gated.
DR PANTHER; PTHR45720:SF4; CHLORIDE CHANNEL PROTEIN 1; 1.
DR PANTHER; PTHR45720; CHLORIDE CHANNEL PROTEIN 2; 1.
DR Pfam; PF00654; Voltage_CLC; 1.
DR PRINTS; PR00762; CLCHANNEL.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF81340; Clc chloride channel; 1.
PE 4: Predicted;
KW CBS domain {ECO:0000256|ARBA:ARBA00023122};
KW Ion channel {ECO:0000256|ARBA:ARBA00022882};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448};
KW Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882}.
FT TRANSMEM 109..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 152..173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 226..245
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 257..281
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 339..361
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 382..401
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 442..463
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 475..499
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 68..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 835..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..750
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..901
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..924
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..963
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 976 AA; 107721 MW; 107F1CC25A42F570 CRC64;
MAADASQRKA LRYQQTLLYG EYREQLGNFA RREAARLLTE RQWRRQAGED TRAAGRRGLG
RRHHHQNPAI LESHHSHSSS TKKPHPYSKC QDCLARVRRY IVTKMGEDWI FLILLGLTMA
LVSWSMDYAS AKSLQAYKWI HGELKGNVPL QYLAWVTYPI ILVVFASLFC HLVSPQAIGS
GIPELKTILR GVVLKEYLTL KAFVAKVIGL TAALGSGMPV GKEGPFVHIA SICAAVLSRF
MSIFSGVYEN PYSYTDILTV GCAVGVGCCF GTPLGGVLFS IEVTSTYFAV RNYWRGYFAA
TFSAFIFRVL SVWNKDAVTI TALFKTNFRM DFPFDLQELP AFAIIGISCG FLGAFFVYLN
RQVVLFMRRP TALTRFLTKH RLIYPGAVTL IIATFTFPPG FGQFMAGELM PRECINSLFD
NFTWTKISGS PAPLSLGRSS AWLHPSVSIF VILLLFFIMK FWMSAVSTTM PIPSGAFMPV
FILGAAFGRL VGEIMATLFP NGILFDGIVY RILPGGYAVI GAAAMTGAVT HTVSTAVICF
ELTGQISHIL PMMVAVILAN MVAQGLQPSL YDSIIQVKKL PYLPELALGH ISKYNIFVED
IMVRKVKFVS SQSTFRELNH LLENTTLKTI PLVDSKESMI LLGSIERTEL QAVLDWWLSP
ERRIFEQSSP DQGSKISWES FTFVDEEEEE SPEKTVTPAQ EECNGPIPAP GPQEPSTNHT
GSDKRKLPSV RRTLQRLFSS TSSTGPTETQ EALPPPVADT MSPEEIKAWE EAELDKPVDM
EQIRIDPSPF QLVERTSLHK THTLFSLLGL SHAYVTSIGK LVGVVALKEL QKAIEGSTRS
GVRLRPPLAS FRDASRKTKK HPPPSSAASS PTRDRDLWGE GSRRESELLR RESRDDSRGK
TPSFRGAPGS ETAPSSSSSC ASERGAEGDA QEAVSPSTSS PTSSLPPASP VTHTSPVLTL
SSLQEERESE ESDEPL
//
