CICH_TETCF
ID CICH_TETCF Reviewed; 810 AA.
AC P35522;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Chloride channel protein;
DE AltName: Full=ClC-0;
OS Tetronarce californica (Pacific electric ray) (Torpedo californica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Batoidea; Torpediniformes; Torpedinidae; Tetronarce.
OX NCBI_TaxID=7787;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Electric organ;
RX PubMed=1721838; DOI=10.1016/0167-4781(91)90228-e;
RA O'Neill G.P., Grygorczyk R., Adam M., Ford-Hutchinson A.W.;
RT "The nucleotide sequence of a voltage-gated chloride channel from the
RT electric organ of Torpedo californica.";
RL Biochim. Biophys. Acta 1129:131-134(1991).
RN [2]
RP PROTEIN SEQUENCE OF 2-11, AND CHARACTERIZATION.
RC TISSUE=Electric organ;
RX PubMed=7947726; DOI=10.1021/bi00249a005;
RA Middleton R.E., Pheasant D.J., Miller C.;
RT "Purification, reconstitution, and subunit composition of a voltage-gated
RT chloride channel from Torpedo electroplax.";
RL Biochemistry 33:13189-13198(1994).
RN [3]
RP CHARACTERIZATION, AND MUTAGENESIS OF GLU-166.
RX PubMed=12649487; DOI=10.1126/science.1082708;
RA Dutzler R., Campbell E.B., MacKinnon R.;
RT "Gating the selectivity filter in ClC chloride channels.";
RL Science 300:108-112(2003).
CC -!- FUNCTION: Voltage-gated chloride channel. This channel is thought to
CC ensure the high conductance of the non-innervated membrane of the
CC electrocyte necessary for efficient current generation caused by sodium
CC influx through the acetylcholine receptor at the innervated membrane.
CC -!- SUBUNIT: Homodimer. Each subunit has channel activity ('Double barreled
CC channel').
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- MISCELLANEOUS: The CLC channel family contains both chloride channels
CC and proton-coupled anion transporters that exchange chloride or another
CC anion for protons. The absence of conserved gating glutamate residues
CC is typical for family members that function as channels (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family. ClC-0
CC subfamily. {ECO:0000305}.
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DR EMBL; X60433; CAA42960.1; -; mRNA.
DR PIR; S19725; S19725.
DR AlphaFoldDB; P35522; -.
DR SMR; P35522; -.
DR DIP; DIP-29258N; -.
DR TCDB; 2.A.49.2.11; the chloride carrier/channel (clc) family.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005247; F:voltage-gated chloride channel activity; IEA:InterPro.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR Gene3D; 3.10.580.10; -; 2.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR014743; Cl-channel_core.
DR InterPro; IPR001807; Cl-channel_volt-gated.
DR InterPro; IPR002242; Cl_channel-0.
DR Pfam; PF00654; Voltage_CLC; 1.
DR PRINTS; PR00762; CLCHANNEL.
DR PRINTS; PR01111; CLCHANNEL0.
DR SUPFAM; SSF54631; SSF54631; 1.
DR SUPFAM; SSF81340; SSF81340; 1.
DR PROSITE; PS51371; CBS; 2.
PE 1: Evidence at protein level;
KW CBS domain; Chloride; Chloride channel; Direct protein sequencing;
KW Glycoprotein; Ion channel; Ion transport; Membrane; Repeat; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7947726"
FT CHAIN 2..810
FT /note="Chloride channel protein"
FT /id="PRO_0000094463"
FT TOPO_DOM 2..48
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 49..86
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 93..116
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 125..132
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 141..160
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 166..184
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 201..213
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 217..225
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 237..254
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 283..311
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 320..339
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 389..408
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 416..439
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 456..470
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 471..472
FT /note="Note=Loop between two helices"
FT /evidence="ECO:0000250"
FT INTRAMEM 473..484
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 485..489
FT /note="Note=Loop between two helices"
FT /evidence="ECO:0000250"
FT TRANSMEM 490..506
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 507..810
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 543..601
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 724..781
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT REGION 604..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 122..126
FT /note="Selectivity filter part_1"
FT /evidence="ECO:0000250"
FT MOTIF 164..168
FT /note="Selectivity filter part_2"
FT /evidence="ECO:0000250"
FT MOTIF 416..420
FT /note="Selectivity filter part_3"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250"
FT BINDING 418
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250"
FT BINDING 512
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250"
FT SITE 166
FT /note="Gate"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT MUTAGEN 166
FT /note="E->A,Q,V: Gating function is lost. The channel is
FT always open."
FT /evidence="ECO:0000269|PubMed:12649487"
SQ SEQUENCE 810 AA; 89447 MW; BD3954973D6C99EA CRC64;
MSHEKNEASG NPEAQSWKAQ EAMLGVKTEV SRWRAVKNCL YRHLVKVLGE DWIFLLLLGA
LMALVSWAMD FIGSRGLRFY KYLFAMVEGN LGLQYLVWVC YPLILILFSS LFCQIVSPQA
VGSGIPELKT IIRGAVLHEY LTLRTFVAKT VGLTVALSAG FPLGKEGPFV HIASICATLL
NQLLCFISGR REEPYYLRAD ILTVGCALGI SCCFGTPLAG VLFSIEVTCS HFGVRSYWRG
FLGGAFSAFI FRVLSVWVKD TVTLTALFKT NFRGDIPFDL QELPAFAIIG IASGFFGALF
VYLNRQIIVF MRKKNFVTKI LKKQRLIYPA VVTFVLATLR FPPGVGQFFG AGLMPRETIN
SLFDNYTWTK TIDPRGLGNS AQWFIPHLNI FIVMALYFVM HFWMAALAVT MPVPCGAFVP
VFNLGAVLGR FVGELMALLF PDGLVSNGNL YHILPGEYAV IGAAAMTGAV THAVSTAVIC
FELTGQISHV LPMMVAVILA NMVAQGLQPS LYDSIIQIKK LPYLPELSWS SANKYNIQVG
DIMVRDVTSI ASTSTYGDLL HVLRQTKLKF FPFVDTPETN TLLGSIERTE VEGLLQRRIS
AYRRQPATAA EAEEEGRNGE RGASFTGDVP GEAETSFAYI DQEEAEGQQQ REGLEAVKVQ
TEDPRPPSPV PAEEPTQTSG IYQKKHKGTG QVASRFEEML TLEEIYQWEQ REKNVVVNFE
TCRIDQSPFQ LVEGTSLQKT HTLFSLLGLD RAYVTSMGKL VGVVALAEIQ AAIEGSYQKG
FRLPPPLASF RDAKNARNSG RTATSNSSGK
