CICH_TORMA
ID CICH_TORMA Reviewed; 805 AA.
AC P21564;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Chloride channel protein;
DE AltName: Full=ClC-0;
OS Torpedo marmorata (Marbled electric ray).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Batoidea; Torpediniformes; Torpedinidae; Torpedo.
OX NCBI_TaxID=7788;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Electric organ;
RX PubMed=2174129; DOI=10.1038/348510a0;
RA Jentsch T.J., Steinmeyer K., Schwarz G.;
RT "Primary structure of Torpedo marmorata chloride channel isolated by
RT expression cloning in Xenopus oocytes.";
RL Nature 348:510-514(1990).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 525-774, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBUNIT.
RX PubMed=16472749; DOI=10.1016/j.str.2005.10.008;
RA Meyer S., Dutzler R.;
RT "Crystal structure of the cytoplasmic domain of the chloride channel ClC-
RT 0.";
RL Structure 14:299-307(2006).
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 contains a channel ('Double barreled
CC channel'). {ECO:0000269|PubMed:16472749}.
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; X56758; CAA40078.1; -; mRNA.
DR PIR; S13410; S13410.
DR PDB; 2D4Z; X-ray; 3.10 A; A/B=525-774.
DR PDBsum; 2D4Z; -.
DR AlphaFoldDB; P21564; -.
DR SMR; P21564; -.
DR DIP; DIP-29086N; -.
DR EvolutionaryTrace; P21564; -.
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 3D-structure; CBS domain; Chloride; Chloride channel; Glycoprotein;
KW Ion channel; Ion transport; Membrane; Repeat; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..805
FT /note="Chloride channel protein"
FT /id="PRO_0000094464"
FT TOPO_DOM 1..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..159
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..256
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 388..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..507
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 508..805
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 543..601
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 719..776
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT REGION 606..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..684
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 COMPBIAS 669..684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT STRAND 541..546
FT /evidence="ECO:0007829|PDB:2D4Z"
FT HELIX 556..565
FT /evidence="ECO:0007829|PDB:2D4Z"
FT STRAND 569..575
FT /evidence="ECO:0007829|PDB:2D4Z"
FT TURN 577..579
FT /evidence="ECO:0007829|PDB:2D4Z"
FT STRAND 581..587
FT /evidence="ECO:0007829|PDB:2D4Z"
FT HELIX 588..600
FT /evidence="ECO:0007829|PDB:2D4Z"
FT STRAND 603..605
FT /evidence="ECO:0007829|PDB:2D4Z"
FT HELIX 697..707
FT /evidence="ECO:0007829|PDB:2D4Z"
FT HELIX 732..742
FT /evidence="ECO:0007829|PDB:2D4Z"
FT STRAND 745..751
FT /evidence="ECO:0007829|PDB:2D4Z"
FT STRAND 754..760
FT /evidence="ECO:0007829|PDB:2D4Z"
FT HELIX 761..769
FT /evidence="ECO:0007829|PDB:2D4Z"
SQ SEQUENCE 805 AA; 88888 MW; 4CD2FA48AE06FC6D CRC64;
MSHEKNEASG YPEAQSWKSQ EAMLGARTEV SRWRAVKNCL YRHLVKVLGE DWIFLLLLGA
LMALVSWAMD FIGSRGLRFY KYLFALVEGN IGLQYLVWVC YPLALILFSS LFCQIVSPQA
VGSGIPELKT IIRGAVLHEY LTLRTFVAKT VGLTVALSAG FPLGKEGPFV HIASICATLL
NQLLCFISGR REEPYYLRAD ILTVGCALGI SCCFGTPLAG VLFSIEVTCS HFGVRSYWRG
FLGGAFSAFI FRVLSVWVKD TVTLTALFKT NFRGDIPFDL QEMPAFAIIG 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 FPFVDTPDTN TLLGSIDRTE VEGLLQRRIS
AYRRQPAAAA EADEEGRNGE TGASFTGEAE SSFAYIDQED AEGQQREGLE AVKVQTEDPR
PPSPVPAEEP TQTSGIYQKK QKGTGQVASR FEEMLTLEEI YRWEQREKNV VVNFETCRID
QSPFQLVEGT SLQKTHTLFS LLGLDRAYVT SMGKLVGVVA LAEIQAAIEG SYQKGFRLPP
PLASFRDVKH ARNSGRTATS NSSGK
