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P21564 (CICH_TORMA) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Chloride channel protein
Alternative name(s):
ClC-0
OrganismTorpedo marmorata (Marbled electric ray)
Taxonomic identifier7788 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Chondrichthyes › Elasmobranchii › Squalea › Hypnosqualea › Pristiorajea › Batoidea › Torpediniformes › Torpedinoidei › Torpedinidae › Torpedo

Protein attributes

Sequence length805 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Voltage-gated chloride channel. This channel is thought to ensure the high conductance of the non-innervated membrane of the electrocyte necessary for efficient current generation caused by sodium influx through the acetylcholine receptor at the innervated membrane.

Subunit structure

Homodimer. Each subunit contains a channel ("Double barreled channel"). Ref.2

Subcellular location

Membrane; Multi-pass membrane protein.

Miscellaneous

The CLC channel family contains both chloride channels and proton-coupled anion transporters that exchange chloride or another anion for protons. The absence of conserved gating glutamate residues is typical for family members that function as channels By similarity.

Sequence similarities

Belongs to the chloride channel (TC 2.A.49) family. ClC-0 subfamily. [View classification]

Contains 2 CBS domains.

Ontologies

Keywords
   Biological processIon transport
Transport
   Cellular componentMembrane
   DomainCBS domain
Repeat
Transmembrane
Transmembrane helix
   LigandChloride
   Molecular functionChloride channel
Ionic channel
Voltage-gated channel
   PTMGlycoprotein
   Technical term3D-structure
Gene Ontology (GO)
   Cellular componentchloride channel complex

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionvoltage-gated chloride channel activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 805805Chloride channel protein
PRO_0000094464

Regions

Topological domain1 – 4848Cytoplasmic By similarity
Transmembrane49 – 8638Helical; By similarity
Transmembrane93 – 11624Helical; By similarity
Intramembrane125 – 1328Helical; By similarity
Transmembrane141 – 15919Helical; By similarity
Transmembrane166 – 18419Helical; By similarity
Intramembrane201 – 21313Helical; By similarity
Intramembrane217 – 2259Helical; By similarity
Transmembrane237 – 25620Helical; By similarity
Transmembrane283 – 31129Helical; By similarity
Transmembrane320 – 33920Helical; By similarity
Transmembrane388 – 40821Helical; By similarity
Transmembrane416 – 43924Helical; By similarity
Intramembrane456 – 47015Helical; By similarity
Intramembrane471 – 4722Note=Loop between two helices; By similarity
Intramembrane473 – 48412Helical; By similarity
Intramembrane485 – 4895Note=Loop between two helices; By similarity
Transmembrane490 – 50718Helical; By similarity
Topological domain508 – 805298Cytoplasmic By similarity
Domain543 – 60159CBS 1
Domain719 – 77658CBS 2
Motif122 – 1265Selectivity filter part_1 By similarity
Motif164 – 1685Selectivity filter part_2 By similarity
Motif416 – 4205Selectivity filter part_3 By similarity

Sites

Binding site1231Chloride By similarity
Binding site4181Chloride; via amide nitrogen By similarity
Binding site5121Chloride By similarity

Amino acid modifications

Glycosylation3651N-linked (GlcNAc...) Potential

Secondary structure

1 ....................... 805
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P21564 [UniParc].

Last modified May 1, 1991. Version 1.
Checksum: 4CD2FA48AE06FC6D

FASTA80588,888
        10         20         30         40         50         60 
MSHEKNEASG YPEAQSWKSQ EAMLGARTEV SRWRAVKNCL YRHLVKVLGE DWIFLLLLGA 

        70         80         90        100        110        120 
LMALVSWAMD FIGSRGLRFY KYLFALVEGN IGLQYLVWVC YPLALILFSS LFCQIVSPQA 

       130        140        150        160        170        180 
VGSGIPELKT IIRGAVLHEY LTLRTFVAKT VGLTVALSAG FPLGKEGPFV HIASICATLL 

       190        200        210        220        230        240 
NQLLCFISGR REEPYYLRAD ILTVGCALGI SCCFGTPLAG VLFSIEVTCS HFGVRSYWRG 

       250        260        270        280        290        300 
FLGGAFSAFI FRVLSVWVKD TVTLTALFKT NFRGDIPFDL QEMPAFAIIG IASGFFGALF 

       310        320        330        340        350        360 
VYLNRQIIVF MRKKNFVTKI LKKQRLIYPA VVTFVLATLR FPPGVGQFFG AGLMPRETIN 

       370        380        390        400        410        420 
SLFDNYTWTK TIDPRGLGNS AQWFIPHLNI FIVMALYFVM HFWMAALAVT MPVPCGAFVP 

       430        440        450        460        470        480 
VFNLGAVLGR FVGELMALLF PDGLVSNGNL YHILPGEYAV IGAAAMTGAV THAVSTAVIC 

       490        500        510        520        530        540 
FELTGQISHV LPMMVAVILA NMVAQGLQPS LYDSIIQIKK LPYLPELSWS SANKYNIQVG 

       550        560        570        580        590        600 
DIMVRDVTSI ASTSTYGDLL HVLRQTKLKF FPFVDTPDTN TLLGSIDRTE VEGLLQRRIS 

       610        620        630        640        650        660 
AYRRQPAAAA EADEEGRNGE TGASFTGEAE SSFAYIDQED AEGQQREGLE AVKVQTEDPR 

       670        680        690        700        710        720 
PPSPVPAEEP TQTSGIYQKK QKGTGQVASR FEEMLTLEEI YRWEQREKNV VVNFETCRID 

       730        740        750        760        770        780 
QSPFQLVEGT SLQKTHTLFS LLGLDRAYVT SMGKLVGVVA LAEIQAAIEG SYQKGFRLPP 

       790        800 
PLASFRDVKH ARNSGRTATS NSSGK

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References

[1]"Primary structure of Torpedo marmorata chloride channel isolated by expression cloning in Xenopus oocytes."
Jentsch T.J., Steinmeyer K., Schwarz G.
Nature 348:510-514(1990) [PubMed: 2174129] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Electric organ.
[2]"Crystal structure of the cytoplasmic domain of the chloride channel ClC-0."
Meyer S., Dutzler R.
Structure 14:299-307(2006) [PubMed: 16472749] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 525-774, MASS SPECTROMETRY, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X56758 mRNA. Translation: CAA40078.1.
PIRS13410.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2D4ZX-ray3.10A/B525-774[»]
ProteinModelPortalP21564.
SMRP21564. Positions 527-770.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-29086N.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG005332.

Family and domain databases

InterProIPR014743. Cl-channel_core.
IPR001807. Cl-channel_volt-gated.
IPR002242. Cl_channel-0.
IPR000644. Cysta_beta_synth_core.
[Graphical view]
Gene3DG3DSA:1.10.3080.10. Cl-channel_core. 1 hit.
PANTHERPTHR11689. Cl-channel_volt. 1 hit.
PfamPF00571. CBS. 1 hit.
PF00654. Voltage_CLC. 1 hit.
[Graphical view]
PRINTSPR00762. CLCHANNEL.
PR01111. CLCHANNEL0.
SMARTSM00116. CBS. 2 hits.
[Graphical view]
SUPFAMSSF81340. Cl-channel_core. 1 hit.
PROSITEPS51371. CBS. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCICH_TORMA
AccessionPrimary (citable) accession number: P21564
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: September 21, 2011
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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