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Protein

Chloride channel protein ClC-Ka

Gene

Clcnka

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Voltage-gated chloride channel. Chloride channels have several functions including the regulation of cell volume; membrane potential stabilization, signal transduction and transepithelial transport. May be important in urinary concentrating mechanisms.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi259 – 2591CalciumBy similarity
Metal bindingi261 – 2611CalciumBy similarity
Metal bindingi278 – 2781CalciumBy similarity
Metal bindingi281 – 2811CalciumBy similarity

GO - Molecular functioni

  • chloride channel activity Source: RGD
  • metal ion binding Source: UniProtKB-KW
  • voltage-gated chloride channel activity Source: InterPro
  • voltage-gated ion channel activity Source: RGD

GO - Biological processi

  • body fluid secretion Source: RGD
  • chloride transmembrane transport Source: GOC
  • kidney development Source: RGD
  • response to calcium ion Source: RGD
  • response to pH Source: RGD
  • response to water deprivation Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Chloride channel, Ion channel, Voltage-gated channel

Keywords - Biological processi

Ion transport, Transport

Keywords - Ligandi

Calcium, Chloride, Metal-binding

Protein family/group databases

TCDBi2.A.49.2.4. the chloride carrier/channel (clc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Chloride channel protein ClC-Ka
Short name:
Chloride channel Ka
Alternative name(s):
ClC-K1
Gene namesi
Name:Clcnka
Synonyms:Clcnk1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi68435. Clcnka.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei52 – 7221HelicalSequence analysisAdd
BLAST
Transmembranei94 – 11421HelicalSequence analysisAdd
BLAST
Transmembranei161 – 18121HelicalSequence analysisAdd
BLAST
Transmembranei204 – 22421HelicalSequence analysisAdd
BLAST
Transmembranei236 – 25621HelicalSequence analysisAdd
BLAST
Transmembranei282 – 30221HelicalSequence analysisAdd
BLAST
Transmembranei325 – 34521HelicalSequence analysisAdd
BLAST
Transmembranei396 – 41621HelicalSequence analysisAdd
BLAST
Transmembranei417 – 43721HelicalSequence analysisAdd
BLAST
Transmembranei458 – 47821HelicalSequence analysisAdd
BLAST
Transmembranei486 – 50621HelicalSequence analysisAdd
BLAST
Topological domaini507 – 687181CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • apical plasma membrane Source: RGD
  • basolateral plasma membrane Source: RGD
  • chloride channel complex Source: UniProtKB-KW
  • endoplasmic reticulum Source: RGD
  • integral component of plasma membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 687687Chloride channel protein ClC-KaPRO_0000094458Add
BLAST

Proteomic databases

PaxDbiQ06393.
PRIDEiQ06393.

PTM databases

PhosphoSiteiQ06393.

Expressioni

Tissue specificityi

Expressed predominantly in the kidney. Expressed strongly in the cortical thick ascending limb and the distal convoluted tubule, with minor expression in the S3 segment of the proximal tubule and the cortical collecting tubule.

Inductioni

Regulated in parallel with BSND under furosemide treatment. Decreased to half in the inner medulla under furosemide treatment. In the renal cortex and outer medulla levels were weak and did not change. Regulation with BSND in inner medulla is limited to the thin limb; levels in collecting ducts were not affected by furosemide treatment. During furosemide treatment selective down-regulation with BSND in thin limb plays a role in maintaining salt and water homeostasis.

Interactioni

Subunit structurei

Homodimer. Interacts with BSND. Forms heteromers with BSND in the thin ascending limb of Henle (By similarity).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000013103.

Structurei

3D structure databases

ProteinModelPortaliQ06393.
SMRiQ06393. Positions 542-687.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini551 – 60959CBS 1PROSITE-ProRule annotationAdd
BLAST
Domaini626 – 68762CBS 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 2 CBS domains.PROSITE-ProRule annotation

Keywords - Domaini

CBS domain, Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0476. Eukaryota.
COG0038. LUCA.
HOGENOMiHOG000231297.
HOVERGENiHBG005332.
InParanoidiQ06393.
KOiK05017.
PhylomeDBiQ06393.

Family and domain databases

Gene3Di1.10.3080.10. 2 hits.
InterProiIPR000644. CBS_dom.
IPR014743. Cl-channel_core.
IPR001807. Cl-channel_volt-gated.
IPR002250. Cl_channel-K.
[Graphical view]
PfamiPF00571. CBS. 1 hit.
PF00654. Voltage_CLC. 1 hit.
[Graphical view]
PRINTSiPR00762. CLCHANNEL.
PR01119. CLCHANNELKDY.
SMARTiSM00116. CBS. 2 hits.
[Graphical view]
SUPFAMiSSF81340. SSF81340. 2 hits.
PROSITEiPS51371. CBS. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q06393-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEELVGLREG SSGKPVTLQE LWGPCPRIRR GVRRGLEWLK ERLFRVGEDW
60 70 80 90 100
HFLVALGVLM ALISYAMNFA IGRVVRAHKW LYREVGDGHL LRYLSWTVYP
110 120 130 140 150
VALLSFSSGF SQSISPFSGG SGLPELKTML SGVVLEDYLD IKNFGAKVVG
160 170 180 190 200
LSCTLATGST IFLGKVGPFV HLSVMISAYL GRVRAKTIGE TENKAKEIEM
210 220 230 240 250
LSAAAAVGVA TVFAAPFSGV LFSIEVMSSH FSVWNYWRGF FAATCGAFMF
260 270 280 290 300
RLLGVFNSEQ ETITSIYKTR FRVDVPFDLP EIFFFVALGF ICGVLSCAYL
310 320 330 340 350
FCQRTFLRFI KTNRYTSRLL ATSKPSYAAL VALVLASITY PPGVGRFMAS
360 370 380 390 400
RLSMAEHLHS LFDNNSWALM TRNSSPPWPA EPDPQNLWLE WCHPRFTIFG
410 420 430 440 450
TLAFFLVMKF WMLILATTIP MPAGYFMPIF IIGAAIGRLL GEALSVAFPE
460 470 480 490 500
GIVAGREVNP IMPGGYALAG AAAFSGAVTH TISTALLAFE LTGQIVHALP
510 520 530 540 550
VLMAVLAANA ISQNCQPSFY DGTIMAKKLP YLPWIRGRQI GSYPVTVEHF
560 570 580 590 600
MNCNLTTLAK DTPLEEVVKV VTSTEVSQYP LVETRESQTL VGIVERTHLV
610 620 630 640 650
QALQTQPASW APGQERFLQD ILAGGCPTQP VTLQLSPETS LYQAHSLFER
660 670 680
LTLQSLFVTS RGKAVGSVSW AELKKAISTL INPPAPK
Length:687
Mass (Da):75,569
Last modified:July 15, 1998 - v3
Checksum:i41434F07E3E6E8AD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti266 – 2661I → V in CAA84064 (PubMed:8041726).Curated
Sequence conflicti534 – 5341W → R in CAA84064 (PubMed:8041726).Curated
Sequence conflicti608 – 6092AS → TP in CAA84064 (PubMed:8041726).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13927 mRNA. Translation: BAA03026.1.
Z34291 mRNA. Translation: CAA84064.1.
PIRiA45483.
A57713.
RefSeqiNP_445779.1. NM_053327.1.
UniGeneiRn.88871.

Genome annotation databases

GeneIDi79425.
KEGGirno:79425.
UCSCiRGD:68435. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13927 mRNA. Translation: BAA03026.1.
Z34291 mRNA. Translation: CAA84064.1.
PIRiA45483.
A57713.
RefSeqiNP_445779.1. NM_053327.1.
UniGeneiRn.88871.

3D structure databases

ProteinModelPortaliQ06393.
SMRiQ06393. Positions 542-687.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000013103.

Protein family/group databases

TCDBi2.A.49.2.4. the chloride carrier/channel (clc) family.

PTM databases

PhosphoSiteiQ06393.

Proteomic databases

PaxDbiQ06393.
PRIDEiQ06393.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi79425.
KEGGirno:79425.
UCSCiRGD:68435. rat.

Organism-specific databases

CTDi1187.
RGDi68435. Clcnka.

Phylogenomic databases

eggNOGiKOG0476. Eukaryota.
COG0038. LUCA.
HOGENOMiHOG000231297.
HOVERGENiHBG005332.
InParanoidiQ06393.
KOiK05017.
PhylomeDBiQ06393.

Miscellaneous databases

PROiQ06393.

Family and domain databases

Gene3Di1.10.3080.10. 2 hits.
InterProiIPR000644. CBS_dom.
IPR014743. Cl-channel_core.
IPR001807. Cl-channel_volt-gated.
IPR002250. Cl_channel-K.
[Graphical view]
PfamiPF00571. CBS. 1 hit.
PF00654. Voltage_CLC. 1 hit.
[Graphical view]
PRINTSiPR00762. CLCHANNEL.
PR01119. CLCHANNELKDY.
SMARTiSM00116. CBS. 2 hits.
[Graphical view]
SUPFAMiSSF81340. SSF81340. 2 hits.
PROSITEiPS51371. CBS. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning of a chloride channel that is regulated by dehydration and expressed predominantly in kidney medulla."
    Uchida S., Sasaki S., Furukawa T., Hiraoka M., Imai T., Hirata Y., Marumo F.
    J. Biol. Chem. 268:3821-3824(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Kidney.
  2. "Molecular cloning of a chloride channel that is regulated by dehydration and expressed predominantly in kidney medulla."
    Uchida S., Sasaki S., Furukawa T., Hiraoka M., Imai T., Hirata Y., Marumo F.
    J. Biol. Chem. 269:19192-19192(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
    Strain: Sprague-Dawley.
    Tissue: Kidney.
  3. Uchida S.
    Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
    Strain: Sprague-Dawley.
    Tissue: Kidney.
  4. "Two highly homologous members of the ClC chloride channel family in both rat and human kidney."
    Kieferle S., Fong P., Bens M., Vandewalle A., Jentsch T.
    Proc. Natl. Acad. Sci. U.S.A. 91:6943-6947(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Kidney.
  5. "Barttin increases surface expression and changes current properties of ClC-K channels."
    Waldegger S., Jeck N., Barth P., Peters M., Vitzthum H., Wolf K., Kurtz A., Konrad M., Seyberth H.W.
    Pflugers Arch. 444:411-418(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BSND.
  6. "Parallel down-regulation of chloride channel CLC-K1 and barttin mRNA in the thin ascending limb of the rat nephron by furosemide."
    Wolf K., Meier-Meitinger M., Bergler T., Castrop H., Vitzthum H., Riegger G.A.J., Kurtz A., Kraemer B.K.
    Pflugers Arch. 446:665-671(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOWN-REGULATION BY FUROSEMIDE.

Entry informationi

Entry nameiCLCKA_RAT
AccessioniPrimary (citable) accession number: Q06393
Secondary accession number(s): P97709
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: July 15, 1998
Last modified: June 8, 2016
This is version 123 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.