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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)DescriptionActionsGraphical viewLength
Metal bindingi259CalciumBy similarity1
Metal bindingi261CalciumBy similarity1
Metal bindingi278CalciumBy similarity1
Metal bindingi281CalciumBy similarity1

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
  • 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)DescriptionActionsGraphical viewLength
Transmembranei52 – 72HelicalSequence analysisAdd BLAST21
Transmembranei94 – 114HelicalSequence analysisAdd BLAST21
Transmembranei161 – 181HelicalSequence analysisAdd BLAST21
Transmembranei204 – 224HelicalSequence analysisAdd BLAST21
Transmembranei236 – 256HelicalSequence analysisAdd BLAST21
Transmembranei282 – 302HelicalSequence analysisAdd BLAST21
Transmembranei325 – 345HelicalSequence analysisAdd BLAST21
Transmembranei396 – 416HelicalSequence analysisAdd BLAST21
Transmembranei417 – 437HelicalSequence analysisAdd BLAST21
Transmembranei458 – 478HelicalSequence analysisAdd BLAST21
Transmembranei486 – 506HelicalSequence analysisAdd BLAST21
Topological domaini507 – 687CytoplasmicSequence analysisAdd BLAST181

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)DescriptionActionsGraphical viewLength
ChainiPRO_00000944581 – 687Chloride channel protein ClC-KaAdd BLAST687

Proteomic databases

PaxDbiQ06393.
PRIDEiQ06393.

PTM databases

PhosphoSitePlusiQ06393.

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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini551 – 609CBS 1PROSITE-ProRule annotationAdd BLAST59
Domaini626 – 687CBS 2PROSITE-ProRule annotationAdd BLAST62

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)DescriptionActionsGraphical viewLength
Sequence conflicti266I → V in CAA84064 (PubMed:8041726).Curated1
Sequence conflicti534W → R in CAA84064 (PubMed:8041726).Curated1
Sequence conflicti608 – 609AS → TP in CAA84064 (PubMed:8041726).Curated2

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.
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

PhosphoSitePlusiQ06393.

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...

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: November 2, 2016
This is version 126 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.