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Protein

Potassium channel subfamily T member 1

Gene

Kcnt1

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

Functioni

Outwardly rectifying potassium channel subunit that may coassemble with other Slo-type channel subunits. Activated by high intracellular sodium or chloride levels. Activated upon stimulation of G-protein coupled receptors, such as CHRM1 and GRIA1. May be regulated by calcium in the absence of sodium ions (in vitro).3 Publications

GO - Molecular functioni

  • calcium-activated potassium channel activity Source: InterPro
  • potassium channel activity Source: RGD

GO - Biological processi

  • potassium ion transport Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Potassium channel

Keywords - Biological processi

Ion transport, Potassium transport, Transport

Keywords - Ligandi

Potassium

Protein family/group databases

TCDBi1.A.1.3.4. the voltage-gated ion channel (vic) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Potassium channel subfamily T member 1
Alternative name(s):
Sequence like a calcium-activated potassium channel subunit
Gene namesi
Name:Kcnt1
Synonyms:Slack
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621106. Kcnt1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 9797CytoplasmicSequence analysisAdd
BLAST
Transmembranei98 – 11821Helical; Name=Segment S1Sequence analysisAdd
BLAST
Topological domaini119 – 15537ExtracellularSequence analysisAdd
BLAST
Transmembranei156 – 17621Helical; Name=Segment S2Sequence analysisAdd
BLAST
Topological domaini177 – 18711CytoplasmicSequence analysisAdd
BLAST
Transmembranei188 – 20821Helical; Name=Segment S3Sequence analysisAdd
BLAST
Topological domaini209 – 2135ExtracellularSequence analysis
Transmembranei214 – 22613Helical; Name=Segment S4Sequence analysisAdd
BLAST
Topological domaini227 – 25125CytoplasmicSequence analysisAdd
BLAST
Transmembranei252 – 27221Helical; Name=Segment S5Sequence analysisAdd
BLAST
Topological domaini273 – 2819ExtracellularSequence analysis
Intramembranei282 – 30221Pore-formingSequence analysisAdd
BLAST
Topological domaini303 – 3042ExtracellularSequence analysis
Transmembranei305 – 32521Helical; Name=Segment S6Sequence analysisAdd
BLAST
Topological domaini326 – 1237912CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: RGD
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi409 – 4091R → Q: Generates currents that resembles wild-type in terms of voltage dependence and kinetic behavior but has 2- to 3-fold higher amplitude compared to wild-type. The mutation shows to cause constitutive activation of the channel, mimicking the effects of phosphorylation of the C-terminal domain by PRKCA activation. 1 Publication
Mutagenesisi913 – 9131A → T: Generates currents that resembles wild-type in terms of voltage dependence and kinetic behavior but has 2- to 3-fold higher amplitude compared to wild-type. The mutation shows to cause constitutive activation of the channel, mimicking the effects of phosphorylation of the C-terminal domain by PRKCA activation. 1 Publication

Chemistry

GuidetoPHARMACOLOGYi385.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12371237Potassium channel subfamily T member 1PRO_0000054092Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi133 – 1331N-linked (GlcNAc...)Sequence analysis
Glycosylationi137 – 1371N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Phosphorylated by protein kinase C. Phosphorylation of the C-terminal domain increases channel activity.1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ9Z258.

Expressioni

Tissue specificityi

Detected in brain and brainstem, in vestibular and oculomotor nuclei, the medial nucleus of the trapezoid in the auditory system, in olfactory bulb, red nucleus, and deep cerebellar nuclei. Detected in thalamus, substantia nigra, and amygdala (at protein level). Highly expressed in the brain and kidney.3 Publications

Interactioni

Subunit structurei

Interacts with CRBN via its cytoplasmic C-terminus.1 Publication

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000023542.

Structurei

3D structure databases

ProteinModelPortaliQ9Z258.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini475 – 596122RCK N-terminalAdd
BLAST

Sequence similaritiesi

Contains 1 RCK N-terminal domain.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3193. Eukaryota.
ENOG410XSMA. LUCA.
HOGENOMiHOG000231460.
HOVERGENiHBG055190.
InParanoidiQ9Z258.
KOiK04946.
PhylomeDBiQ9Z258.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR003929. K_chnl_Ca-activ_BK_asu.
IPR013099. K_chnl_dom.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF03493. BK_channel_a. 1 hit.
PF07885. Ion_trans_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Z258-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MARAKLPRSP SEGKAGPGDT PAGSAAPEEP HGLSPLLPTR GGGSVGSDVG
60 70 80 90 100
QRLHVEDFSL DSSLSQVQVE FYVNENTFKE RLKLFFIKNQ RSSLRIRLFN
110 120 130 140 150
FSLKLLTCLL YIVRVLLDNP DQGIGCWGCT KYNYTFNGSS SEFHWAPILW
160 170 180 190 200
VERKMALWVI QVIVATISFL ETMLLIYLSY KGNIWEQIFH VSFVLEMINT
210 220 230 240 250
LPFIITVFWP PLRNLFIPVF LNCWLAKHAL ENMINDFHRA ILRTQSAMFN
260 270 280 290 300
QVLILFCTLL CLVFTGTCGI QHLERAGGNL NLLTSFYFCI VTFSTVGFGD
310 320 330 340 350
VTPKIWPSQL LVVILICVTL VVLPLQFEEL VYLWMERQKS GGNYSRHRAR
360 370 380 390 400
TEKHVVLCVS SLKIDLLMDF LNEFYAHPRL QDYYVVILCP SEMDVQVRRV
410 420 430 440 450
LQIPLWSQRV IYLQGSALKD QDLMRAKMDN GEACFILSSR NEVDRTAADH
460 470 480 490 500
QTILRAWAVK DFAPNCPLYV QILKPENKFH VKFADHVVCE EECKYAMLAL
510 520 530 540 550
NCICPATSTL ITLLVHTSRG QEGQESPEQW QRMYGRCSGN EVYHIRMGDS
560 570 580 590 600
KFFREYEGKS FTYAAFHAHK KYGVCLIGLK REENKSILLN PGPRHILAAS
610 620 630 640 650
DTCFYINITK EENSAFIFKQ EEKQNRRGLA GQALYEGPSR LPVHSIIASM
660 670 680 690 700
VAMDLQNTDC RPSQGGSGGG GGKLTLPTEN GSGSRRPSIA PVLELADSSA
710 720 730 740 750
LLPCDLLSDQ SEDEVTPSDD EGLSVVEYVK GYPPNSPYIG SSPTLCHLLP
760 770 780 790 800
VKAPFCCLRL DKGCKHNSYE DAKAYGFKNK LIIVSAETAG NGLYNFIVPL
810 820 830 840 850
RAYYRSRREL NPIVLLLDNK PDHHFLEAIC CFPMVYYMEG SVDNLDSLLQ
860 870 880 890 900
CGIIYADNLV VVDKESTMSA EEDYMADAKT IVNVQTMFRL FPSLSITTEL
910 920 930 940 950
THPSNMRFMQ FRAKDSYSLA LSKLEKQERE NGSNLAFMFR LPFAAGRVFS
960 970 980 990 1000
ISMLDTLLYQ SFVKDYMITI TRLLLGLDTT PGSGYLCAMK VTEDDLWIRT
1010 1020 1030 1040 1050
YGRLFQKLCS SSAEIPIGIY RTECHVFSSE PHDLRAQSQI SVNMEDCEDT
1060 1070 1080 1090 1100
REAKGPWGTR AASGGGSTHG RHGGSADPVE HPLLRRKSLQ WARKLSRKSS
1110 1120 1130 1140 1150
KQAGKAPMTT DWITQQRLSL YRRSERQELS ELVKNRMKHL GLPTTGYEDV
1160 1170 1180 1190 1200
ANLTASDVMN RVNLGYLQDE MNDHHQNTLS YVLINPPPDT RLEPNDIVYL
1210 1220 1230
IRSDPLAHVT SSSQSRKSSC SNKLSSCNPE TRDETQL
Length:1,237
Mass (Da):139,615
Last modified:May 1, 1999 - v1
Checksum:iE11B4A7A77EB612B
GO
Isoform 2 (identifier: Q9Z258-2) [UniParc]FASTAAdd to basket

Also known as: SLACK-A

The sequence of this isoform differs from the canonical sequence as follows:
     1-66: MARAKLPRSP...DFSLDSSLSQ → MNDLDTEVLPLPPRYRFRDLLLGDQTFPNDDR

Show »
Length:1,203
Mass (Da):136,827
Checksum:i4C97FBDE3966BA72
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6666MARAK…SSLSQ → MNDLDTEVLPLPPRYRFRDL LLGDQTFPNDDR in isoform 2. 1 PublicationVSP_015472Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF089730 mRNA. Translation: AAC83350.1.
AY884213 mRNA. Translation: AAX16016.1.
PIRiT46609.
RefSeqiNP_068625.1. NM_021853.1. [Q9Z258-1]
UniGeneiRn.162642.

Genome annotation databases

GeneIDi60444.
KEGGirno:60444.
UCSCiRGD:621106. rat. [Q9Z258-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF089730 mRNA. Translation: AAC83350.1.
AY884213 mRNA. Translation: AAX16016.1.
PIRiT46609.
RefSeqiNP_068625.1. NM_021853.1. [Q9Z258-1]
UniGeneiRn.162642.

3D structure databases

ProteinModelPortaliQ9Z258.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000023542.

Chemistry

GuidetoPHARMACOLOGYi385.

Protein family/group databases

TCDBi1.A.1.3.4. the voltage-gated ion channel (vic) superfamily.

Proteomic databases

PaxDbiQ9Z258.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi60444.
KEGGirno:60444.
UCSCiRGD:621106. rat. [Q9Z258-1]

Organism-specific databases

CTDi57582.
RGDi621106. Kcnt1.

Phylogenomic databases

eggNOGiKOG3193. Eukaryota.
ENOG410XSMA. LUCA.
HOGENOMiHOG000231460.
HOVERGENiHBG055190.
InParanoidiQ9Z258.
KOiK04946.
PhylomeDBiQ9Z258.

Miscellaneous databases

NextBioi612180.
PROiQ9Z258.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR003929. K_chnl_Ca-activ_BK_asu.
IPR013099. K_chnl_dom.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF03493. BK_channel_a. 1 hit.
PF07885. Ion_trans_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Formation of intermediate-conductance calcium-activated potassium channels by interaction of Slack and Slo subunits."
    Joiner W.J., Tang M.D., Wang L.-Y., Dworetzky S.I., Boissard C.G., Gan L., Gribkoff V.K., Kaczmarek L.K.
    Nat. Neurosci. 1:462-469(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
    Tissue: Brain.
  2. "An alternative isoform of the sodium-activated potassium channel Slack exhibits fast gating kinetics."
    Bhattacharjee A., von Hehn C.A., Kaczmarek L.K.
    Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Strain: Sprague-Dawley.
  3. "Localization of the Slack potassium channel in the rat central nervous system."
    Bhattacharjee A., Gan L., Kaczmarek L.K.
    J. Comp. Neurol. 454:241-254(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  4. "The sodium-activated potassium channel is encoded by a member of the Slo gene family."
    Yuan A., Santi C.M., Wei A., Wang Z.W., Pollak K., Nonet M., Kaczmarek L., Crowder C.M., Salkoff L.
    Neuron 37:765-773(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Identification and functional characterization of cereblon as a binding protein for large-conductance calcium-activated potassium channel in rat brain."
    Jo S., Lee K.-H., Song S., Jung Y.-K., Park C.-S.
    J. Neurochem. 94:1212-1224(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TOPOLOGY, INTERACTION WITH CRBN.
  6. "Opposite regulation of Slick and Slack K+ channels by neuromodulators."
    Santi C.M., Ferreira G., Yang B., Gazula V.R., Butler A., Wei A., Kaczmarek L.K., Salkoff L.
    J. Neurosci. 26:5059-5068(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION, TISSUE SPECIFICITY.
  7. Cited for: MUTAGENESIS OF ARG-409 AND ALA-913.

Entry informationi

Entry nameiKCNT1_RAT
AccessioniPrimary (citable) accession number: Q9Z258
Secondary accession number(s): Q5D6C6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: May 1, 1999
Last modified: May 11, 2016
This is version 110 of the entry and version 1 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.