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Protein

Potassium channel KAT1

Gene

KAT1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Highly selective inward-rectifying potassium channel. This voltage-gated channel could mediate long-term potassium influx into guard cells leading to stomatal opening. Assuming opened or closed conformations in response to the voltage difference across the membrane, the channel is activated by hyperpolarization. The channel activity is enhanced upon external acidification. Also permeable to ammonium ions. Blocked by tetraethylammonium and barium ions.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi377 – 496120cNMPAdd
BLAST

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • inward rectifier potassium channel activity Source: TAIR

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Potassium channel, Voltage-gated channel

Keywords - Biological processi

Ion transport, Potassium transport, Transport

Keywords - Ligandi

Potassium

Enzyme and pathway databases

BioCyciARA:AT5G46240-MONOMER.
MetaCyc:MONOMER-14553.
ReactomeiR-ATH-1296072. Voltage gated Potassium channels.

Protein family/group databases

TCDBi1.A.1.4.7. the voltage-gated ion channel (vic) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Potassium channel KAT1
Gene namesi
Name:KAT1
Ordered Locus Names:At5g46240
ORF Names:MPL12.2
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G46240.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 6363CytoplasmicSequence analysisAdd
BLAST
Transmembranei64 – 8421Helical; Name=Segment S1Sequence analysisAdd
BLAST
Topological domaini85 – 906ExtracellularSequence analysis
Transmembranei91 – 11121Helical; Name=Segment S2Sequence analysisAdd
BLAST
Topological domaini112 – 13423CytoplasmicSequence analysisAdd
BLAST
Transmembranei135 – 15521Helical; Name=Segment S3Sequence analysisAdd
BLAST
Topological domaini156 – 16510ExtracellularSequence analysis
Transmembranei166 – 18621Helical; Voltage-sensor; Name=Segment S4Sequence analysisAdd
BLAST
Topological domaini187 – 20014CytoplasmicSequence analysisAdd
BLAST
Transmembranei201 – 22121Helical; Name=Segment S5Sequence analysisAdd
BLAST
Topological domaini222 – 24827ExtracellularSequence analysisAdd
BLAST
Intramembranei249 – 26820Pore-forming; Name=Segment H5Sequence analysisAdd
BLAST
Topological domaini269 – 2724ExtracellularSequence analysis
Transmembranei273 – 29321Helical; Name=Segment S6Sequence analysisAdd
BLAST
Topological domaini294 – 677384CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi176 – 1761R → S or L: Affects the voltage-dependent gating. 2 Publications
Mutagenesisi177 – 1771R → Q: Affects the voltage-dependent gating. 1 Publication
Mutagenesisi251 – 2511L → I or F: Enhances cesium sensitivity. 1 Publication
Mutagenesisi256 – 2561T → D, G, Q or E: Increases sensitivity to ammonium and sodium. 4 Publications
Mutagenesisi256 – 2561T → E: Increases rubidium uptake and both cesium and calcium sensitivity; facilitated entry of calcium ions; when associated with A-267. 4 Publications
Mutagenesisi256 – 2561T → F, L, P, R or W: Abolishes channel activity. 4 Publications
Mutagenesisi256 – 2561T → S: Increases calcium sensitivity; facilitated entry of calcium ions; when associated with A-267. 4 Publications
Mutagenesisi259 – 2591T → S: Increases rubidium uptake and cesium sensitivity; additional increase of rubidium uptake; when associated with S-260. 1 Publication
Mutagenesisi260 – 2601T → S: Increases rubidium uptake; additional increase of rubidium uptake; when associated with S-259. 1 Publication
Mutagenesisi262 – 2621G → K: Abolishes channel activity. 1 Publication
Mutagenesisi263 – 2631Y → F: The only mutation at this site that do not perturb the channel activity. 1 Publication
Mutagenesisi264 – 2641G → C, F, K, L, P, S or T: Abolishes channel activity. 1 Publication
Mutagenesisi265 – 2651D → N: Affects the pH-dependence. 1 Publication
Mutagenesisi267 – 2671H → A: Increases calcium sensitivity; facilitated entry of calcium ions; when associated with S-256. 2 Publications
Mutagenesisi267 – 2671H → T: Resistance to the cesium inhibition of stomatal opening; when associated with V-269. 2 Publications
Mutagenesisi269 – 2691E → V: Resistance to the cesium inhibition of stomatal opening; when associated with T-267. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 677677Potassium channel KAT1PRO_0000054125Add
BLAST

Proteomic databases

PaxDbiQ39128.
PRIDEiQ39128.

PTM databases

iPTMnetiQ39128.

Expressioni

Tissue specificityi

Expressed in guard cells, and in roots.1 Publication

Gene expression databases

ExpressionAtlasiQ39128. baseline and differential.
GenevisibleiQ39128. AT.

Interactioni

Subunit structurei

The potassium channel is probably composed of a homo- or heterotetrameric complex of pore-forming subunits. May interact with AKT2 and KAT2.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-1552490,EBI-1552490
AKT2Q388984EBI-1552490,EBI-1552774
KAT2Q388493EBI-1552490,EBI-2117720

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi19915. 10 interactions.
IntActiQ39128. 4 interactions.
STRINGi3702.AT5G46240.1.

Structurei

3D structure databases

ProteinModelPortaliQ39128.
SMRiQ39128. Positions 310-475.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini612 – 67766KHAPROSITE-ProRule annotationAdd
BLAST

Domaini

The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids. The pore-forming region H5 is enclosed by the transmembrane segments S5 and S6 in the Shaker-type (1P/6TM) and contains the GYGD signature motif which seems to be involved in potassium selectivity.
The KHA domain (rich in hydrophobic and acidic residues) present in the C-terminal part is likely to be important for tetramerization.

Sequence similaritiesi

Contains 1 cyclic nucleotide-binding domain.PROSITE-ProRule annotation
Contains 1 KHA domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0498. Eukaryota.
ENOG410XPSE. LUCA.
HOGENOMiHOG000238230.
InParanoidiQ39128.
OMAiCVEEYNI.
PhylomeDBiQ39128.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
InterProiIPR018490. cNMP-bd-like.
IPR000595. cNMP-bd_dom.
IPR005821. Ion_trans_dom.
IPR003938. K_chnl_volt-dep_EAG/ELK/ERG.
IPR021789. KHA_dom.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
PfamiPF00027. cNMP_binding. 1 hit.
PF00520. Ion_trans. 1 hit.
PF11834. KHA. 1 hit.
[Graphical view]
PRINTSiPR01463. EAGCHANLFMLY.
SMARTiSM00100. cNMP. 1 hit.
[Graphical view]
SUPFAMiSSF51206. SSF51206. 1 hit.
PROSITEiPS50042. CNMP_BINDING_3. 1 hit.
PS51490. KHA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q39128-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSISWTRNFF ERFCVEEYNI DTIKQSSFLS ADLLPSLGAR INQSTKLRKH
60 70 80 90 100
IISPFNPRYR AWEMWLVLLV IYSAWICPFQ FAFITYKKDA IFIIDNIVNG
110 120 130 140 150
FFAIDIILTF FVAYLDSHSY LLVDSPKKIA IRYLSTWFAF DVCSTAPFQP
160 170 180 190 200
LSLLFNYNGS ELGFRILSML RLWRLRRVSS LFARLEKDIR FNYFWIRCTK
210 220 230 240 250
LISVTLFAIH CAGCFNYLIA DRYPNPRKTW IGAVYPNFKE ASLWNRYVTA
260 270 280 290 300
LYWSITTLTT TGYGDFHAEN PREMLFDIFF MMFNLGLTAY LIGNMTNLVV
310 320 330 340 350
HWTSRTRTFR DSVRAASEFA SRNQLPHDIQ DQMLSHICLK FKTEGLKQQE
360 370 380 390 400
TLNNLPKAIR SSIANYLFFP IVHNIYLFQG VSRNFLFQLV SDIDAEYFPP
410 420 430 440 450
KEDIILQNEA PTDLYILVSG AVDFTVYVDG HDQFQGKAVI GETFGEVGVL
460 470 480 490 500
YYRPQPFTVR TTELSQILRI SRTSLMSAMH AHADDGRVIM NNLFMKLRGQ
510 520 530 540 550
QSIAIDDSNT SGHENRDFKS MGWEEWRDSR KDGYGLDVTN PTSDTALMDA
560 570 580 590 600
IHKEDTEMVK KILKEQKIER AKVERSSSET AGRSYANDSS KKDPYCSSSN
610 620 630 640 650
QIIKPCKREE KRVTIHMMSE SKNGKLILLP SSIEELLRLA SEKFGGCNFT
660 670
KITNADNAEI DDLDVIWDGD HLYFSSN
Length:677
Mass (Da):78,271
Last modified:March 1, 2004 - v2
Checksum:i7F9C8285ED702338
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51W → C in CAA63601 (PubMed:8798465).Curated
Sequence conflicti330 – 3301Q → E in CAA63601 (PubMed:8798465).Curated
Sequence conflicti573 – 5731V → E in CAA63601 (PubMed:8798465).Curated
Sequence conflicti580 – 5801T → S in CAA63601 (PubMed:8798465).Curated
Sequence conflicti629 – 6291L → V in CAA63601 (PubMed:8798465).Curated
Sequence conflicti664 – 6641D → N in CAA63601 (PubMed:8798465).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86990 mRNA. Translation: AAA32824.1.
U25088 Genomic DNA. Translation: AAC49113.1.
X93022 mRNA. Translation: CAA63601.1.
AB010698 Genomic DNA. Translation: BAB11079.1.
CP002688 Genomic DNA. Translation: AED95356.1.
PIRiS32816.
RefSeqiNP_199436.1. NM_123993.2.
UniGeneiAt.305.

Genome annotation databases

EnsemblPlantsiAT5G46240.1; AT5G46240.1; AT5G46240.
GeneIDi834666.
GrameneiAT5G46240.1; AT5G46240.1; AT5G46240.
KEGGiath:AT5G46240.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86990 mRNA. Translation: AAA32824.1.
U25088 Genomic DNA. Translation: AAC49113.1.
X93022 mRNA. Translation: CAA63601.1.
AB010698 Genomic DNA. Translation: BAB11079.1.
CP002688 Genomic DNA. Translation: AED95356.1.
PIRiS32816.
RefSeqiNP_199436.1. NM_123993.2.
UniGeneiAt.305.

3D structure databases

ProteinModelPortaliQ39128.
SMRiQ39128. Positions 310-475.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi19915. 10 interactions.
IntActiQ39128. 4 interactions.
STRINGi3702.AT5G46240.1.

Protein family/group databases

TCDBi1.A.1.4.7. the voltage-gated ion channel (vic) superfamily.

PTM databases

iPTMnetiQ39128.

Proteomic databases

PaxDbiQ39128.
PRIDEiQ39128.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G46240.1; AT5G46240.1; AT5G46240.
GeneIDi834666.
GrameneiAT5G46240.1; AT5G46240.1; AT5G46240.
KEGGiath:AT5G46240.

Organism-specific databases

TAIRiAT5G46240.

Phylogenomic databases

eggNOGiKOG0498. Eukaryota.
ENOG410XPSE. LUCA.
HOGENOMiHOG000238230.
InParanoidiQ39128.
OMAiCVEEYNI.
PhylomeDBiQ39128.

Enzyme and pathway databases

BioCyciARA:AT5G46240-MONOMER.
MetaCyc:MONOMER-14553.
ReactomeiR-ATH-1296072. Voltage gated Potassium channels.

Miscellaneous databases

PROiQ39128.

Gene expression databases

ExpressionAtlasiQ39128. baseline and differential.
GenevisibleiQ39128. AT.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
InterProiIPR018490. cNMP-bd-like.
IPR000595. cNMP-bd_dom.
IPR005821. Ion_trans_dom.
IPR003938. K_chnl_volt-dep_EAG/ELK/ERG.
IPR021789. KHA_dom.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
PfamiPF00027. cNMP_binding. 1 hit.
PF00520. Ion_trans. 1 hit.
PF11834. KHA. 1 hit.
[Graphical view]
PRINTSiPR01463. EAGCHANLFMLY.
SMARTiSM00100. cNMP. 1 hit.
[Graphical view]
SUPFAMiSSF51206. SSF51206. 1 hit.
PROSITEiPS50042. CNMP_BINDING_3. 1 hit.
PS51490. KHA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Functional expression of a probable Arabidopsis thaliana potassium channel in Saccharomyces cerevisiae."
    Anderson J.A., Huprikar S.S., Kochian L.V., Lucas W.J., Gaber R.F.
    Proc. Natl. Acad. Sci. U.S.A. 89:3736-3740(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
    Strain: cv. RLD.
  3. "The baculovirus/insect cell system as an alternative to Xenopus oocytes. First characterization of the AKT1 K+ channel from Arabidopsis thaliana."
    Gaymard F., Cerrutti M., Horeau C., Lemaillet G., Urbach S., Ravallec M., Devauchelle G., Sentenac H., Thibaud J.-B.
    J. Biol. Chem. 271:22863-22870(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Landsberg erecta.
  4. "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence features of the regions of 1,381,565 bp covered by twenty one physically assigned P1 and TAC clones."
    Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N., Tabata S.
    DNA Res. 5:131-145(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  5. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  6. "Expression of an inward-rectifying potassium channel by the Arabidopsis KAT1 cDNA."
    Schachtman D.P., Schroeder J.I., Lucas W.J., Anderson J.A., Gaber R.F.
    Science 258:1654-1658(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Identification of strong modifications in cation selectivity in an Arabidopsis inward rectifying potassium channel by mutant selection in yeast."
    Uozumi N., Gassmann W., Cao Y., Schroeder J.I.
    J. Biol. Chem. 270:24276-24281(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PORE SELECTIVITY, MUTAGENESIS OF THR-256.
  8. "Changes in voltage activation, Cs+ sensitivity, and ion permeability in H5 mutants of the plant K+ channel KAT1."
    Becker D., Dreyer I., Hoth S., Reid J.D., Busch H., Lehnen M., Palme K., Hedrich R.
    Proc. Natl. Acad. Sci. U.S.A. 93:8123-8128(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PORE SELECTIVITY, MUTAGENESIS OF LEU-251; THR-256; THR-259; THR-260 AND 259-THR-THR-260.
  9. "Determination of key structural requirements of a K+ channel pore."
    Nakamura R.L., Anderson J.A., Gaber R.F.
    J. Biol. Chem. 272:1011-1018(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PORE SELECTIVITY, MUTAGENESIS OF TYR-263 AND GLY-264.
  10. "Expression of a Cs(+)-resistant guard cell K+ channel confers Cs(+)-resistant, light-induced stomatal opening in transgenic Arabidopsis."
    Ichida A.M., Pei Z.-M., Baizabal-Aguirre V.M., Turner K.J., Schroeder J.I.
    Plant Cell 9:1843-1857(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PORE SELECTIVITY, MUTAGENESIS OF HIS-267 AND GLU-269.
  11. "Single mutations strongly alter the K(+)-selective pore of the K(in) channel KAT1."
    Dreyer I., Becker D., Bregante M., Gambale F., Lehnen M., Palme K., Hedrich R.
    FEBS Lett. 430:370-376(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PORE SELECTIVITY, MUTAGENESIS OF THR-256 AND HIS-267.
  12. "The N-terminus of the K channel KAT1 controls its voltage-dependent gating by altering the membrane electric field."
    Marten I., Hoshi T.
    Biophys. J. 74:2953-2962(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VOLTAGE-DEPENDENT GATING, MUTAGENESIS OF ARG-176.
  13. "Voltage-dependent gating of single wild-type and S4 mutant KAT1 inward rectifier potassium channels."
    Zei P.C., Aldrich R.W.
    J. Gen. Physiol. 112:679-713(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VOLTAGE-DEPENDENT GATING, MUTAGENESIS OF ARG-176 AND ARG-177.
  14. "Suppression of inward-rectifying K+ channels KAT1 and AKT2 by dominant negative point mutations in the KAT1 alpha-subunit."
    Baizabal-Aguirre V.M., Clemens S., Uozumi N., Schroeder J.I.
    J. Membr. Biol. 167:119-125(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AKT2, MUTAGENESIS OF THR-256 AND GLY-262.
  15. "Distinct molecular bases for pH sensitivity of the guard cell K+ channels KST1 and KAT1."
    Hoth S., Hedrich R.
    J. Biol. Chem. 274:11599-11603(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTON SENSITIVITY, MUTAGENESIS OF ASP-265.
  16. "Guard cell inward K+ channel activity in Arabidopsis involves expression of the twin channel subunits KAT1 and KAT2."
    Pilot G., Lacombe B., Gaymard F., Cherel I., Boucherez J., Thibaud J.-B., Sentenac H.
    J. Biol. Chem. 276:3215-3221(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KAT2.
  17. Cited for: GENE FAMILY, NOMENCLATURE.

Entry informationi

Entry nameiKAT1_ARATH
AccessioniPrimary (citable) accession number: Q39128
Secondary accession number(s): Q42426
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: March 1, 2004
Last modified: May 11, 2016
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. 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.