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Protein

Potassium channel KAT1

Gene

KAT1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Nucleotide bindingi377 – 496cNMPAdd BLAST120

GO - Molecular functioni

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

GO - Biological processi

Keywordsi

Molecular functionIon channel, Potassium channel, Voltage-gated channel
Biological processIon transport, Potassium transport, Transport
LigandPotassium

Enzyme and pathway databases

BioCyciARA:AT5G46240-MONOMER
MetaCyc:MONOMER-14553

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

AraportiAT5G46240
TAIRilocus:2170468 AT5G46240

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 63CytoplasmicSequence analysisAdd BLAST63
Transmembranei64 – 84Helical; Name=Segment S1Sequence analysisAdd BLAST21
Topological domaini85 – 90ExtracellularSequence analysis6
Transmembranei91 – 111Helical; Name=Segment S2Sequence analysisAdd BLAST21
Topological domaini112 – 134CytoplasmicSequence analysisAdd BLAST23
Transmembranei135 – 155Helical; Name=Segment S3Sequence analysisAdd BLAST21
Topological domaini156 – 165ExtracellularSequence analysis10
Transmembranei166 – 186Helical; Voltage-sensor; Name=Segment S4Sequence analysisAdd BLAST21
Topological domaini187 – 200CytoplasmicSequence analysisAdd BLAST14
Transmembranei201 – 221Helical; Name=Segment S5Sequence analysisAdd BLAST21
Topological domaini222 – 248ExtracellularSequence analysisAdd BLAST27
Intramembranei249 – 268Pore-forming; Name=Segment H5Sequence analysisAdd BLAST20
Topological domaini269 – 272ExtracellularSequence analysis4
Transmembranei273 – 293Helical; Name=Segment S6Sequence analysisAdd BLAST21
Topological domaini294 – 677CytoplasmicSequence analysisAdd BLAST384

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi176R → S or L: Affects the voltage-dependent gating. 2 Publications1
Mutagenesisi177R → Q: Affects the voltage-dependent gating. 1 Publication1
Mutagenesisi251L → I or F: Enhances cesium sensitivity. 1 Publication1
Mutagenesisi256T → D, G, Q or E: Increases sensitivity to ammonium and sodium. 4 Publications1
Mutagenesisi256T → E: Increases rubidium uptake and both cesium and calcium sensitivity; facilitated entry of calcium ions; when associated with A-267. 4 Publications1
Mutagenesisi256T → F, L, P, R or W: Abolishes channel activity. 4 Publications1
Mutagenesisi256T → S: Increases calcium sensitivity; facilitated entry of calcium ions; when associated with A-267. 4 Publications1
Mutagenesisi259T → S: Increases rubidium uptake and cesium sensitivity; additional increase of rubidium uptake; when associated with S-260. 1 Publication1
Mutagenesisi260T → S: Increases rubidium uptake; additional increase of rubidium uptake; when associated with S-259. 1 Publication1
Mutagenesisi262G → K: Abolishes channel activity. 1 Publication1
Mutagenesisi263Y → F: The only mutation at this site that do not perturb the channel activity. 1 Publication1
Mutagenesisi264G → C, F, K, L, P, S or T: Abolishes channel activity. 1 Publication1
Mutagenesisi265D → N: Affects the pH-dependence. 1 Publication1
Mutagenesisi267H → A: Increases calcium sensitivity; facilitated entry of calcium ions; when associated with S-256. 2 Publications1
Mutagenesisi267H → T: Resistance to the cesium inhibition of stomatal opening; when associated with V-269. 2 Publications1
Mutagenesisi269E → V: Resistance to the cesium inhibition of stomatal opening; when associated with T-267. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000541251 – 677Potassium channel KAT1Add BLAST677

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 (Probable). Interacts with SLAC1 and SLAH3 (PubMed:27002025).Curated1 Publication

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi19915, 16 interactors
IntActiQ39128, 6 interactors
STRINGi3702.AT5G46240.1

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5NWIX-ray2.35P673-677[»]
5NWJX-ray2.07P671-677[»]
5NWKX-ray3.30P/Q/R/S/T/U/V/W673-677[»]
ProteinModelPortaliQ39128
SMRiQ39128
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini612 – 677KHAPROSITE-ProRule annotationAdd BLAST66

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0498 Eukaryota
ENOG410XPSE LUCA
HOGENOMiHOG000238230
InParanoidiQ39128
KOiK21867
OMAiHLFLLEM
OrthoDBiEOG093606I1
PhylomeDBiQ39128

Family and domain databases

CDDicd00038 CAP_ED, 1 hit
Gene3Di2.60.120.10, 1 hit
InterProiView protein in InterPro
IPR018490 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
PfamiView protein in Pfam
PF00027 cNMP_binding, 1 hit
PF00520 Ion_trans, 1 hit
PF11834 KHA, 1 hit
PRINTSiPR01463 EAGCHANLFMLY
SMARTiView protein in SMART
SM00100 cNMP, 1 hit
SUPFAMiSSF51206 SSF51206, 1 hit
PROSITEiView protein in PROSITE
PS50042 CNMP_BINDING_3, 1 hit
PS51490 KHA, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti5W → C in CAA63601 (PubMed:8798465).Curated1
Sequence conflicti330Q → E in CAA63601 (PubMed:8798465).Curated1
Sequence conflicti573V → E in CAA63601 (PubMed:8798465).Curated1
Sequence conflicti580T → S in CAA63601 (PubMed:8798465).Curated1
Sequence conflicti629L → V in CAA63601 (PubMed:8798465).Curated1
Sequence conflicti664D → N in CAA63601 (PubMed:8798465).Curated1

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_123993.3
UniGeneiAt.305

Genome annotation databases

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

Similar proteinsi

Entry informationi

Entry nameiKAT1_ARATH
AccessioniPrimary (citable) accession number: Q39128
Secondary accession number(s): Q42426
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: March 1, 2004
Last modified: May 23, 2018
This is version 139 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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