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1.A.1.4.7
The voltage-sensitive inward rectifying K+ channel, KAT1 (similar to 1.A.1.4.3; activated by protein 14-3-3 (AAF87262)) (Sottocornola et al., 2006). May also transport Na+ and Cs+ (Nakamura and Gaber, 2009). Forms heterotetrameric channels with KAT2 with a stoichiometry of 2:2 (Lebaudy et al., 2010). The pH-sensor is built of a sensory cloud rather than of single key amino acids (Gonzalez et al., 2011). The transmembrane core region of KAT1 is important for its activity in S. cerevisiae, and this involves not only the pore region but also parts of its voltage-sensor domain (Saito et al. 2017).

Accession Number:Q39128
Protein Name:Potassium channel KAT1
Length:677
Molecular Weight:78271.00
Species:Arabidopsis thaliana (Mouse-ear cress) [3702]
Number of TMSs:6
Location1 / Topology2 / Orientation3: Membrane1 / Multi-pass membrane protein2
Substrate K+

Cross database links:

Genevestigator: Q39128
eggNOG: KOG0498
HEGENOM: HBG318539
RefSeq: NP_199436.1   
Entrez Gene ID: 834666   
Pfam: PF00027    PF11834    PF00520   
BioCyc: MetaCyc:MONOMER-14553   
KEGG: ath:AT5G46240   

Gene Ontology

GO:0016021 C:integral to membrane
GO:0005886 C:plasma membrane
GO:0042802 F:identical protein binding
GO:0005249 F:voltage-gated potassium channel activity
GO:0006813 P:potassium ion transport
GO:0055085 P:transmembrane transport

References (16)

[1] “Functional expression of a probable Arabidopsis thaliana potassium channel in Saccharomyces cerevisiae.”  Anderson J.A.et.al.   1570292
[2] “Expression of an Arabidopsis potassium channel gene in guard cells.”  Nakamura R.L.et.al.   7480337
[3] “The baculovirus/insect cell system as an alternative to Xenopus oocytes. First characterization of the AKT1 K+ channel from Arabidopsis thaliana.”  Gaymard F.et.al.   8798465
[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.et.al.   9679202
[5] “Expression of an inward-rectifying potassium channel by the Arabidopsis KAT1 cDNA.”  Schachtman D.P.et.al.   8966547
[6] “Identification of strong modifications in cation selectivity in an Arabidopsis inward rectifying potassium channel by mutant selection in yeast.”  Uozumi N.et.al.   7592636
[7] “Changes in voltage activation, Cs+ sensitivity, and ion permeability in H5 mutants of the plant K+ channel KAT1.”  Becker D.et.al.   8755614
[8] “Determination of key structural requirements of a K+ channel pore.”  Nakamura R.L.et.al.   8995396
[9] “Expression of a Cs(+)-resistant guard cell K+ channel confers Cs(+)-resistant, light-induced stomatal opening in transgenic Arabidopsis.”  Ichida A.M.et.al.   9368418
[10] “Single mutations strongly alter the K(+)-selective pore of the K(in) channel KAT1.”  Dreyer I.et.al.   9688573
[11] “The N-terminus of the K channel KAT1 controls its voltage-dependent gating by altering the membrane electric field.”  Marten I.et.al.   9635749
[12] “Voltage-dependent gating of single wild-type and S4 mutant KAT1 inward rectifier potassium channels.”  Zei P.C.et.al.   9834140
[13] “Suppression of inward-rectifying K+ channels KAT1 and AKT2 by dominant negative point mutations in the KAT1 alpha-subunit.”  Baizabal-Aguirre V.M.et.al.   9916143
[14] “Distinct molecular bases for pH sensitivity of the guard cell K+ channels KST1 and KAT1.”  Hoth S.et.al.   10206968
[15] “Guard cell inward K+ channel activity in Arabidopsis involves expression of the twin channel subunits KAT1 and KAT2.”  Pilot G.et.al.   11042178
[16] “Phylogenetic relationships within cation transporter families of Arabidopsis.”  Maeser P.et.al.   11500563

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MSISWTRNFF ERFCVEEYNI DTIKQSSFLS ADLLPSLGAR INQSTKLRKH IISPFNPRYR 
61:	AWEMWLVLLV IYSAWICPFQ FAFITYKKDA IFIIDNIVNG FFAIDIILTF FVAYLDSHSY 
121:	LLVDSPKKIA IRYLSTWFAF DVCSTAPFQP LSLLFNYNGS ELGFRILSML RLWRLRRVSS 
181:	LFARLEKDIR FNYFWIRCTK LISVTLFAIH CAGCFNYLIA DRYPNPRKTW IGAVYPNFKE 
241:	ASLWNRYVTA LYWSITTLTT TGYGDFHAEN PREMLFDIFF MMFNLGLTAY LIGNMTNLVV 
301:	HWTSRTRTFR DSVRAASEFA SRNQLPHDIQ DQMLSHICLK FKTEGLKQQE TLNNLPKAIR 
361:	SSIANYLFFP IVHNIYLFQG VSRNFLFQLV SDIDAEYFPP KEDIILQNEA PTDLYILVSG 
421:	AVDFTVYVDG HDQFQGKAVI GETFGEVGVL YYRPQPFTVR TTELSQILRI SRTSLMSAMH 
481:	AHADDGRVIM NNLFMKLRGQ QSIAIDDSNT SGHENRDFKS MGWEEWRDSR KDGYGLDVTN 
541:	PTSDTALMDA IHKEDTEMVK KILKEQKIER AKVERSSSET AGRSYANDSS KKDPYCSSSN 
601:	QIIKPCKREE KRVTIHMMSE SKNGKLILLP SSIEELLRLA SEKFGGCNFT KITNADNAEI 
661:	DDLDVIWDGD HLYFSSN