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Potassium channel KAT1

 KAT1_ARATH              Reviewed;         677 AA.
Q39128; Q42426;
01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
01-MAR-2004, sequence version 2.
25-OCT-2017, entry version 135.
RecName: Full=Potassium channel KAT1;
Name=KAT1; OrderedLocusNames=At5g46240; ORFNames=MPL12.2;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1570292; DOI=10.1073/pnas.89.9.3736;
Anderson J.A., Huprikar S.S., Kochian L.V., Lucas W.J., Gaber R.F.;
"Functional expression of a probable Arabidopsis thaliana potassium
channel in Saccharomyces cerevisiae.";
Proc. Natl. Acad. Sci. U.S.A. 89:3736-3740(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
STRAIN=cv. RLD;
PubMed=7480337; DOI=10.1104/pp.109.2.371;
Nakamura R.L., McKendree W.L. Jr., Hirsch R.E., Sedbrook J.C.,
Gaber R.F., Sussman M.R.;
"Expression of an Arabidopsis potassium channel gene in guard cells.";
Plant Physiol. 109:371-374(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Landsberg erecta;
PubMed=8798465; DOI=10.1074/jbc.271.37.22863;
Gaymard F., Cerrutti M., Horeau C., Lemaillet G., Urbach S.,
Ravallec M., Devauchelle G., Sentenac H., Thibaud J.-B.;
"The baculovirus/insect cell system as an alternative to Xenopus
oocytes. First characterization of the AKT1 K+ channel from
Arabidopsis thaliana.";
J. Biol. Chem. 271:22863-22870(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9679202; DOI=10.1093/dnares/5.2.131;
Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
Tabata S.;
"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.";
DNA Res. 5:131-145(1998).
[5]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[6]
FUNCTION.
PubMed=8966547; DOI=10.1126/science.8966547;
Schachtman D.P., Schroeder J.I., Lucas W.J., Anderson J.A.,
Gaber R.F.;
"Expression of an inward-rectifying potassium channel by the
Arabidopsis KAT1 cDNA.";
Science 258:1654-1658(1992).
[7]
PORE SELECTIVITY, AND MUTAGENESIS OF THR-256.
PubMed=7592636; DOI=10.1074/jbc.270.41.24276;
Uozumi N., Gassmann W., Cao Y., Schroeder J.I.;
"Identification of strong modifications in cation selectivity in an
Arabidopsis inward rectifying potassium channel by mutant selection in
yeast.";
J. Biol. Chem. 270:24276-24281(1995).
[8]
PORE SELECTIVITY, AND MUTAGENESIS OF LEU-251; THR-256; THR-259;
THR-260 AND 259-THR-THR-260.
PubMed=8755614; DOI=10.1073/pnas.93.15.8123;
Becker D., Dreyer I., Hoth S., Reid J.D., Busch H., Lehnen M.,
Palme K., Hedrich R.;
"Changes in voltage activation, Cs+ sensitivity, and ion permeability
in H5 mutants of the plant K+ channel KAT1.";
Proc. Natl. Acad. Sci. U.S.A. 93:8123-8128(1996).
[9]
PORE SELECTIVITY, AND MUTAGENESIS OF TYR-263 AND GLY-264.
PubMed=8995396; DOI=10.1074/jbc.272.2.1011;
Nakamura R.L., Anderson J.A., Gaber R.F.;
"Determination of key structural requirements of a K+ channel pore.";
J. Biol. Chem. 272:1011-1018(1997).
[10]
PORE SELECTIVITY, AND MUTAGENESIS OF HIS-267 AND GLU-269.
PubMed=9368418; DOI=10.1105/tpc.9.10.1843;
Ichida A.M., Pei Z.-M., Baizabal-Aguirre V.M., Turner K.J.,
Schroeder J.I.;
"Expression of a Cs(+)-resistant guard cell K+ channel confers Cs(+)-
resistant, light-induced stomatal opening in transgenic Arabidopsis.";
Plant Cell 9:1843-1857(1997).
[11]
PORE SELECTIVITY, AND MUTAGENESIS OF THR-256 AND HIS-267.
PubMed=9688573; DOI=10.1016/S0014-5793(98)00694-2;
Dreyer I., Becker D., Bregante M., Gambale F., Lehnen M., Palme K.,
Hedrich R.;
"Single mutations strongly alter the K(+)-selective pore of the K(in)
channel KAT1.";
FEBS Lett. 430:370-376(1998).
[12]
VOLTAGE-DEPENDENT GATING, AND MUTAGENESIS OF ARG-176.
PubMed=9635749; DOI=10.1016/S0006-3495(98)78002-6;
Marten I., Hoshi T.;
"The N-terminus of the K channel KAT1 controls its voltage-dependent
gating by altering the membrane electric field.";
Biophys. J. 74:2953-2962(1998).
[13]
VOLTAGE-DEPENDENT GATING, AND MUTAGENESIS OF ARG-176 AND ARG-177.
PubMed=9834140; DOI=10.1085/jgp.112.6.679;
Zei P.C., Aldrich R.W.;
"Voltage-dependent gating of single wild-type and S4 mutant KAT1
inward rectifier potassium channels.";
J. Gen. Physiol. 112:679-713(1998).
[14]
INTERACTION WITH AKT2, AND MUTAGENESIS OF THR-256 AND GLY-262.
PubMed=9916143; DOI=10.1007/s002329900476;
Baizabal-Aguirre V.M., Clemens S., Uozumi N., Schroeder J.I.;
"Suppression of inward-rectifying K+ channels KAT1 and AKT2 by
dominant negative point mutations in the KAT1 alpha-subunit.";
J. Membr. Biol. 167:119-125(1999).
[15]
PROTON SENSITIVITY, AND MUTAGENESIS OF ASP-265.
PubMed=10206968; DOI=10.1074/jbc.274.17.11599;
Hoth S., Hedrich R.;
"Distinct molecular bases for pH sensitivity of the guard cell K+
channels KST1 and KAT1.";
J. Biol. Chem. 274:11599-11603(1999).
[16]
INTERACTION WITH KAT2.
PubMed=11042178; DOI=10.1074/jbc.M007303200;
Pilot G., Lacombe B., Gaymard F., Cherel I., Boucherez J.,
Thibaud J.-B., Sentenac H.;
"Guard cell inward K+ channel activity in Arabidopsis involves
expression of the twin channel subunits KAT1 and KAT2.";
J. Biol. Chem. 276:3215-3221(2001).
[17]
GENE FAMILY, AND NOMENCLATURE.
PubMed=11500563; DOI=10.1104/pp.126.4.1646;
Maeser P., Thomine S., Schroeder J.I., Ward J.M., Hirschi K., Sze H.,
Talke I.N., Amtmann A., Maathuis F.J.M., Sanders D., Harper J.F.,
Tchieu J., Gribskov M., Persans M.W., Salt D.E., Kim S.A.,
Guerinot M.L.;
"Phylogenetic relationships within cation transporter families of
Arabidopsis.";
Plant Physiol. 126:1646-1667(2001).
[18]
INTERACTION WITH SLAC1 AND SLAH3.
PubMed=27002025; DOI=10.1105/tpc.16.01050;
Zhang A., Ren H.M., Tan Y.Q., Qi G.N., Yao F.Y., Wu G.L., Yang L.W.,
Hussain J., Sun S.J., Wang Y.F.;
"S-type anion channels SLAC1 and SLAH3 function as essential negative
regulators of inward K+ channels and stomatal opening in
Arabidopsis.";
Plant Cell 0:0-0(2016).
-!- FUNCTION: 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. {ECO:0000269|PubMed:8966547}.
-!- SUBUNIT: 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). {ECO:0000269|PubMed:27002025, ECO:0000305}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-1552490, EBI-1552490;
Q38898:AKT2; NbExp=4; IntAct=EBI-1552490, EBI-1552774;
Q38849:KAT2; NbExp=3; IntAct=EBI-1552490, EBI-2117720;
-!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
-!- TISSUE SPECIFICITY: Expressed in guard cells, and in roots.
{ECO:0000269|PubMed:7480337}.
-!- DOMAIN: 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.
-!- DOMAIN: The KHA domain (rich in hydrophobic and acidic residues)
present in the C-terminal part is likely to be important for
tetramerization.
-!- SIMILARITY: Belongs to the potassium channel family. Plant (TC
1.A.1.4) subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M86990; AAA32824.1; -; mRNA.
EMBL; U25088; AAC49113.1; -; Genomic_DNA.
EMBL; X93022; CAA63601.1; -; mRNA.
EMBL; AB010698; BAB11079.1; -; Genomic_DNA.
EMBL; CP002688; AED95356.1; -; Genomic_DNA.
PIR; S32816; S32816.
RefSeq; NP_199436.1; NM_123993.3.
UniGene; At.305; -.
ProteinModelPortal; Q39128; -.
BioGrid; 19915; 16.
IntAct; Q39128; 4.
STRING; 3702.AT5G46240.1; -.
TCDB; 1.A.1.4.7; the voltage-gated ion channel (vic) superfamily.
iPTMnet; Q39128; -.
PaxDb; Q39128; -.
EnsemblPlants; AT5G46240.1; AT5G46240.1; AT5G46240.
GeneID; 834666; -.
Gramene; AT5G46240.1; AT5G46240.1; AT5G46240.
KEGG; ath:AT5G46240; -.
Araport; AT5G46240; -.
TAIR; locus:2170468; AT5G46240.
eggNOG; KOG0498; Eukaryota.
eggNOG; ENOG410XPSE; LUCA.
HOGENOM; HOG000238230; -.
InParanoid; Q39128; -.
KO; K21867; -.
OMA; HLFLLEM; -.
OrthoDB; EOG093606I1; -.
PhylomeDB; Q39128; -.
BioCyc; ARA:AT5G46240-MONOMER; -.
BioCyc; MetaCyc:MONOMER-14553; -.
PRO; PR:Q39128; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q39128; baseline and differential.
Genevisible; Q39128; AT.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005242; F:inward rectifier potassium channel activity; IDA:TAIR.
GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
CDD; cd00038; CAP_ED; 1.
Gene3D; 2.60.120.10; -; 1.
InterPro; IPR018490; cNMP-bd-like.
InterPro; IPR000595; cNMP-bd_dom.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
InterPro; IPR021789; KHA_dom.
InterPro; IPR014710; RmlC-like_jellyroll.
Pfam; PF00027; cNMP_binding; 1.
Pfam; PF00520; Ion_trans; 1.
Pfam; PF11834; KHA; 1.
PRINTS; PR01463; EAGCHANLFMLY.
SMART; SM00100; cNMP; 1.
SUPFAM; SSF51206; SSF51206; 1.
PROSITE; PS50042; CNMP_BINDING_3; 1.
PROSITE; PS51490; KHA; 1.
1: Evidence at protein level;
Complete proteome; Ion channel; Ion transport; Membrane; Potassium;
Potassium channel; Potassium transport; Reference proteome;
Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
CHAIN 1 677 Potassium channel KAT1.
/FTId=PRO_0000054125.
TOPO_DOM 1 63 Cytoplasmic. {ECO:0000255}.
TRANSMEM 64 84 Helical; Name=Segment S1. {ECO:0000255}.
TOPO_DOM 85 90 Extracellular. {ECO:0000255}.
TRANSMEM 91 111 Helical; Name=Segment S2. {ECO:0000255}.
TOPO_DOM 112 134 Cytoplasmic. {ECO:0000255}.
TRANSMEM 135 155 Helical; Name=Segment S3. {ECO:0000255}.
TOPO_DOM 156 165 Extracellular. {ECO:0000255}.
TRANSMEM 166 186 Helical; Voltage-sensor; Name=Segment S4.
{ECO:0000255}.
TOPO_DOM 187 200 Cytoplasmic. {ECO:0000255}.
TRANSMEM 201 221 Helical; Name=Segment S5. {ECO:0000255}.
TOPO_DOM 222 248 Extracellular. {ECO:0000255}.
INTRAMEM 249 268 Pore-forming; Name=Segment H5.
{ECO:0000255}.
TOPO_DOM 269 272 Extracellular. {ECO:0000255}.
TRANSMEM 273 293 Helical; Name=Segment S6. {ECO:0000255}.
TOPO_DOM 294 677 Cytoplasmic. {ECO:0000255}.
DOMAIN 612 677 KHA. {ECO:0000255|PROSITE-
ProRule:PRU00823}.
NP_BIND 377 496 cNMP.
MUTAGEN 176 176 R->S,L: Affects the voltage-dependent
gating. {ECO:0000269|PubMed:9635749,
ECO:0000269|PubMed:9834140}.
MUTAGEN 177 177 R->Q: Affects the voltage-dependent
gating. {ECO:0000269|PubMed:9834140}.
MUTAGEN 251 251 L->I,F: Enhances cesium sensitivity.
{ECO:0000269|PubMed:8755614}.
MUTAGEN 256 256 T->D,G,Q,E: Increases sensitivity to
ammonium and sodium.
{ECO:0000269|PubMed:7592636,
ECO:0000269|PubMed:8755614,
ECO:0000269|PubMed:9688573,
ECO:0000269|PubMed:9916143}.
MUTAGEN 256 256 T->E: Increases rubidium uptake and both
cesium and calcium sensitivity;
facilitated entry of calcium ions; when
associated with A-267.
{ECO:0000269|PubMed:7592636,
ECO:0000269|PubMed:8755614,
ECO:0000269|PubMed:9688573,
ECO:0000269|PubMed:9916143}.
MUTAGEN 256 256 T->F,L,P,R,W: Abolishes channel activity.
{ECO:0000269|PubMed:7592636,
ECO:0000269|PubMed:8755614,
ECO:0000269|PubMed:9688573,
ECO:0000269|PubMed:9916143}.
MUTAGEN 256 256 T->S: Increases calcium sensitivity;
facilitated entry of calcium ions; when
associated with A-267.
{ECO:0000269|PubMed:7592636,
ECO:0000269|PubMed:8755614,
ECO:0000269|PubMed:9688573,
ECO:0000269|PubMed:9916143}.
MUTAGEN 259 259 T->S: Increases rubidium uptake and
cesium sensitivity; additional increase
of rubidium uptake; when associated with
S-260. {ECO:0000269|PubMed:8755614}.
MUTAGEN 260 260 T->S: Increases rubidium uptake;
additional increase of rubidium uptake;
when associated with S-259.
{ECO:0000269|PubMed:8755614}.
MUTAGEN 262 262 G->K: Abolishes channel activity.
{ECO:0000269|PubMed:9916143}.
MUTAGEN 263 263 Y->F: The only mutation at this site that
do not perturb the channel activity.
{ECO:0000269|PubMed:8995396}.
MUTAGEN 264 264 G->C,F,K,L,P,S,T: Abolishes channel
activity. {ECO:0000269|PubMed:8995396}.
MUTAGEN 265 265 D->N: Affects the pH-dependence.
{ECO:0000269|PubMed:10206968}.
MUTAGEN 267 267 H->A: Increases calcium sensitivity;
facilitated entry of calcium ions; when
associated with S-256.
{ECO:0000269|PubMed:9368418,
ECO:0000269|PubMed:9688573}.
MUTAGEN 267 267 H->T: Resistance to the cesium inhibition
of stomatal opening; when associated with
V-269. {ECO:0000269|PubMed:9368418,
ECO:0000269|PubMed:9688573}.
MUTAGEN 269 269 E->V: Resistance to the cesium inhibition
of stomatal opening; when associated with
T-267. {ECO:0000269|PubMed:9368418}.
CONFLICT 5 5 W -> C (in Ref. 3; CAA63601).
{ECO:0000305}.
CONFLICT 330 330 Q -> E (in Ref. 3; CAA63601).
{ECO:0000305}.
CONFLICT 573 573 V -> E (in Ref. 3; CAA63601).
{ECO:0000305}.
CONFLICT 580 580 T -> S (in Ref. 3; CAA63601).
{ECO:0000305}.
CONFLICT 629 629 L -> V (in Ref. 3; CAA63601).
{ECO:0000305}.
CONFLICT 664 664 D -> N (in Ref. 3; CAA63601).
{ECO:0000305}.
SEQUENCE 677 AA; 78271 MW; 7F9C8285ED702338 CRC64;
MSISWTRNFF ERFCVEEYNI DTIKQSSFLS ADLLPSLGAR INQSTKLRKH IISPFNPRYR
AWEMWLVLLV IYSAWICPFQ FAFITYKKDA IFIIDNIVNG FFAIDIILTF FVAYLDSHSY
LLVDSPKKIA IRYLSTWFAF DVCSTAPFQP LSLLFNYNGS ELGFRILSML RLWRLRRVSS
LFARLEKDIR FNYFWIRCTK LISVTLFAIH CAGCFNYLIA DRYPNPRKTW IGAVYPNFKE
ASLWNRYVTA LYWSITTLTT TGYGDFHAEN PREMLFDIFF MMFNLGLTAY LIGNMTNLVV
HWTSRTRTFR DSVRAASEFA SRNQLPHDIQ DQMLSHICLK FKTEGLKQQE TLNNLPKAIR
SSIANYLFFP IVHNIYLFQG VSRNFLFQLV SDIDAEYFPP KEDIILQNEA PTDLYILVSG
AVDFTVYVDG HDQFQGKAVI GETFGEVGVL YYRPQPFTVR TTELSQILRI SRTSLMSAMH
AHADDGRVIM NNLFMKLRGQ QSIAIDDSNT SGHENRDFKS MGWEEWRDSR KDGYGLDVTN
PTSDTALMDA IHKEDTEMVK KILKEQKIER AKVERSSSET AGRSYANDSS KKDPYCSSSN
QIIKPCKREE KRVTIHMMSE SKNGKLILLP SSIEELLRLA SEKFGGCNFT KITNADNAEI
DDLDVIWDGD HLYFSSN


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