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Protein

Potassium channel AKT2/3

Gene

AKT2

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

Functioni

Highly selective and weak inward-rectifying potassium channel. Plays a role in both loading and unloading potassium into/from the phloem sap. Seems to control sugar loading into phloem via a voltage-dependent process. Blocked by physiological concentrations of external calcium and by external acidification. May interact with the cytoskeleton or with regulatory proteins. Dephosphorylation by PP2CA not only leads to the inhibition of potassium currents but also to an increase of the voltage-dependence of the channel. Regulated by the CBL4/CIPK6 calcium sensor/protein kinase complex via a kinase interaction-dependent but phosphorylation-independent translocation of the channel to the plasma membrane.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi394 – 513120cNMPAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • regulation of membrane potential Source: TAIR
  • response to abscisic acid Source: TAIR
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

ReactomeiR-ATH-1296072. Voltage gated Potassium channels.

Protein family/group databases

TCDBi1.A.1.4.6. the voltage-gated ion channel (vic) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Potassium channel AKT2/3
Gene namesi
Name:AKT2
Synonyms:AKT3
Ordered Locus Names:At4g22200
ORF Names:T10I14.30
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G22200.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 7979CytoplasmicSequence analysisAdd
BLAST
Transmembranei80 – 10021Helical; Name=Segment S1Sequence analysisAdd
BLAST
Topological domaini101 – 1099ExtracellularSequence analysis
Transmembranei110 – 13021Helical; Name=Segment S2Sequence analysisAdd
BLAST
Topological domaini131 – 15323CytoplasmicSequence analysisAdd
BLAST
Transmembranei154 – 17421Helical; Name=Segment S3Sequence analysisAdd
BLAST
Topological domaini175 – 1839ExtracellularSequence analysis
Transmembranei184 – 20421Helical; Voltage-sensor; Name=Segment S4Sequence analysisAdd
BLAST
Topological domaini205 – 21814CytoplasmicSequence analysisAdd
BLAST
Transmembranei219 – 23921Helical; Name=Segment S5Sequence analysisAdd
BLAST
Topological domaini240 – 26526ExtracellularSequence analysisAdd
BLAST
Intramembranei266 – 28520Pore-forming; Name=Segment H5Sequence analysisAdd
BLAST
Topological domaini286 – 2883ExtracellularSequence analysis
Transmembranei289 – 30921Helical; Name=Segment S6Sequence analysisAdd
BLAST
Topological domaini310 – 802493CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • integral component of plasma membrane Source: GO_Central
  • plasmodesma Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Disruption phenotypei

Delayed development and flowering.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi243 – 2431H → D: Abolishes the proton sensitivity; lack of susceptibility to extracellular potassium; when associated with E-286. 1 Publication
Mutagenesisi286 – 2861S → E: Abolishes the proton and the potassium sensitivity; lack of susceptibility to extracellular potassium; when associated with D-243. 1 Publication
Mutagenesisi289 – 2891I → R: No change in proton sensitivity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 802802Potassium channel AKT2/3PRO_0000054122Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi179 – 1791N-linked (GlcNAc...)Sequence analysis
Glycosylationi254 – 2541N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Dephosphorylated by PP2CA.

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ38898.
PRIDEiQ38898.

Expressioni

Tissue specificityi

Expressed mainly in the phloem tissues throughout the plant but also, at a lower level, in leaf epiderm, mesophyll and guard cells.4 Publications

Inductioni

In shoots, strongly induced by abscisic acid (ABA) treatment and reduced after NaCl treatment or potassium starvation.1 Publication

Gene expression databases

GenevisibleiQ38898. AT.

Interactioni

Subunit structurei

The potassium channel is probably composed of a homo- or heterotetrameric complex of pore-forming subunits. Interacts with the phosphatase PPC2A and the kinase CIPK6. May interact with AKT1, KAT1 and KAT3.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-1552774,EBI-1552774
AKT1Q389983EBI-1552774,EBI-974289
KAT1Q391284EBI-1552774,EBI-1552490
KAT2Q388493EBI-1552774,EBI-2117720
PP2CAP495985EBI-1552774,EBI-1764934

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi13600. 13 interactions.
IntActiQ38898. 5 interactions.
MINTiMINT-8066047.
STRINGi3702.AT4G22200.1.

Structurei

3D structure databases

ProteinModelPortaliQ38898.
SMRiQ38898. Positions 327-487, 516-727.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati540 – 56930ANK 1Add
BLAST
Repeati573 – 60230ANK 2Add
BLAST
Repeati606 – 63631ANK 3Add
BLAST
Repeati637 – 66630ANK 4Add
BLAST
Repeati670 – 69930ANK 5Add
BLAST
Domaini725 – 80278KHAPROSITE-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 5 ANK repeats.PROSITE-ProRule annotation
Contains 1 cyclic nucleotide-binding domain.PROSITE-ProRule annotation
Contains 1 KHA domain.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0498. Eukaryota.
ENOG410XPSE. LUCA.
HOGENOMiHOG000238230.
InParanoidiQ38898.
OMAiYLSTWFL.
PhylomeDBiQ38898.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
2.60.120.10. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
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.
[Graphical view]
PfamiPF12796. Ank_2. 1 hit.
PF00027. cNMP_binding. 1 hit.
PF00520. Ion_trans. 1 hit.
PF11834. KHA. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
PR01463. EAGCHANLFMLY.
SMARTiSM00248. ANK. 5 hits.
SM00100. cNMP. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF51206. SSF51206. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
PS50042. CNMP_BINDING_3. 1 hit.
PS51490. KHA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q38898-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDLKYSASHC NLSSDMKLRR FHQHRGKGRE EEYDASSLSL NNLSKLILPP
60 70 80 90 100
LGVASYNQNH IRSSGWIISP MDSRYRCWEF YMVLLVAYSA WVYPFEVAFL
110 120 130 140 150
NSSPKRNLCI ADNIVDLFFA VDIVLTFFVA YIDERTQLLV REPKQIAVRY
160 170 180 190 200
LSTWFLMDVA STIPFDAIGY LITGTSTLNI TCNLLGLLRF WRLRRVKHLF
210 220 230 240 250
TRLEKDIRYS YFWIRCFRLL SVTLFLVHCA GCSYYLIADR YPHQGKTWTD
260 270 280 290 300
AIPNFTETSL SIRYIAAIYW SITTMTTVGY GDLHASNTIE MVFITVYMLF
310 320 330 340 350
NLGLTAYLIG NMTNLVVEGT RRTMEFRNSI EAASNFVNRN RLPPRLKDQI
360 370 380 390 400
LAYMCLRFKA ESLNQQHLID QLPKSIYKSI CQHLFLPSVE KVYLFKGVSR
410 420 430 440 450
EILLLLVSKM KAEYIPPRED VIMQNEAPDD VYIIVSGEVE IIDSEMERES
460 470 480 490 500
VLGTLRCGDI FGEVGALCCR PQSYTFQTKS LSQLLRLKTS FLIETMQIKQ
510 520 530 540 550
QDNATMLKNF LQHHKKLSNL DIGDLKAQQN GENTDVVPPN IASNLIAVVT
560 570 580 590 600
TGNAALLDEL LKAKLSPDIT DSKGKTPLHV AASRGYEDCV LVLLKHGCNI
610 620 630 640 650
HIRDVNGNSA LWEAIISKHY EIFRILYHFA AISDPHIAGD LLCEAAKQNN
660 670 680 690 700
VEVMKALLKQ GLNVDTEDHH GVTALQVAMA EDQMDMVNLL ATNGADVVCV
710 720 730 740 750
NTHNEFTPLE KLRVVEEEEE EERGRVSIYR GHPLERRERS CNEAGKLILL
760 770 780 790 800
PPSLDDLKKI AGEKFGFDGS ETMVTNEDGA EIDSIEVIRD NDKLYFVVNK

II
Length:802
Mass (Da):91,308
Last modified:November 1, 1996 - v1
Checksum:i6F138F9149ED3CD7
GO

Sequence cautioni

The sequence AAA96153.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAA96154.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAA16770.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAB79175.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U40154 mRNA. Translation: AAA97865.1.
U44744 Genomic DNA. Translation: AAA96153.1. Different initiation.
U44745 mRNA. Translation: AAA96154.1. Different initiation.
AL021712 Genomic DNA. Translation: CAA16770.1. Different initiation.
AL161556 Genomic DNA. Translation: CAB79175.1. Different initiation.
CP002687 Genomic DNA. Translation: AEE84571.1.
AK229735 mRNA. Translation: BAF01572.1.
PIRiS68699.
RefSeqiNP_567651.1. NM_118342.2.
UniGeneiAt.1970.

Genome annotation databases

EnsemblPlantsiAT4G22200.1; AT4G22200.1; AT4G22200.
GeneIDi828311.
GrameneiAT4G22200.1; AT4G22200.1; AT4G22200.
KEGGiath:AT4G22200.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U40154 mRNA. Translation: AAA97865.1.
U44744 Genomic DNA. Translation: AAA96153.1. Different initiation.
U44745 mRNA. Translation: AAA96154.1. Different initiation.
AL021712 Genomic DNA. Translation: CAA16770.1. Different initiation.
AL161556 Genomic DNA. Translation: CAB79175.1. Different initiation.
CP002687 Genomic DNA. Translation: AEE84571.1.
AK229735 mRNA. Translation: BAF01572.1.
PIRiS68699.
RefSeqiNP_567651.1. NM_118342.2.
UniGeneiAt.1970.

3D structure databases

ProteinModelPortaliQ38898.
SMRiQ38898. Positions 327-487, 516-727.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi13600. 13 interactions.
IntActiQ38898. 5 interactions.
MINTiMINT-8066047.
STRINGi3702.AT4G22200.1.

Protein family/group databases

TCDBi1.A.1.4.6. the voltage-gated ion channel (vic) superfamily.

Proteomic databases

PaxDbiQ38898.
PRIDEiQ38898.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G22200.1; AT4G22200.1; AT4G22200.
GeneIDi828311.
GrameneiAT4G22200.1; AT4G22200.1; AT4G22200.
KEGGiath:AT4G22200.

Organism-specific databases

TAIRiAT4G22200.

Phylogenomic databases

eggNOGiKOG0498. Eukaryota.
ENOG410XPSE. LUCA.
HOGENOMiHOG000238230.
InParanoidiQ38898.
OMAiYLSTWFL.
PhylomeDBiQ38898.

Enzyme and pathway databases

ReactomeiR-ATH-1296072. Voltage gated Potassium channels.

Miscellaneous databases

PROiQ38898.

Gene expression databases

GenevisibleiQ38898. AT.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
2.60.120.10. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
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.
[Graphical view]
PfamiPF12796. Ank_2. 1 hit.
PF00027. cNMP_binding. 1 hit.
PF00520. Ion_trans. 1 hit.
PF11834. KHA. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
PR01463. EAGCHANLFMLY.
SMARTiSM00248. ANK. 5 hits.
SM00100. cNMP. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF51206. SSF51206. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
PS50042. CNMP_BINDING_3. 1 hit.
PS51490. KHA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Multiple genes, tissue specificity, and expression-dependent modulation contribute to the functional diversity of potassium channels in Arabidopsis thaliana."
    Cao Y., Ward J.M., Kelly W.B., Ichida A.M., Gaber R.F., Anderson J.A., Uozumi N., Schroeder J.I., Crawford N.M.
    Plant Physiol. 109:1093-1106(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: cv. Columbia.
  2. "Isolation of an ion channel gene from Arabidopsis thaliana using the H5 signature sequence from voltage-dependent K+ channels."
    Ketchum K.A., Slayman C.W.
    FEBS Lett. 378:19-26(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  3. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. Cited for: CHARACTERIZATION, TISSUE SPECIFICITY.
  7. "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 KAT1.
  8. "A shaker-like K(+) channel with weak rectification is expressed in both source and sink phloem tissues of Arabidopsis."
    Lacombe B., Pilot G., Michard E., Gaymard F., Sentenac H., Thibaud J.-B.
    Plant Cell 12:837-851(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, TISSUE SPECIFICITY.
  9. "The AKT3 potassium channel protein interacts with the AtPP2CA protein phosphatase 2C."
    Vranova E., Taehtiharju S., Sriprang R., Willekens H., Heino P., Palva E.T., Inze D., Van Camp W.
    J. Exp. Bot. 52:181-182(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PP2CA.
  10. Cited for: GENE FAMILY, NOMENCLATURE.
  11. "Loss of the AKT2/3 potassium channel affects sugar loading into the phloem of Arabidopsis."
    Deeken R., Geiger D., Fromm J., Koroleva O., Ache P., Langenfeld-Heyser R., Sauer N., May S.T., Hedrich R.
    Planta 216:334-344(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Physical and functional interaction of the Arabidopsis K(+) channel AKT2 and phosphatase AtPP2CA."
    Cherel I., Michard E., Platet N., Mouline K., Alcon C., Sentenac H., Thibaud J.-B.
    Plant Cell 14:1133-1146(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PP2CA, DEPHOSPHORYLATION BY PP2CA, TISSUE SPECIFICITY.
  13. "Outer pore residues control the H(+) and K(+) sensitivity of the Arabidopsis potassium channel AKT3."
    Geiger D., Becker D., Lacombe B., Hedrich R.
    Plant Cell 14:1859-1868(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF HIS-243; SER-286 AND ILE-289.
  14. "Regulated expression of Arabidopsis shaker K(+) channel genes involved in K(+) uptake and distribution in the plant."
    Pilot G., Gaymard F., Mouline K., Cherel I., Sentenac H.
    Plant Mol. Biol. 51:773-787(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH AKT1 AND KAT3, INDUCTION.
  15. "Calcium-dependent modulation and plasma membrane targeting of the AKT2 potassium channel by the CBL4/CIPK6 calcium sensor/protein kinase complex."
    Held K., Pascaud F., Eckert C., Gajdanowicz P., Hashimoto K., Corratge-Faillie C., Offenborn J.N., Lacombe B., Dreyer I., Thibaud J.B., Kudla J.
    Cell Res. 21:1116-1130(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CIPK6, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiAKT2_ARATH
AccessioniPrimary (citable) accession number: Q38898
Secondary accession number(s): Q0WMS8, Q42408, Q9M0L6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 137 of the entry and version 1 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.