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Q38998 (AKT1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Potassium channel AKT1
Gene names
Name:AKT1
Ordered Locus Names:At2g26650
ORF Names:F18A8.2
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length857 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Highly selective inward-rectifying potassium channel that mediate potassium uptake by plant roots in response to low K+ conditions, by a calcium-, CBL-, and CIPK-dependent pathway. Positively regulated by phosphorylation by CIPK23. Negatively regulated by a kinase-independent regulatory mechanism involving a competing direct binding of CBL10. Involved in the stomatal regulation by monitoring the turgor pressure in guard cells. Assuming opened or closed conformations in response to the voltage difference across the membrane, the channel is activated by hyperpolarization. May interact with the cytoskeleton or with regulatory proteins. Ref.10 Ref.12 Ref.13 Ref.14 Ref.15

Subunit structure

The potassium channel is probably composed of a homo- or heterotetrameric complex of pore-forming subunits. Possible heteromultimer with AKT2 or KAT3. Part of a K+-channel calcium-sensing kinase/phosphatase complex composed by a calcium sensor CBL (CBL1, CBL2, CBL3 or CBL9), a kinase CIPK (CIPK6, CIPK16 or CIPK23), a phosphatase PP2C (AIP1) and a K+-channel (AKT1). Interacts directly with AIP1, CBL10, CIPK6, CIPK16 and CIPK23. Ref.9 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16

Subcellular location

Cell membrane; Multi-pass membrane protein Ref.13.

Tissue specificity

Preferentially expressed in the peripheral cell layers of root mature including root cortex and root hairs. Detected also, at a lower level, in the mesophyll of the leaves and at restricted sites corresponding to hydathodes and guard cells. Ref.3 Ref.8

Induction

In roots, strongly reduced after 2,4-dichlorophenoxyacetic acid (2,4-D) treatment and weakly reduced after benzyladenine (BA) treatment. In shoots, strongly reduced after abscisic acid (ABA) treatment and induced after benzyladenine (BA) treatment. Ref.12

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.

The KHA domain (rich in hydrophobic and acidic residues) present in the C-terminal part is likely to be important for tetramerization.

Post-translational modification

Phosphorylated by CIPK proteins CIPK6, CIPK16 and CIPK23. The activation by phosphorylation is induced by low K+ conditions and stimulates K+ uptake and relocation. Dephosphorylation by AIP1 repressed the transport activity. Ref.13 Ref.14 Ref.15

Sequence similarities

Belongs to the potassium channel family. Plant (TC 1.A.1.4) subfamily. [View classification]

Contains 6 ANK repeats.

Contains 1 cyclic nucleotide-binding domain.

Contains 1 KHA domain.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 857857Potassium channel AKT1
PRO_0000054121

Regions

Topological domain1 – 6161Cytoplasmic Potential
Transmembrane62 – 8221Helical; Name=Segment S1; Potential
Topological domain83 – 908Extracellular Potential
Transmembrane91 – 11121Helical; Name=Segment S2; Potential
Topological domain112 – 13423Cytoplasmic Potential
Transmembrane135 – 15521Helical; Name=Segment S3; Potential
Topological domain156 – 1583Extracellular Potential
Transmembrane159 – 17921Helical; Voltage-sensor; Name=Segment S4; Potential
Topological domain180 – 19314Cytoplasmic Potential
Transmembrane194 – 21421Helical; Name=Segment S5; Potential
Topological domain215 – 24127Extracellular Potential
Intramembrane242 – 26120Pore-forming; Name=Segment H5; Potential
Topological domain262 – 2654Extracellular Potential
Transmembrane266 – 28621Helical; Name=Segment S6; Potential
Topological domain287 – 857571Cytoplasmic Potential
Repeat515 – 54632ANK 1
Repeat550 – 57930ANK 2
Repeat583 – 61230ANK 3
Repeat614 – 64330ANK 4
Repeat647 – 67630ANK 5
Repeat680 – 70930ANK 6
Domain790 – 85768KHA
Nucleotide binding372 – 493122cNMP

Sequences

Sequence LengthMass (Da)Tools
Q38998 [UniParc].

Last modified January 1, 1998. Version 2.
Checksum: 28E1622BA3505F4C

FASTA85796,990
        10         20         30         40         50         60 
MRGGALLCGQ VQDEIEQLSR ESSHFSLSTG ILPSLGARSN RRVKLRRFVV SPYDHKYRIW 

        70         80         90        100        110        120 
EAFLVVLVVY TAWVSPFEFG FLRKPRPPLS ITDNIVNAFF AIDIIMTFFV GYLDKSTYLI 

       130        140        150        160        170        180 
VDDRKQIAFK YLRSWFLLDL VSTIPSEAAM RISSQSYGLF NMLRLWRLRR VGALFARLEK 

       190        200        210        220        230        240 
DRNFNYFWVR CAKLVCVTLF AVHCAACFYY LIAARNSNPA KTWIGANVAN FLEESLWMRY 

       250        260        270        280        290        300 
VTSMYWSITT LTTVGYGDLH PVNTKEMIFD IFYMLFNLGL TAYLIGNMTN LVVHGTSRTR 

       310        320        330        340        350        360 
NFRDTIQAAS NFAHRNHLPP RLQDQMLAHL CLKYRTDSEG LQQQETLDAL PKAIRSSISH 

       370        380        390        400        410        420 
FLFYSLMDKV YLFRGVSNDL LFQLVSEMKA EYFPPKEDVI LQNEAPTDFY ILVNGTADLV 

       430        440        450        460        470        480 
DVDTGTESIV REVKAGDIIG EIGVLCYRPQ LFTVRTKRLC QLLRMNRTTF LNIIQANVGD 

       490        500        510        520        530        540 
GTIIMNNLLQ HLKEMNDPVM TNVLLEIENM LARGKMDLPL NLCFAAIRED DLLLHQLLKR 

       550        560        570        580        590        600 
GLDPNESDNN GRTPLHIAAS KGTLNCVLLL LEYHADPNCR DAEGSVPLWE AMVEGHEKVV 

       610        620        630        640        650        660 
KVLLEHGSTI DAGDVGHFAC TAAEQGNLKL LKEIVLHGGD VTRPRATGTS ALHTAVCEEN 

       670        680        690        700        710        720 
IEMVKYLLEQ GADVNKQDMH GWTPRDLAEQ QGHEDIKALF REKLHERRVH IETSSSVPIL 

       730        740        750        760        770        780 
KTGIRFLGRF TSEPNIRPAS REVSFRIRET RARRKTNNFD NSLFGILANQ SVPKNGLATV 

       790        800        810        820        830        840 
DEGRTGNPVR VTISCAEKDD IAGKLVLLPG SFKELLELGS NKFGIVATKV MNKDNNAEID 

       850 
DVDVIRDGDH LIFATDS 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and expression in yeast of a plant potassium ion transport system."
Sentenac H., Bonneaud N., Minet M., Lacroute F., Salmon J.-M., Gaymard F., Grignon C.
Science 256:663-665(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Landsberg erecta.
[2]Sentenac H.
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Organization and expression of the gene coding for the potassium transport system AKT1 of Arabidopsis thaliana."
Basset M., Conejero G., Lepetit M., Fourcroy P., Sentenac H.
Plant Mol. Biol. 29:947-958(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
Strain: cv. Landsberg erecta.
[4]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [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]"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. expand/collapse author list , 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] OF 79-857.
Strain: cv. Columbia.
[7]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 106-857.
Strain: cv. Columbia.
[8]"Tissue-specific expression of Arabidopsis AKT1 gene is consistent with a role in K+ nutrition."
Lagarde D., Basset M., Lepetit M., Conejero G., Gaymard F., Astruc S., Grignon C.
Plant J. 9:195-203(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[9]"Tetramerization of the AKT1 plant potassium channel involves its C-terminal cytoplasmic domain."
Daram P., Urbach S., Gaymard F., Sentenac H., Cherel I.
EMBO J. 16:3455-3463(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[10]"A role for the AKT1 potassium channel in plant nutrition."
Hirsch R.E., Lewis B.D., Spalding E.P., Sussman M.R.
Science 280:918-921(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Phylogenetic relationships within cation transporter families of Arabidopsis."
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.
Plant Physiol. 126:1646-1667(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.
[12]"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 AKT2 AND KAT3, INDUCTION.
[13]"A protein kinase, interacting with two calcineurin B-like proteins, regulates K+ transporter AKT1 in Arabidopsis."
Xu J., Li H.-D., Chen L.-Q., Wang Y., Liu L.-L., He L., Wu W.-H.
Cell 125:1347-1360(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CIPK23, PHOSPHORYLATION, SUBCELLULAR LOCATION.
[14]"A Ca(2)+ signaling pathway regulates a K(+) channel for low-K response in Arabidopsis."
Li L., Kim B.-G., Cheong Y.H., Pandey G.K., Luan S.
Proc. Natl. Acad. Sci. U.S.A. 103:12625-12630(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CIPK23, PHOSPHORYLATION.
[15]"A protein phosphorylation/dephosphorylation network regulates a plant potassium channel."
Lee S.-C., Lan W.-Z., Kim B.-G., Li L., Cheong Y.H., Pandey G.K., Lu G., Buchanan B.B., Luan S.
Proc. Natl. Acad. Sci. U.S.A. 104:15959-15964(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH AIP1; CIPK6; CIPK16 AND CIPK23.
[16]"Calcineurin B-like protein CBL10 directly interacts with AKT1 and modulates K+ homeostasis in Arabidopsis."
Ren X.L., Qi G.N., Feng H.Q., Zhao S., Zhao S.S., Wang Y., Wu W.H.
Plant J. 74:258-266(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CBL10.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X62907 mRNA. Translation: CAA44693.1.
U06745 Genomic DNA. Translation: AAA96810.1.
AC003105 Genomic DNA. Translation: AAB95299.1.
CP002685 Genomic DNA. Translation: AEC07870.1.
AK227601 mRNA. Translation: BAE99592.1.
BT006442 mRNA. Translation: AAP21250.1.
PIRS23606.
S62694.
RefSeqNP_180233.1. NM_128222.5.
UniGeneAt.48521.
At.68413.

3D structure databases

ProteinModelPortalQ38998.
SMRQ38998. Positions 190-299, 485-840.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid2558. 12 interactions.
DIPDIP-36762N.
IntActQ38998. 7 interactions.

Protein family/group databases

TCDB1.A.1.4.1. the voltage-gated ion channel (vic) superfamily.

Proteomic databases

PaxDbQ38998.
PRIDEQ38998.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G26650.1; AT2G26650.1; AT2G26650.
GeneID817206.
KEGGath:AT2G26650.

Organism-specific databases

GeneFarm2792. 266.
TAIRAT2G26650.

Phylogenomic databases

eggNOGCOG0666.
HOGENOMHOG000238230.
InParanoidQ38998.
OMAAEQQGHE.
PhylomeDBQ38998.

Enzyme and pathway databases

BioCycARA:AT2G26550-MONOMER.
MetaCyc:MONOMER-14552.

Gene expression databases

GenevestigatorQ38998.

Family and domain databases

Gene3D1.25.40.20. 1 hit.
2.60.120.10. 1 hit.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR018490. cNMP-bd-like.
IPR000595. cNMP-bd_dom.
IPR005821. Ion_trans_dom.
IPR021789. K_channel_plant.
IPR003938. K_chnl_volt-dep_EAG/ELK/ERG.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
PfamPF00023. Ank. 3 hits.
PF00027. cNMP_binding. 1 hit.
PF11834. DUF3354. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSPR01415. ANKYRIN.
PR01463. EAGCHANLFMLY.
SMARTSM00248. ANK. 5 hits.
SM00100. cNMP. 1 hit.
[Graphical view]
SUPFAMSSF48403. SSF48403. 1 hit.
SSF51206. SSF51206. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 3 hits.
PS50042. CNMP_BINDING_3. 1 hit.
PS51490. KHA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAKT1_ARATH
AccessionPrimary (citable) accession number: Q38998
Secondary accession number(s): Q0WTF6, Q38797, Q84MA7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: January 1, 1998
Last modified: June 11, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names