AKT6_ARATH
ID AKT6_ARATH Reviewed; 888 AA.
AC Q8GXE6; Q9SLA3;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Potassium channel AKT6;
DE AltName: Full=Potassium channel SPIK;
DE AltName: Full=Shaker pollen inward rectifier K(+) channel;
GN Name=AKT6; Synonyms=SPIK; OrderedLocusNames=At2g25600; ORFNames=F3N11.5;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, TISSUE SPECIFICITY,
RP AND FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=11825875; DOI=10.1101/gad.213902;
RA Mouline K., Very A.-A., Gaymard F., Boucherez J., Pilot G., Devic M.,
RA Bouchez D., Thibaud J.-B., Sentenac H.;
RT "Pollen tube development and competitive ability are impaired by disruption
RT of a Shaker K(+) channel in Arabidopsis.";
RL Genes Dev. 16:339-350(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 407-888.
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=10852932; DOI=10.2307/3871214;
RA Lacombe B., Pilot G., Michard E., Gaymard F., Sentenac H., Thibaud J.-B.;
RT "A shaker-like K(+) channel with weak rectification is expressed in both
RT source and sink phloem tissues of Arabidopsis.";
RL Plant Cell 12:837-851(2000).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11500563; DOI=10.1104/pp.126.4.1646;
RA Maeser P., Thomine S., Schroeder J.I., Ward J.M., Hirschi K., Sze H.,
RA Talke I.N., Amtmann A., Maathuis F.J.M., Sanders D., Harper J.F.,
RA Tchieu J., Gribskov M., Persans M.W., Salt D.E., Kim S.A., Guerinot M.L.;
RT "Phylogenetic relationships within cation transporter families of
RT Arabidopsis.";
RL Plant Physiol. 126:1646-1667(2001).
CC -!- FUNCTION: Highly selective inward-rectifying potassium channel that
CC could mediate potassium uptake in the pollen membrane. Plays an
CC important role in pollen tube development. Assuming opened or closed
CC conformations in response to the voltage difference across the
CC membrane, the channel is activated by hyperpolarization. May interact
CC with the cytoskeleton or with regulatory proteins.
CC {ECO:0000269|PubMed:11825875}.
CC -!- SUBUNIT: The potassium channel is probably composed of a homo- or
CC heterotetrameric complex of pore-forming subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in flowers; especially in
CC pollen. {ECO:0000269|PubMed:10852932, ECO:0000269|PubMed:11825875}.
CC -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC characterized by a series of positively charged amino acids. The pore-
CC forming region H5 is enclosed by the transmembrane segments S5 and S6
CC in the Shaker-type (1P/6TM) and contains the GYGD signature motif which
CC seems to be involved in potassium selectivity.
CC -!- DOMAIN: The KHA domain (rich in hydrophobic and acidic residues)
CC present in the C-terminal part is likely to be important for
CC tetramerization.
CC -!- SIMILARITY: Belongs to the potassium channel family. Plant (TC 1.A.1.4)
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: Was originally erroneously termed AKT5.
CC {ECO:0000305|PubMed:10852932}.
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DR EMBL; AJ309323; CAC85283.1; -; Genomic_DNA.
DR EMBL; AC006053; AAD31377.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07722.1; -; Genomic_DNA.
DR EMBL; AK118279; BAC42897.1; -; mRNA.
DR PIR; D84650; D84650.
DR RefSeq; NP_180131.3; NM_128118.5.
DR AlphaFoldDB; Q8GXE6; -.
DR SMR; Q8GXE6; -.
DR BioGRID; 2451; 7.
DR IntAct; Q8GXE6; 7.
DR STRING; 3702.AT2G25600.1; -.
DR TCDB; 1.A.1.4.8; the voltage-gated ion channel (vic) superfamily.
DR PaxDb; Q8GXE6; -.
DR PRIDE; Q8GXE6; -.
DR ProteomicsDB; 244705; -.
DR EnsemblPlants; AT2G25600.1; AT2G25600.1; AT2G25600.
DR GeneID; 817099; -.
DR Gramene; AT2G25600.1; AT2G25600.1; AT2G25600.
DR KEGG; ath:AT2G25600; -.
DR Araport; AT2G25600; -.
DR TAIR; locus:2050276; AT2G25600.
DR eggNOG; KOG0498; Eukaryota.
DR HOGENOM; CLU_005746_8_3_1; -.
DR InParanoid; Q8GXE6; -.
DR OMA; GSHYCVV; -.
DR OrthoDB; 1073751at2759; -.
DR PhylomeDB; Q8GXE6; -.
DR PRO; PR:Q8GXE6; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8GXE6; baseline and differential.
DR Genevisible; Q8GXE6; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
DR InterPro; IPR045319; KAT/AKT.
DR InterPro; IPR021789; KHA_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR45743; PTHR45743; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF13857; Ank_5; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF11834; KHA; 1.
DR PRINTS; PR01463; EAGCHANLFMLY.
DR SMART; SM00248; ANK; 4.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF51206; SSF51206; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 3.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS51490; KHA; 1.
PE 1: Evidence at protein level;
KW ANK repeat; Ion channel; Ion transport; Membrane; Potassium;
KW Potassium channel; Potassium transport; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..888
FT /note="Potassium channel AKT6"
FT /id="PRO_0000054124"
FT TOPO_DOM 1..84
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 106..113
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 135..155
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..184
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..219
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 241..267
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 268..287
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 288..291
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 313..888
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 543..572
FT /note="ANK 1"
FT REPEAT 576..605
FT /note="ANK 2"
FT REPEAT 609..638
FT /note="ANK 3"
FT REPEAT 640..669
FT /note="ANK 4"
FT REPEAT 673..702
FT /note="ANK 5"
FT DOMAIN 822..888
FT /note="KHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00823"
FT REGION 10..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 398..519
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
SQ SEQUENCE 888 AA; 99215 MW; 60479CE59404505E CRC64;
MEKKKVWFWG VKDDGEGGGG RGGGRTKDAE DDVADHLSRD GTMSQYSLSK GLLPSLGANN
RSSRDVILPR FIVSPFDPRY RAWETFLVFL VLYTAWASPF EFGFLQKPRP PLSILDNIVN
GFFAVDIVLT FFVAFLDKVT YLLVDDPKRI AWRYASTWLI FDVVSTFPYE IFGSLLHESI
QGYGIFSMLR LWRLRRVSNC FARLEKDRKY SYFWVRCSKL LLVTLFVIHC GACFLYSIAA
HYPDPSKTFM ALTDENWKES PIAVRYNTAM YWSITTFSTT GYGDIHGVNS REMTFILFYM
VFNLGLSAYI IGNMTNLVVH VTGRTRKFRD TIQAASGFGQ RNNLPVRLQD QMVAHLCLRY
RTDSEGLQQQ EIIDSLPKAI RSSISHYLFY EVVDKIYLFH GISNDLLFQL VTEMKAEYFP
PKEDVILQNE APTDFYILVT GAVDIIARVN GVEQVVSEAQ RGHVFGEVGV LCYRPQLFTV
RTKRLSQLLR LNRTVLLNLV QANVGDGAII MNNLLQHLKD SEDPVMKGVL ADTEHMLAQG
KMDLPLSLCF AAARGDDLLL HQLLRRGSSP NEMDKDGRTA LHIAASKGSH YCVVLLLEHG
ADPNIRDSEG NVPLWEAIIG RHREIAKLLA ENGAKLSLDS VSYFSGLAVE KNCLDALKDI
IKYGGDVTLP DGNGTTALHR AVSEGHLEIV KFLLDQGADL DWPDSYGWTP RGLADHQGNE
EIKTLFHNHR PVEKKPKPIP GIPQSPVTGK PLMKYSSEPT MHSGELVLDG GQVVVSQKRK
LNNFRNSLFG IISAANSADD GGEVPRSPAV PGGGGSMIYP ERVTISSPEN GETGGKVVLL
PNSMEELLKI GENKMGFVPT KVLTREGAEI DDITLIRDGD FLLLSRDP
