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 01-MAY-2013, entry version 86.
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;
GN ORFNames=F3N11.5;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, TISSUE
RP SPECIFICITY, 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
RT disruption 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.,
RA Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
RA Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
RA Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
RA Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
RA Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis
RT thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RG The Arabidopsis Information Resource (TAIR);
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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.,
RA Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T.,
RA Shibata K., 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=10.1105/tpc.12.6.837;
RA Lacombe B., Pilot G., Michard E., Gaymard F., Sentenac H.,
RA Thibaud J.-B.;
RT "A shaker-like K(+) channel with weak rectification is expressed in
RT both 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.,
RA 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
CC that could mediate potassium uptake in the pollen membrane. Plays
CC an important role in pollen tube development. Assuming opened or
CC closed conformations in response to the voltage difference across
CC the membrane, the channel is activated by hyperpolarization. May
CC interact with the cytoskeleton or with regulatory proteins.
CC -!- SUBUNIT: The potassium channel is probably composed of a homo- or
CC heterotetrameric complex of pore-forming subunits (By similarity).
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in flowers; especially
CC in pollen.
CC -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC characterized by a series of positively charged amino acids. The
CC pore-forming region H5 is enclosed by the transmembrane segments
CC S5 and S6 in the Shaker-type (1P/6TM) and contains the GYGD
CC signature motif which seems to be involved in potassium
CC 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
CC (TC 1.A.1.4) subfamily.
CC -!- SIMILARITY: Contains 5 ANK repeats.
CC -!- SIMILARITY: Contains 1 cyclic nucleotide-binding domain.
CC -!- SIMILARITY: Contains 1 KHA domain.
CC -!- CAUTION: Was originally (PubMed:10852932) erroneously termed AKT5.
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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 IPI; IPI00538925; -.
DR PIR; D84650; D84650.
DR RefSeq; NP_180131.3; NM_128118.4.
DR UniGene; At.39001; -.
DR ProteinModelPortal; Q8GXE6; -.
DR SMR; Q8GXE6; 266-318, 325-492, 515-874.
DR STRING; 3702.AT2G25600.1-P; -.
DR TCDB; 1.A.1.4.8; voltage-gated ion channel (VIC) superfamily.
DR PaxDb; Q8GXE6; -.
DR PRIDE; Q8GXE6; -.
DR EnsemblPlants; AT2G25600.1; AT2G25600.1; AT2G25600.
DR GeneID; 817099; -.
DR KEGG; ath:AT2G25600; -.
DR GeneFarm; 2793; 266.
DR TAIR; At2g25600; -.
DR eggNOG; COG0666; -.
DR HOGENOM; HOG000238230; -.
DR InParanoid; Q8GXE6; -.
DR OMA; ERDESMI; -.
DR PhylomeDB; Q8GXE6; -.
DR Genevestigator; Q8GXE6; -.
DR GermOnline; AT2G25600; Arabidopsis thaliana.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR021789; K_channel_plant.
DR InterPro; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF11834; DUF3354; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR PRINTS; PR01463; EAGCHANLFMLY.
DR SMART; SM00248; ANK; 4.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF48403; ANK; 1.
DR SUPFAM; SSF51206; cNMP_binding; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 3.
DR PROSITE; PS00888; CNMP_BINDING_1; FALSE_NEG.
DR PROSITE; PS00889; CNMP_BINDING_2; FALSE_NEG.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS51490; KHA; 1.
PE 1: Evidence at protein level;
KW ANK repeat; Complete proteome; Ion channel; Ion transport; Membrane;
KW Potassium; Potassium channel; Potassium transport; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel.
FT CHAIN 1 888 Potassium channel AKT6.
FT /FTId=PRO_0000054124.
FT TOPO_DOM 1 84 Cytoplasmic (Potential).
FT TRANSMEM 85 105 Helical; Name=Segment S1; (Potential).
FT TOPO_DOM 106 113 Extracellular (Potential).
FT TRANSMEM 114 134 Helical; Name=Segment S2; (Potential).
FT TOPO_DOM 135 155 Cytoplasmic (Potential).
FT TRANSMEM 156 176 Helical; Name=Segment S3; (Potential).
FT TOPO_DOM 177 184 Extracellular (Potential).
FT TRANSMEM 185 205 Helical; Voltage-sensor; Name=Segment S4;
FT (Potential).
FT TOPO_DOM 206 219 Cytoplasmic (Potential).
FT TRANSMEM 220 240 Helical; Name=Segment S5; (Potential).
FT TOPO_DOM 241 267 Extracellular (Potential).
FT INTRAMEM 268 287 Pore-forming; Name=Segment H5;
FT (Potential).
FT TOPO_DOM 288 291 Extracellular (Potential).
FT TRANSMEM 292 312 Helical; Name=Segment S6; (Potential).
FT TOPO_DOM 313 888 Cytoplasmic (Potential).
FT REPEAT 543 572 ANK 1.
FT REPEAT 576 605 ANK 2.
FT REPEAT 609 638 ANK 3.
FT REPEAT 640 669 ANK 4.
FT REPEAT 673 702 ANK 5.
FT DOMAIN 822 888 KHA.
FT NP_BIND 398 519 cNMP.
FT COMPBIAS 15 24 Poly-Gly.
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
//
