AKT5_ARATH
ID AKT5_ARATH Reviewed; 880 AA.
AC Q9SCX5; Q9SUU2;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Probable potassium channel AKT5;
GN Name=AKT5; OrderedLocusNames=At4g32500; ORFNames=F8B4.200;
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 [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Hypocotyl;
RA Scheuermann S., Philippar K., Becker D., Hedrich R.;
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 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 [5]
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: Probable potassium channel. May interact with the
CC cytoskeleton or with regulatory proteins (By similarity).
CC {ECO:0000250}.
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.
CC {ECO:0000269|PubMed:10852932}.
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 AKT6.
CC {ECO:0000305|PubMed:10852932}.
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DR EMBL; AJ249479; CAB64728.1; -; mRNA.
DR EMBL; AL034567; CAA22577.2; -; Genomic_DNA.
DR EMBL; AL161581; CAB79967.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86069.1; -; Genomic_DNA.
DR PIR; F85381; F85381.
DR PIR; T05360; T05360.
DR RefSeq; NP_194976.1; NM_119402.4.
DR AlphaFoldDB; Q9SCX5; -.
DR SMR; Q9SCX5; -.
DR BioGRID; 14671; 2.
DR STRING; 3702.AT4G32500.1; -.
DR iPTMnet; Q9SCX5; -.
DR PaxDb; Q9SCX5; -.
DR PRIDE; Q9SCX5; -.
DR ProteomicsDB; 244945; -.
DR EnsemblPlants; AT4G32500.1; AT4G32500.1; AT4G32500.
DR GeneID; 829385; -.
DR Gramene; AT4G32500.1; AT4G32500.1; AT4G32500.
DR KEGG; ath:AT4G32500; -.
DR Araport; AT4G32500; -.
DR TAIR; locus:2127866; AT4G32500.
DR eggNOG; KOG0498; Eukaryota.
DR HOGENOM; CLU_005746_8_3_1; -.
DR InParanoid; Q9SCX5; -.
DR OMA; NESDHYG; -.
DR OrthoDB; 1073751at2759; -.
DR PhylomeDB; Q9SCX5; -.
DR PRO; PR:Q9SCX5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SCX5; baseline and differential.
DR Genevisible; Q9SCX5; 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; 2.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF11834; KHA; 1.
DR PRINTS; PR01415; ANKYRIN.
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; 2.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS51490; KHA; 1.
PE 2: Evidence at transcript 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..880
FT /note="Probable potassium channel AKT5"
FT /id="PRO_0000054123"
FT TOPO_DOM 1..82
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..111
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..182
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..217
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..265
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 266..285
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..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..880
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 541..570
FT /note="ANK 1"
FT REPEAT 574..603
FT /note="ANK 2"
FT REPEAT 607..636
FT /note="ANK 3"
FT REPEAT 637..667
FT /note="ANK 4"
FT REPEAT 671..700
FT /note="ANK 5"
FT DOMAIN 809..880
FT /note="KHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00823"
FT BINDING 396..517
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT CONFLICT 18
FT /note="E -> D (in Ref. 1; CAB64728)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="V -> F (in Ref. 1; CAB64728)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 880 AA; 98504 MW; E4412913D742E081 CRC64;
MGIEKRKKMV WFWPEKHEGG VIKEAEDVAA EHISREGTMS HYSFSKGLLP PLGVGATARS
SRHIKLRCFI VSPFDPRYRA WDWFLVILVL YTAWASPFEF GFLQTPRAPL SILDNVVNGF
FAVDIVLTFF VAFLDKATYL LVDDPKRIAW RYTSTWLIFD VVSTVPYELF GSLLHNTIQG
YGIFSMLRLW RLHRVSKCFA RLEKDRKYNY FWIRCTKLLL VSLFVVHCGA CFCYSIAAHY
PDPSMTFMAL AEANWKQKSL LIRYVTAMYW SITTFSTTGY GDIHGNNAEE RAFILFYMIF
NLGLLAYIIG NMTNLVVHVT SRTRNFRDTI QAASAFAQRN NLPLGLQEQM VAHLSLRYRT
DSEGLQQQEI IDSLPKAIRS SISHYLFYEV VDKTYLFHGI SNDLLFQLVS EMKAEYFPPK
EDVILRNEAP SDFYIMVTGA VDIIARVNGV DQVVGEAQTG HVFGEVGVLC YRPQLFTVRT
KRLSQLLRLN RTAFLNLVQA NVGDGAIIMN NLLQHLKDST DPVMKGILAE TELMLAQGKM
DLPLSLCFAA ARGDDLLLHQ LLKRGSNPNE TDKNGRTALH IAASKGSQYC VVLLLEHGAD
PNIRDSEGSV PLWEAIIGRH EENAKLLSEN GATLSFDTVG YFSCLAVGQN NLNALKDIVK
YGGDISLSDV NGTTALHRAV SEGNLEIVQF LLEKGADMDK PDVYGWTARA LAEHQGHEDI
KALFYNQRPV ERKTILVSGT PEIKPLMKHS SEPVMTHHHS REAMPPLARA VSQRRKLSNF
KNSLFGIMSA AKTGDEGGAS TRTGISEGVG GVYPARVTIS GEASSSGKVV KLPDSLEELI
EIGEKKLGFV ATKILSREGA EIDDIRIIRD GDFLLLLKVS
