KAT3_ARATH
ID KAT3_ARATH Reviewed; 662 AA.
AC P92960;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Potassium channel KAT3;
DE AltName: Full=AKT4;
DE AltName: Full=AtKC1;
DE AltName: Full=Potassium channel TKC;
GN Name=KAT3; Synonyms=AKT4, KC1; OrderedLocusNames=At4g32650;
GN ORFNames=F4D11.150;
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=Leaf;
RA Saalbach G.;
RT "Characterisation of a putative chloroplast potassium channel in
RT Arabidopsis thaliana.";
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=cv. Columbia;
RA Kuech A., Reintanz B., Redhead C., Palme K.;
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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).
RN [7]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, CHARACTERIZATION, AND FUNCTION.
RX PubMed=11904452; DOI=10.1073/pnas.052677799;
RA Reintanz B., Szyroki A., Ivashikina N., Ache P., Godde M., Becker D.,
RA Palme K., Hedrich R.;
RT "AtKC1, a silent Arabidopsis potassium channel alpha-subunit modulates root
RT hair K+ influx.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4079-4084(2002).
RN [8]
RP FUNCTION, INTERACTION WITH AKT1 AND AKT2, TISSUE SPECIFICITY, AND
RP INDUCTION.
RX PubMed=12678562; DOI=10.1023/a:1022597102282;
RA Pilot G., Gaymard F., Mouline K., Cherel I., Sentenac H.;
RT "Regulated expression of Arabidopsis shaker K(+) channel genes involved in
RT K(+) uptake and distribution in the plant.";
RL Plant Mol. Biol. 51:773-787(2003).
RN [9]
RP INTERACTION WITH SLAC1.
RX PubMed=27002025; DOI=10.1105/tpc.16.01050;
RA Zhang A., Ren H.M., Tan Y.Q., Qi G.N., Yao F.Y., Wu G.L., Yang L.W.,
RA Hussain J., Sun S.J., Wang Y.F.;
RT "S-type anion channels SLAC1 and SLAH3 function as essential negative
RT regulators of inward K+ channels and stomatal opening in Arabidopsis.";
RL Plant Cell 28:949-955(2016).
CC -!- FUNCTION: Probable modulatory (alpha) subunit of inward-rectifying
CC potassium channels. Could mediate potassium uptake from the soil
CC solution by plant roots in association with AKT1.
CC {ECO:0000269|PubMed:11904452, ECO:0000269|PubMed:12678562}.
CC -!- SUBUNIT: The potassium channel is probably composed of a homo- or
CC heterotetrameric complex of pore-forming subunits. May interact with
CC AKT1 and AKT2 (PubMed:12678562). Interacts with SLAC1
CC (PubMed:27002025). {ECO:0000269|PubMed:12678562,
CC ECO:0000269|PubMed:27002025}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11904452}; Multi-
CC pass membrane protein {ECO:0000269|PubMed:11904452}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=P92960-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed predominantly in root hairs and root
CC endodermis and, at a lower level, in leaf nodes, trichomes, and
CC hydathodes. {ECO:0000269|PubMed:11904452, ECO:0000269|PubMed:12678562}.
CC -!- INDUCTION: Strongly reduced in roots after 2,4-dichlorophenoxyacetic
CC acid (2,4-D) treatment and after benzyladenine (BA) treatment. Strongly
CC induced in shoots after NaCl treatment. {ECO:0000269|PubMed:12678562}.
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}.
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DR EMBL; Z83202; CAB05669.1; -; mRNA.
DR EMBL; U73325; AAC98810.1; -; Genomic_DNA.
DR EMBL; U81239; AAD00503.1; -; mRNA.
DR EMBL; AL022537; CAA18596.1; -; Genomic_DNA.
DR EMBL; AL161581; CAB79982.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86097.1; -; Genomic_DNA.
DR EMBL; AY052233; AAK97703.1; -; mRNA.
DR EMBL; BT003093; AAO23890.1; -; mRNA.
DR PIR; T04461; T04461.
DR RefSeq; NP_194991.1; NM_119417.4. [P92960-1]
DR AlphaFoldDB; P92960; -.
DR SMR; P92960; -.
DR BioGRID; 14686; 19.
DR IntAct; P92960; 14.
DR STRING; 3702.AT4G32650.1; -.
DR TCDB; 1.A.1.4.9; the voltage-gated ion channel (vic) superfamily.
DR PaxDb; P92960; -.
DR PRIDE; P92960; -.
DR ProteomicsDB; 232274; -. [P92960-1]
DR EnsemblPlants; AT4G32650.1; AT4G32650.1; AT4G32650. [P92960-1]
DR GeneID; 829400; -.
DR Gramene; AT4G32650.1; AT4G32650.1; AT4G32650. [P92960-1]
DR KEGG; ath:AT4G32650; -.
DR Araport; AT4G32650; -.
DR TAIR; locus:2005524; AT4G32650.
DR eggNOG; KOG0498; Eukaryota.
DR InParanoid; P92960; -.
DR PhylomeDB; P92960; -.
DR PRO; PR:P92960; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P92960; baseline and differential.
DR Genevisible; P92960; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IMP:TAIR.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0009624; P:response to nematode; HEP:TAIR.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 2.60.120.10; -; 1.
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; PF00027; cNMP_binding; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF11834; KHA; 1.
DR PRINTS; PR01463; EAGCHANLFMLY.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF51206; SSF51206; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS51490; KHA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Ion channel; Ion transport; Membrane;
KW Potassium; Potassium channel; Potassium transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..662
FT /note="Potassium channel KAT3"
FT /id="PRO_0000054127"
FT TOPO_DOM 1..90
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 112..118
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..163
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..194
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..229
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..277
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 278..297
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..301
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..662
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 591..662
FT /note="KHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00823"
FT COILED 528..558
FT /evidence="ECO:0000255"
FT BINDING 406..527
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
SQ SEQUENCE 662 AA; 75598 MW; A6E90C9EB48387AC CRC64;
MSTTTTEARS PLPLLLRRGR SSTALSASTA EARSPLSILQ FRRRSSKDVR NITSVSSSLL
PAFGTFIEDD NPSSKPFIVL HFDRRYRLWE LFLVILVGYS AWASLFELAF EKAAEGALLT
IDLVVDFFFA VDIILTFFVS YLDNTTYLNV TDHKLIAKRY LKSVAFVMDV ASTLPIQFIY
KTITGDVGRG QAFGFLNLLR LWRLRRVAEL FKRLEKDAHF NYFVIRVIKL LCVTIFWIHL
AGCILYWIAY HYPRPTDTWI GSQVEDFKER SVWLGYTYSM YWSIVTLTTV GYGDLHAVNS
REKTFNMFYM LFNIGLTSYI IGIMTNLVVH GALRTFAMRS AINDILRYTS KNRLPDTMRE
QMLAHMQLKF KTAELRQEEV LQDLPKAIRS SINQHLFRSI IEEAYLFKGF PEGLLVQLVS
QIQAEYFPPK MEIILQNEIP TDFYVIVSGG VDIIASKGVS EQVLAKLGPG SMAGEIGVVF
NIPQPFTVRT RRLSQVIRIG HHKFKEMVQS DNDVDAKMII ANFMTYLKGL NDELKKEIPF
LRDLLDDADA QVQETVQSEE TPQSNDEEIV TVSRHENGQI EERRREGVPK RVIIHGQAPP
NQDNKNNGDS NGRLIILPDS IQLLFDLAEK KLGKRGSTIA MADGAHVEQI DALRENDHLY
IF
