KAT2_ARATH
ID KAT2_ARATH Reviewed; 697 AA.
AC Q38849; O49732; Q9C5V9;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 3.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Potassium channel KAT2;
GN Name=KAT2; OrderedLocusNames=At4g18290; ORFNames=T9A21.140;
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, AND INTERACTION WITH
RP KAT1.
RC STRAIN=cv. Columbia;
RX PubMed=11042178; DOI=10.1074/jbc.m007303200;
RA Pilot G., Lacombe B., Gaymard F., Cherel I., Boucherez J., Thibaud J.-B.,
RA Sentenac H.;
RT "Guard cell inward K+ channel activity in Arabidopsis involves expression
RT of the twin channel subunits KAT1 and KAT2.";
RL J. Biol. Chem. 276:3215-3221(2001).
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 NUCLEOTIDE SEQUENCE [MRNA] OF 133-697.
RC STRAIN=cv. Columbia;
RA Butt A.D., Blatt M.R., Ainsworth C.C.;
RT "Expression, evolution and genomic complexity of potassium ion channel
RT genes of Arabidopsis thaliana.";
RL J. Plant Physiol. 150:652-660(1997).
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).
RN [6]
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: Highly selective inward-rectifying potassium channel. This
CC voltage-dependent channel could mediate long-term potassium influx into
CC guard cells leading to stomatal opening. Assuming opened or closed
CC conformations in response to the voltage difference across the
CC membrane, the channel is activated by hyperpolarization. The channel
CC activity is enhanced upon external acidification.
CC -!- SUBUNIT: The potassium channel is probably composed of a homo- or
CC heterotetrameric complex of pore-forming subunits. May interact with
CC KAT1 (Probable). Interacts with SLAC1 (PubMed:27002025).
CC {ECO:0000269|PubMed:27002025, ECO:0000305}.
CC -!- INTERACTION:
CC Q38849; Q38898: AKT2; NbExp=3; IntAct=EBI-2117720, EBI-1552774;
CC Q38849; Q39128: KAT1; NbExp=3; IntAct=EBI-2117720, EBI-1552490;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in guard cells of hypocotyls, stems
CC leaves and petioles. Detected also in the phloem of minor veins and in
CC flower at a lower level.
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 -!- SEQUENCE CAUTION:
CC Sequence=CAC28122.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ288900; CAC28122.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL021713; CAA16801.1; -; Genomic_DNA.
DR EMBL; AL161548; CAB78831.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84021.1; -; Genomic_DNA.
DR EMBL; U25694; AAA67070.1; -; mRNA.
DR PIR; H85205; H85205.
DR PIR; T04931; T04931.
DR RefSeq; NP_001329801.1; NM_001341273.1.
DR RefSeq; NP_193563.3; NM_117939.5.
DR AlphaFoldDB; Q38849; -.
DR SMR; Q38849; -.
DR BioGRID; 12848; 3.
DR IntAct; Q38849; 2.
DR STRING; 3702.AT4G18290.1; -.
DR TCDB; 1.A.1.4.6; the voltage-gated ion channel (vic) superfamily.
DR PaxDb; Q38849; -.
DR PRIDE; Q38849; -.
DR ProteomicsDB; 232243; -.
DR EnsemblPlants; AT4G18290.1; AT4G18290.1; AT4G18290.
DR GeneID; 827555; -.
DR Gramene; AT4G18290.1; AT4G18290.1; AT4G18290.
DR KEGG; ath:AT4G18290; -.
DR Araport; AT4G18290; -.
DR TAIR; locus:2005531; AT4G18290.
DR eggNOG; KOG0498; Eukaryota.
DR HOGENOM; CLU_005746_8_2_1; -.
DR InParanoid; Q38849; -.
DR OMA; FPIIRQA; -.
DR OrthoDB; 247304at2759; -.
DR PRO; PR:Q38849; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q38849; baseline and differential.
DR Genevisible; Q38849; 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:0007623; P:circadian rhythm; IMP:TAIR.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0009644; P:response to high light intensity; IMP:TAIR.
DR GO; GO:0010118; P:stomatal movement; IMP: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 Glycoprotein; Ion channel; Ion transport; Membrane; Potassium;
KW Potassium channel; Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..697
FT /note="Potassium channel KAT2"
FT /id="PRO_0000054126"
FT TOPO_DOM 1..63
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..91
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..134
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 156..165
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 187..200
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..248
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 249..268
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 269..272
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..293
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 294..697
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 629..697
FT /note="KHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00823"
FT BINDING 377..496
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 358
FT /note="A -> R (in Ref. 4; AAA67070)"
FT /evidence="ECO:0000305"
FT CONFLICT 612
FT /note="R -> S (in Ref. 4; AAA67070)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 697 AA; 80150 MW; 55E1DFE6AB2A2453 CRC64;
MSISCTRNFF KRFCVEEYNM DTFKHSSFLS ADLLPSLGAR INQSTKLRKH IISPFDPRFR
GWEMWLVILV IYSAWICPFE FAFITYKKDA LFIIDNIVNG FFAIDIILTF FVAYLDSHSY
LLVDKPKKIA IRYLSTWFAF DVCSTAPFQS LSLLFKYNGS EIGFRVLSML RLWRLRRVSS
LFARLEKDIR FNYFWTRCTK LISVTLFAVH CAGCFAYLIA DQYHDPTKTW IGAVYPNFKE
TSVWSRYVTA LYWSITTLTT TGYGDLHAEN PREMLFFVFF MLFNLGFTSY LIGNMTNLVV
HWTSRTRNFR DTVRAASEFA SRNQLPPNIQ DQMLSHICLK FKTEGLKQQE ALNGLPKAIR
SSIANYLFFP IVQNVYLFHG VSRNFLFQLV SDIDAEYFPP REDVILQNEA PTDLYILVSG
AVDFTVYVGE EDQVQGKAVV GDAFGEIGVL CYTPQPFTVR TTELSQILRI SKKSLMSAMR
AHVEDGRVIM NNLFMKLRGQ QSIAIDDPNS EPESLLKEWL VGGSKTGEGN ASDQGHGHKY
LQLHDSENID MGSTEWRDSR RSGYGETKRV REHTIEIEEG EKPNKEFDGK GCSDADLTSF
EFHSQEAYPY CRSNIQIKQH EAAKPKDKRV TIHLKSRDKD LSKLIILPAS IEELLRLAGE
KFGYSFTKVT NAENAEIDDE DVIRDGDHLY ILINENS
