Swiss-Prot entry
ID KAT2_ARATH STANDARD; PRT; 708 AA.
AC Q38849; O49732; Q9C5V9;
DT 29-MAR-2004 (Rel. 43, Created)
DT 29-MAR-2004 (Rel. 43, Last sequence update)
DT 10-MAY-2005 (Rel. 47, Last annotation update)
DE 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; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE, CHARACTERIZATION, AND INTERACTION WITH KAT1.
RC STRAIN=cv. Columbia;
RX MEDLINE=21264790; PubMed=11042178 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1074/jbc.M007303200;
RA Pilot G., Lacombe B., Gaymard F., Cherel I., Boucherez J.,
RA Thibaud J.-B., Sentenac H.;
RT "Guard cell inward K+ channel activity in Arabidopsis involves
RT expression 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 MEDLINE=20083488; PubMed=10617198 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
RA Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
RA Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
RA Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
RA Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
RA Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
RA Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
RA Langham S.-A., McCullagh B., Bilham L., Robben J.,
RA Van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
RA Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
RA Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
RA De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
RA Van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
RA Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
RA Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
RA Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
RA Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
RA Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
RA Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
RA Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
RA Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
RA Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
RA Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
RA Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
RA Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
RA Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
RA Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
RA Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
RA Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
RA 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.,
RA Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
RA Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
RA Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
RA Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
RA Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
RA Chen E., Marra M.A., Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis
RT thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE OF 144-708.
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 [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX MEDLINE=21392307; PubMed=11500563 [NCBI, ExPASy, EBI, Israel, Japan]; 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 This voltage-dependent channel could mediate long-term potassium
CC influx into guard cells leading to stomatal opening. Assuming
CC opened or closed conformations in response to the voltage
CC difference across the membrane, the channel is activated by
CC hyperpolarization. The channel activity is enhanced upon external
CC acidification.
CC -!- SUBUNIT: The potassium channel is probably composed of a homo- or
CC heterotetrameric complex of pore-forming subunits. May interact
CC with KAT1.
CC -!- SUBCELLULAR LOCATION: Integral membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in guard cells of hypocotyls, stems
CC leaves and petioles. Detected also in the phloem of minor veins
CC and in 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
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 (TC 1.A.1.4) family.
CC -!- SIMILARITY: Contains 1 cyclic nucleotide-binding domain.
CC -!- SIMILARITY: Contains 1 KHA domain.
CC --------------------------------------------------------------------------
CC This Swiss-Prot entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use as long as its content is in no way modified and this statement is not
CC removed.
CC --------------------------------------------------------------------------
DR EMBL; AJ288900; CAC28122.1; -; Genomic_DNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AL021713; CAA16801.1; ALT_INIT; Genomic_DNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AL161548; CAB78831.1; ALT_INIT; Genomic_DNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; U25694; AAA67070.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR PIR; H85205; H85205.
DR PIR; T04931; T04931.
DR GeneFarm; 2794; 266.
DR InterPro; IPR000595; cNMP_binding.
DR InterPro; IPR003938; EAG_ELK_ERG.
DR InterPro; IPR005821; Ion_trans.
DR InterPro; IPR001622; K+channel_pore.
DR InterPro; IPR005820; M+channel_nlg.
DR InterPro; Graphical view of domain structure.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; Graphical view of domain structure.
DR PRINTS; PR01463; EAGCHANLFMLY.
DR SMART; SM00100; cNMP; 1.
DR PROSITE; PS00888; CNMP_BINDING_1; FALSE_NEG.
DR PROSITE; PS00889; CNMP_BINDING_2; FALSE_NEG.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR CMR; Q38849.
DR ProDom [Domain structure / List of seq. sharing at least 1 domain]
DR BLOCKS; Q38849.
DR ProtoNet; Q38849.
DR ProtoMap; Q38849.
DR PRESAGE; Q38849.
DR DIP; Q38849.
DR ModBase; Q38849.
DR TAIR; At4g18290.
DR SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW Glycoprotein; Ion transport; Ionic channel; Potassium;
KW Potassium channel; Potassium transport; Transmembrane; Transport;
KW Voltage-gated channel.
FT TOPO_DOM 1 74 Cytoplasmic (Potential).
FT TRANSMEM 75 95 Segment S1 (Potential).
FT TRANSMEM 103 123 Segment S2 (Potential).
FT TOPO_DOM 124 145 Cytoplasmic (Potential).
FT TRANSMEM 146 166 Segment S3 (Potential).
FT TRANSMEM 177 197 Segment S4 (Potential).
FT TOPO_DOM 198 211 Cytoplasmic (Potential).
FT TRANSMEM 212 232 Segment S5 (Potential).
FT TRANSMEM 284 304 Segment S6 (Potential).
FT TOPO_DOM 305 708 Cytoplasmic (Potential).
FT DOMAIN 651 708 KHA.
FT NP_BIND 388 507 cNMP.
FT REGION 260 279 Segment H5 (pore-forming, in membrane)
FT (Potential).
FT CARBOHYD 169 169 N-linked (GlcNAc...) (Potential).
FT CONFLICT 369 369 A -> R (in Ref. 3).
FT CONFLICT 623 623 R -> S (in Ref. 3).
SQ SEQUENCE 708 AA; 81525 MW; 81010D8FEA5D8BFD CRC64;
MLKRKHLNTR PMSISCTRNF FKRFCVEEYN MDTFKHSSFL SADLLPSLGA RINQSTKLRK
HIISPFDPRF RGWEMWLVIL VIYSAWICPF EFAFITYKKD ALFIIDNIVN GFFAIDIILT
FFVAYLDSHS YLLVDKPKKI AIRYLSTWFA FDVCSTAPFQ SLSLLFKYNG SEIGFRVLSM
LRLWRLRRVS SLFARLEKDI RFNYFWTRCT KLISVTLFAV HCAGCFAYLI ADQYHDPTKT
WIGAVYPNFK ETSVWSRYVT ALYWSITTLT TTGYGDLHAE NPREMLFFVF FMLFNLGFTS
YLIGNMTNLV VHWTSRTRNF RDTVRAASEF ASRNQLPPNI QDQMLSHICL KFKTEGLKQQ
EALNGLPKAI RSSIANYLFF PIVQNVYLFH GVSRNFLFQL VSDIDAEYFP PREDVILQNE
APTDLYILVS GAVDFTVYVG EEDQVQGKAV VGDAFGEIGV LCYTPQPFTV RTTELSQILR
ISKKSLMSAM RAHVEDGRVI MNNLFMKLRG QQSIAIDDPN SEPESLLKEW LVGGSKTGEG
NASDQGHGHK YLQLHDSENI DMGSTEWRDS RRSGYGETKR VREHTIEIEE GEKPNKEFDG
KGCSDADLTS FEFHSQEAYP YCRSNIQIKQ HEAAKPKDKR VTIHLKSRDK DLSKLIILPA
SIEELLRLAG EKFGYSFTKV TNAENAEIDD EDVIRDGDHL YILINENS
//