KEA2_ARATH
ID KEA2_ARATH Reviewed; 1174 AA.
AC O65272; O65273;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=K(+) efflux antiporter 2, chloroplastic {ECO:0000303|PubMed:11500563};
DE Short=AtKEA2 {ECO:0000303|PubMed:11500563};
DE Flags: Precursor;
GN Name=KEA2 {ECO:0000303|PubMed:11500563};
GN OrderedLocusNames=At4g00630/At4g00640 {ECO:0000312|Araport:AT4G00630};
GN ORFNames=F6N23.14/F6N23.15 {ECO:0000312|EMBL:AAC13619.1,
GN ECO:0000312|EMBL:AAC13638.1};
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 638-920.
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [4]
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP ASP-721 AND GLU-833.
RX PubMed=22551943; DOI=10.1016/j.bbamem.2012.04.011;
RA Aranda-Sicilia M.N., Cagnac O., Chanroj S., Sze H., Rodriguez-Rosales M.P.,
RA Venema K.;
RT "Arabidopsis KEA2, a homolog of bacterial KefC, encodes a K(+)/H(+)
RT antiporter with a chloroplast transit peptide.";
RL Biochim. Biophys. Acta 1818:2362-2371(2012).
RN [8]
RP FUNCTION, GENE FAMILY, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=24278440; DOI=10.1371/journal.pone.0081463;
RA Zheng S., Pan T., Fan L., Qiu Q.S.;
RT "A novel AtKEA gene family, homolog of bacterial K+/H+ antiporters, plays
RT potential roles in K+ homeostasis and osmotic adjustment in Arabidopsis.";
RL PLoS ONE 8:E81463-E81463(2013).
RN [9]
RP DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=24794527; DOI=10.1073/pnas.1323899111;
RA Kunz H.H., Gierth M., Herdean A., Satoh-Cruz M., Kramer D.M., Spetea C.,
RA Schroeder J.I.;
RT "Plastidial transporters KEA1, -2, and -3 are essential for chloroplast
RT osmoregulation, integrity, and pH regulation in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:7480-7485(2014).
CC -!- FUNCTION: Electroneutral K(+)/H(+) antiporter modulating monovalent
CC cation and pH homeostasis in plastids (PubMed:22551943,
CC PubMed:24278440). Transports K(+) and Cs(+) preferentially relative to
CC Na(+) or Li(+) (PubMed:22551943). May function in osmotic adjustment
CC (PubMed:24278440). {ECO:0000269|PubMed:22551943,
CC ECO:0000269|PubMed:24278440}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC {ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:22551943,
CC ECO:0000269|PubMed:24794527}; Multi-pass membrane protein
CC {ECO:0000255}.
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=O65272-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Detected in leaves, stems and flowers
CC (PubMed:22551943). Expressed in shoots and roots (PubMed:24278440).
CC {ECO:0000269|PubMed:22551943, ECO:0000269|PubMed:24278440}.
CC -!- INDUCTION: Up-regulated by osmotic stress and down-regulated by high
CC K(+). {ECO:0000269|PubMed:24278440}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Kea1 and kea2 double
CC mutants display strong growth retardation along with pale green leaves.
CC Kea1, kea2 and kea3 triple mutants are extremely stunted in size with
CC entirely pale leaves and died before steeing seeds.
CC {ECO:0000269|PubMed:24794527}.
CC -!- MISCELLANEOUS: The full-length protein being inactive in a heterologous
CC system, the N-terminal region (58-556) seems to have a regulatory or
CC auto-inhibitory function. {ECO:0000269|PubMed:22551943}.
CC -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 2 (CPA2)
CC transporter (TC 2.A.37) family. KEA (TC 2.A.37.1) subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC13619.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At4g00630 and At4g00640.; Evidence={ECO:0000305};
CC Sequence=AAC13638.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At4g00630 and At4g00640.; Evidence={ECO:0000305};
CC Sequence=BX839410; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
CC Sequence=CAB80872.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At4g00630 and At4g00640.; Evidence={ECO:0000305};
CC Sequence=CAB80873.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At4g00630 and At4g00640.; Evidence={ECO:0000305};
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DR EMBL; AF058919; AAC13619.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF058919; AAC13638.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161472; CAB80872.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161472; CAB80873.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE81911.1; -; Genomic_DNA.
DR EMBL; BX839410; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T01227; T01227.
DR PIR; T01228; T01228.
DR RefSeq; NP_191972.6; NM_116288.7. [O65272-1]
DR AlphaFoldDB; O65272; -.
DR SMR; O65272; -.
DR STRING; 3702.AT4G00630.2; -.
DR TCDB; 2.A.37.1.7; the monovalent cation:proton antiporter-2 (cpa2) family.
DR iPTMnet; O65272; -.
DR PaxDb; O65272; -.
DR PRIDE; O65272; -.
DR ProteomicsDB; 237059; -. [O65272-1]
DR EnsemblPlants; AT4G00630.1; AT4G00630.1; AT4G00630. [O65272-1]
DR GeneID; 825834; -.
DR Gramene; AT4G00630.1; AT4G00630.1; AT4G00630. [O65272-1]
DR KEGG; ath:AT4G00630; -.
DR Araport; AT4G00630; -.
DR eggNOG; KOG1650; Eukaryota.
DR InParanoid; O65272; -.
DR OMA; ITCQAND; -.
DR PRO; PR:O65272; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O65272; baseline and differential.
DR Genevisible; O65272; AT.
DR GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR GO; GO:0009706; C:chloroplast inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0015386; F:potassium:proton antiporter activity; IMP:CACAO.
DR Gene3D; 1.20.1530.20; -; 1.
DR InterPro; IPR006153; Cation/H_exchanger.
DR InterPro; IPR004771; K/H_exchanger.
DR InterPro; IPR038770; Na+/solute_symporter_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003148; RCK_N.
DR Pfam; PF00999; Na_H_Exchanger; 1.
DR Pfam; PF02254; TrkA_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00932; 2a37; 1.
DR PROSITE; PS51201; RCK_N; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Antiport; Chloroplast; Coiled coil; Ion transport;
KW Membrane; Plastid; Plastid inner membrane; Potassium; Potassium transport;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix;
KW Transport.
FT TRANSIT 1..57
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 58..1174
FT /note="K(+) efflux antiporter 2, chloroplastic"
FT /id="PRO_0000395098"
FT TRANSMEM 566..586
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 593..613
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 621..641
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 649..669
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 679..699
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 714..734
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 747..767
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 808..828
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 842..862
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 866..886
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 899..919
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 929..949
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 977..1099
FT /note="RCK N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00543"
FT REGION 119..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1141..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 142..350
FT /evidence="ECO:0000255"
FT COMPBIAS 420..448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1142..1168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 721
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:22551943"
FT MUTAGEN 833
FT /note="E->K: Loss of activity."
FT /evidence="ECO:0000269|PubMed:22551943"
SQ SEQUENCE 1174 AA; 126157 MW; 0A2EFED250DADF80 CRC64;
MDFASSVQRQ SMFHGGADFA SYCLPNRMIS AKLCPKGLGG TRFWDPMIDS KVRSAIRSKR
NVSYRSSLTL NADFNGRFYG HLLPAKPQNV PLGFRLLCQS SDSVGDLVGN DRNLEFAEGS
DDREVTFSKE EKDTREQDSA PSLEELRDLL NKATKELEVA SLNSTMFEEK AQRISEVAIA
LKDEAASAWN DVNQTLNVVQ EAVDEESVAK EAVQKATMAL SLAEARLQVA LESLEAEGYN
TSEESEVRDG VKDKEEALLS AKADIKECQE NLASCEEQLR RLQVKKDELQ KEVDRLNEAA
ERAQISALKA EEDVANIMVL AEQAVAFELE ATQRVNDAEI ALQRAEKTLF GSQTQETTQG
KVLDGKNTIV GEDEVLSEIV DVSHQAERDL VVVGVSSDVG TQSYESDNEN GKPTADFAKE
AEGEAEKSKN VVLTKKQEVQ KDLPRESSSH NGTKTSLKKS SRFFPASFFS SNGDGTATVF
ESLVESAKQQ WPKLILGFTL LGAGVAIYSN GVGRNNQLPQ QPNIVSTSAE DVSSSTKPLI
RQMQKLPKRI KKLLEMFPQQ EVNEEEASLL DVLWLLLASV IFVPLFQKIP GGSPVLGYLA
AGILIGPYGL SIIRNVHGTK AIAEFGVVFL LFNIGLELSV ERLSSMKKYV FGLGSAQVLV
TAAVIGLITH YVAGQAGPAA IVIGNGLALS STAVVLQVLQ ERGESTSRHG RATFSVLLFQ
DLAVVVLLIL IPLISPNSSK GGIGFQAIAE ALGLAAIKAA VAITGIIAGG RLLLRPIYKQ
IAENRNAEIF SANTLLVILG TSLLTARAGL SMALGAFLAG LLLAETEFSL QVESDIAPYR
GLLLGLFFMT VGMSIDPKLL LANFPLIMGT LGLLLVGKTI LVVIIGKLFG ISIISAVRVG
LLLAPGGEFA FVAFGEAVNQ GIMTPQLSSL LFLVVGISMA LTPWLAAGGQ LIASRFELQD
VRSLLPVESE TDDLQGHIII CGFGRIGQII AQLLSERLIP FVALDVSSDR VAIGRSLDLP
VYFGDAGSRE VLHKIGADRA CAAAIALDTP GANYRCVWAL SKYFPNVKTF VRAHDVDHGL
NLEKAGATAV VPETLEPSLQ LAAAVLAQAK LPTSEIATTI NEFRSRHLSE LAELCEASGS
SLGYGFSRST SKPKPPSPSE TSDDNQIIEG TLAI
