KEA3_ARATH
ID KEA3_ARATH Reviewed; 776 AA.
AC Q9M0Z3; F4JGY3; Q9ZS89;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=K(+) efflux antiporter 3, chloroplastic {ECO:0000303|PubMed:11500563};
DE Short=AtKEA3 {ECO:0000303|PubMed:11500563};
DE Flags: Precursor;
GN Name=KEA3 {ECO:0000303|PubMed:11500563};
GN OrderedLocusNames=At4g04850 {ECO:0000312|Araport:AT4G04850};
GN ORFNames=T4B21.3 {ECO:0000312|EMBL:AAD03448.1};
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] (ISOFORM 2).
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 [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 GENE FAMILY, TISSUE SPECIFICITY, INDUCTION, AND SUBCELLULAR LOCATION.
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 [7]
RP FUNCTION, ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=25451040; DOI=10.1038/ncomms6439;
RA Armbruster U., Carrillo L.R., Venema K., Pavlovic L., Schmidtmann E.,
RA Kornfeld A., Jahns P., Berry J.A., Kramer D.M., Jonikas M.C.;
RT "Ion antiport accelerates photosynthetic acclimation in fluctuating light
RT environments.";
RL Nat. Commun. 5:5439-5439(2014).
RN [8]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
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. Accelerates
CC photosynthetic acclimation in fluctuating light environments.
CC {ECO:0000269|PubMed:25451040}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC {ECO:0000269|PubMed:18431481}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:24278440};
CC Multi-pass membrane protein {ECO:0000255}. Plastid, chloroplast
CC thylakoid membrane {ECO:0000269|PubMed:24794527,
CC ECO:0000269|PubMed:25451040}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Enriched in the stromal lamellae.
CC {ECO:0000269|PubMed:25451040}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9M0Z3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9M0Z3-2; Sequence=VSP_039359, VSP_039360, VSP_039361,
CC VSP_039362;
CC Name=3;
CC IsoId=Q9M0Z3-3; Sequence=VSP_039361, VSP_039362;
CC -!- TISSUE SPECIFICITY: Expressed in shoots and roots.
CC {ECO:0000269|PubMed:24278440}.
CC -!- INDUCTION: Up-regulated by low K(+) stress.
CC {ECO:0000269|PubMed:24278440}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:25451040,
CC PubMed:24794527). Kea1, kea2 and kea3 triple mutants are extremely
CC stunted in size with entirely pale leaves and died before steeing seeds
CC (PubMed:24794527). {ECO:0000269|PubMed:24794527,
CC ECO:0000269|PubMed:25451040}.
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=AAD03448.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AY051006; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAB80850.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF118223; AAD03448.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161501; CAB80850.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82432.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82433.1; -; Genomic_DNA.
DR EMBL; AY051006; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; A85061; A85061.
DR RefSeq; NP_001190675.1; NM_001203746.1. [Q9M0Z3-1]
DR RefSeq; NP_567272.4; NM_116723.5. [Q9M0Z3-3]
DR AlphaFoldDB; Q9M0Z3; -.
DR SMR; Q9M0Z3; -.
DR STRING; 3702.AT4G04850.2; -.
DR TCDB; 2.A.37.1.6; the monovalent cation:proton antiporter-2 (cpa2) family.
DR PaxDb; Q9M0Z3; -.
DR PRIDE; Q9M0Z3; -.
DR ProteomicsDB; 237042; -. [Q9M0Z3-1]
DR EnsemblPlants; AT4G04850.1; AT4G04850.1; AT4G04850. [Q9M0Z3-3]
DR EnsemblPlants; AT4G04850.2; AT4G04850.2; AT4G04850. [Q9M0Z3-1]
DR GeneID; 825822; -.
DR Gramene; AT4G04850.1; AT4G04850.1; AT4G04850. [Q9M0Z3-3]
DR Gramene; AT4G04850.2; AT4G04850.2; AT4G04850. [Q9M0Z3-1]
DR KEGG; ath:AT4G04850; -.
DR Araport; AT4G04850; -.
DR TAIR; locus:2138942; AT4G04850.
DR eggNOG; KOG1650; Eukaryota.
DR InParanoid; Q9M0Z3; -.
DR OMA; IRPFHDV; -.
DR OrthoDB; 138730at2759; -.
DR PhylomeDB; Q9M0Z3; -.
DR PRO; PR:Q9M0Z3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9M0Z3; baseline and differential.
DR Genevisible; Q9M0Z3; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:TAIR.
DR GO; GO:0000139; C:Golgi 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:0042651; C:thylakoid membrane; IDA:TAIR.
DR GO; GO:0015299; F:solute:proton antiporter activity; IEA:InterPro.
DR GO; GO:0009658; P:chloroplast organization; IGI:TAIR.
DR GO; GO:0009643; P:photosynthetic acclimation; IMP:TAIR.
DR GO; GO:1905157; P:positive regulation of photosynthesis; IMP:TAIR.
DR GO; GO:0006813; P:potassium ion transport; IEA:UniProtKB-KW.
DR GO; GO:0010109; P:regulation of photosynthesis; IGI:TAIR.
DR Gene3D; 1.20.1530.20; -; 1.
DR InterPro; IPR006153; Cation/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 PROSITE; PS51201; RCK_N; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Antiport; Chloroplast; Golgi apparatus;
KW Ion transport; Membrane; Plastid; Potassium; Potassium transport;
KW Reference proteome; Thylakoid; Transit peptide; Transmembrane;
KW Transmembrane helix; Transport.
FT TRANSIT 1..93
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 94..776
FT /note="K(+) efflux antiporter 3, chloroplastic"
FT /id="PRO_0000395099"
FT TRANSMEM 104..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 416..436
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 446..466
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 469..489
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 526..656
FT /note="RCK N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00543"
FT REGION 728..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..149
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_039359"
FT VAR_SEQ 150..163
FT /note="TDVKVLSEWGILFL -> MSSNDWPYPDYLWQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_039360"
FT VAR_SEQ 624..637
FT /note="SPIYARAQDLPHLL -> VISLFLLPFVNKIV (in isoform 2 and
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_039361"
FT VAR_SEQ 638..776
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_039362"
SQ SEQUENCE 776 AA; 83791 MW; 7D9B3A71AC7B8161 CRC64;
MAISTMLGSI SCCPSPKGYE MVKQHSVRLK HCVFTVKSSV PVYSEGVNDG IKLHSFGNLV
KKKVFLDTSK RFYFQGRWSE SSGRRVETYA GVDVASAVDV INDLGFDTLT FLMVTVIIVP
AFRILKASPI LGFFFAGVVL NQFGLIRNLT DVKVLSEWGI LFLLFEMGLE LSLARLKALA
KFAFGMGLTQ VLLCTAAFTA FELPPNGAIG TKILEFLFHS RPDLVNIRSI DEAVVIGAAL
SLSSSAFVLQ LLAEKGELPT RFGSATLGIL LLQDIAVVPL LVILPVLESQ DIGGESIWPM
LAKESAKALG GLGILSLGGK FFLRRIFEVV AETRSSEAFV ALCLLTVAGT SLVTQWLGFS
DTLGAFLAGA LLAETNFRTQ IEADIRPFRG LLLGLFFVTT GTSIDMEVLF REWPNVLSLL
GGLIVIKTLI ITAIGPRVGL TIQESVRVGF LLSQGGEFAF VVFSLANRLG VLPNELNKLL
IIVVVLSMAL TPYLNQLGRK AADFLDERLD PGEKIGEDVN FDVSESIVII GFGQMGQVLA
NFLSTPLVSD SDLVGWPYIG FDLNPAVVKE SRKLGFPILY GDGSRPSVLQ SAGVSSPKAI
MIMYKGKKRT TEAVQRLRLA FPGSPIYARA QDLPHLLELK KAGATDAILE NAETSLQLGS
KLLTGFGVMS DDVSFLSKVF RDSMEIQAQE EITASETNAG LKPMQMKASD INVVSAATQK
QVQLMKPMQM KASDSNSDSA AEILQETAGL SQPPEIDDSS VNIDNGFVGK ADKAQD
