KEA1_ARATH
ID KEA1_ARATH Reviewed; 1193 AA.
AC Q9ZTZ7; Q9LQ76; Q9LQ77;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=K(+) efflux antiporter 1, chloroplastic {ECO:0000303|PubMed:11500563};
DE Short=AtKEA1 {ECO:0000303|PubMed:11500563};
DE Flags: Precursor;
GN Name=KEA1 {ECO:0000303|PubMed:11500563};
GN OrderedLocusNames=At1g01790 {ECO:0000312|Araport:AT1G01790};
GN ORFNames=T1N6.20/T1N6.21 {ECO:0000312|EMBL:AAF78418.1,
GN ECO:0000312|EMBL:AAF78419.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 [MRNA] OF 474-1193.
RA Yao W., Hadjeb N., Berkowitz G.A.;
RT "KEA1, K efflux antiporter from Arabidopsis thaliana.";
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
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].
RC STRAIN=cv. Wassilewskija;
RX PubMed=12766230; DOI=10.1074/mcp.m300030-mcp200;
RA Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M.,
RA Garin J., Joyard J., Rolland N.;
RT "Proteomics of the chloroplast envelope membranes from Arabidopsis
RT thaliana.";
RL Mol. Cell. Proteomics 2:325-345(2003).
RN [6]
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 [7]
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 [8]
RP FUNCTION, GENE FAMILY, TISSUE SPECIFICITY, AND INDUCTION.
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: K(+)/H(+) antiporter involved in K(+) homeostasis and osmotic
CC adjustment. {ECO:0000269|PubMed:24278440}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC {ECO:0000269|PubMed:12766230, ECO:0000269|PubMed:18431481,
CC ECO:0000269|PubMed:24794527}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in shoots and roots.
CC {ECO:0000269|PubMed:24278440}.
CC -!- INDUCTION: Up-regulated by low K(+) 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 seems to have a regulatory or auto-
CC inhibitory function. {ECO:0000269|PubMed:24278440}.
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=AAD01191.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAF78418.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes.; Evidence={ECO:0000305};
CC Sequence=AAF78419.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes.; Evidence={ECO:0000305};
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DR EMBL; AF003382; AAD01191.1; ALT_INIT; mRNA.
DR EMBL; AC009273; AAF78418.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC009273; AAF78419.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27335.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58176.1; -; Genomic_DNA.
DR PIR; E86149; E86149.
DR PIR; F86149; F86149.
DR RefSeq; NP_001320631.1; NM_001331307.1.
DR RefSeq; NP_171684.2; NM_100062.5.
DR AlphaFoldDB; Q9ZTZ7; -.
DR SMR; Q9ZTZ7; -.
DR BioGRID; 22573; 6.
DR IntAct; Q9ZTZ7; 6.
DR STRING; 3702.AT1G01790.1; -.
DR TCDB; 2.A.37.1.4; the monovalent cation:proton antiporter-2 (cpa2) family.
DR iPTMnet; Q9ZTZ7; -.
DR PaxDb; Q9ZTZ7; -.
DR PRIDE; Q9ZTZ7; -.
DR ProteomicsDB; 250758; -.
DR EnsemblPlants; AT1G01790.1; AT1G01790.1; AT1G01790.
DR EnsemblPlants; AT1G01790.2; AT1G01790.2; AT1G01790.
DR GeneID; 837332; -.
DR Gramene; AT1G01790.1; AT1G01790.1; AT1G01790.
DR Gramene; AT1G01790.2; AT1G01790.2; AT1G01790.
DR KEGG; ath:AT1G01790; -.
DR Araport; AT1G01790; -.
DR TAIR; locus:2198215; AT1G01790.
DR eggNOG; KOG1650; Eukaryota.
DR HOGENOM; CLU_005126_3_0_1; -.
DR InParanoid; Q9ZTZ7; -.
DR OMA; YGFSRMM; -.
DR OrthoDB; 138730at2759; -.
DR PhylomeDB; Q9ZTZ7; -.
DR PRO; PR:Q9ZTZ7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9ZTZ7; baseline and differential.
DR Genevisible; Q9ZTZ7; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0031969; C:chloroplast membrane; IDA:TAIR.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:TAIR.
DR GO; GO:0015386; F:potassium:proton antiporter activity; IBA:GO_Central.
DR GO; GO:0009658; P:chloroplast organization; IGI:TAIR.
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; 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 Antiport; Chloroplast; Coiled coil; Ion transport; Membrane; Plastid;
KW Potassium; Potassium transport; Reference proteome; Transit peptide;
KW Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..49
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 50..1193
FT /note="K(+) efflux antiporter 1, chloroplastic"
FT /id="PRO_0000395097"
FT TRANSMEM 586..606
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 613..633
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 641..661
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 669..689
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 699..719
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 734..754
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 767..787
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 828..848
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 861..881
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 884..904
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 913..933
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 949..969
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 997..1119
FT /note="RCK N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00543"
FT REGION 103..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1165..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 131..355
FT /evidence="ECO:0000255"
FT COMPBIAS 106..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..463
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 649
FT /note="F -> L (in Ref. 3; AAD01191)"
FT /evidence="ECO:0000305"
FT CONFLICT 1021
FT /note="F -> Y (in Ref. 3; AAD01191)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1193 AA; 128033 MW; B4DDCD90AE6DDF3F CRC64;
MEYASTFQRP ILFHGGDGAS YCFPNRLISP KGISITSGDS KVHSCFRLRR NVAQSGTLNL
MNACFSGRFY SGHLHSTKSI LGNGHQAKRI PFGFRLRCQG HESLGNADSN DHRIGESSES
SDETEATDLK DARVENDTDS LEELKELLHK AIKELEVARL NSTMFEEKAQ RISERAIALK
DEAATAWLDV NKTLDVIRDT VYEEALAKEA VQTATMALSL AEARLQVIVE SLEAGAGNDI
PHVSEETEET IDVNDKEEAL LAAKDDIKEC QVNLDNCESQ LSALLSKKDE LQKEVDKLNE
FAETIQISSL KAEEDVTNIM KLAEQAVAFE LEATQRVNDA EIALQRAEKS LSISQTPEET
QGQLSDEETS QEDAMVLSGN VEDVTHQVEK ESPKDGDLPV VQITAELVPD IVGQRNKKLT
QPYESSDHEN GKPSVESSKV VEADSEKPKI NVQTKKQETQ KDLPKEGSSL NSPKASFNKS
SRFFSASFFS SNPDGTATVF GSLVGSVKQQ WPKLVLGLAL LGAGLTLYSN GVGGNNQLLQ
QPDVTSTSTE DVSSSTKPLI RQVQKLPKRI KKLLEMIPHQ EVNEEEASLF DFLWLLLASV
IFVPLFQKIP GGSPVLGYLA AGILIGPYGL SIIRNVHGTR AIAEFGVVFL LFNIGLELSV
ERLSSMKKYV FGLGSAQVLV TAAVVGLLAH YVAGQAGPAA IVIGNGLALS STAVVLQVLQ
ERGESTSRHG RASFSVLLFQ DLAVVVLLIL IPLISPNSSK GGIGFQAIAE ALGLAAVKAA
VAITAIIAGG RLLLRPIYKQ IAENRNAEIF SANTLLVILG TSLLTARAGL SMALGAFLAG
LLLAETEFSL QVESDIAPYR GLLLGLFFMT VGMSIDPKLL LSNFPVIVGT LGLLIVGKTM
LVVIMGKLFG ISIISAIRVG LLLAPGGEFA FVAFGEAVNQ GIMSPQLSSL LFLVVGISMA
ITPWLAAGGQ LIASRFELHD VRSLLPVESE TDDLQGHIII CGFGRVGQII AQLLSERLIP
FVALDVSSDR VTIGRSLDLP VYFGDAGSKE VLHKIGAGRA CAAVVALDAP GANYRCVWAL
SKFYPNVKTF VRAHDVVHGL NLEKAGATAV VPETLEPSLQ LAAAVLAQAK LPTSEIANTI
NEFRTRHLSE LTELCEASGS SLGYGYSRTS KPKPQPSDAS GDNQIIEGGT VVI
