CHX17_ARATH
ID CHX17_ARATH Reviewed; 820 AA.
AC Q9SUQ7;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Cation/H(+) antiporter 17;
DE AltName: Full=Protein CATION/H+ EXCHANGER 17;
DE Short=AtCHX17;
GN Name=CHX17; OrderedLocusNames=At4g23700; ORFNames=F9D16.170;
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 [MRNA], TISSUE SPECIFICITY, GENE FAMILY, AND
RP NOMENCLATURE.
RC TISSUE=Pollen;
RX PubMed=15347787; DOI=10.1104/pp.104.046003;
RA Sze H., Padmanaban S., Cellier F., Honys D., Cheng N.-H., Bock K.W.,
RA Conejero G., Li X., Twell D., Ward J.M., Hirschi K.D.;
RT "Expression patterns of a novel AtCHX gene family highlight potential roles
RT in osmotic adjustment and K+ homeostasis in pollen development.";
RL Plant Physiol. 136:2532-2547(2004).
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 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 FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=15341627; DOI=10.1111/j.1365-313x.2004.02177.x;
RA Cellier F., Conejero G., Ricaud L., Luu D.T., Lepetit M., Gosti F.,
RA Casse F.;
RT "Characterization of AtCHX17, a member of the cation/H+ exchangers, CHX
RT family, from Arabidopsis thaliana suggests a role in K+ homeostasis.";
RL Plant J. 39:834-846(2004).
RN [6]
RP FUNCTION.
RX PubMed=17133624; DOI=10.1002/yea.1424;
RA Maresova L., Sychrova H.;
RT "Arabidopsis thaliana CHX17 gene complements the kha1 deletion phenotypes
RT in Saccharomyces cerevisiae.";
RL Yeast 23:1167-1171(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-817 AND SER-819, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17869214; DOI=10.1016/j.bbrc.2007.08.177;
RA Hem S., Rofidal V., Sommerer N., Rossignol M.;
RT "Novel subsets of the Arabidopsis plasmalemma phosphoproteome identify
RT phosphorylation sites in secondary active transporters.";
RL Biochem. Biophys. Res. Commun. 363:375-380(2007).
CC -!- FUNCTION: Operates as a K(+)/H(+) antiporter that controls K(+)
CC acquisition and homeostasis. {ECO:0000269|PubMed:15341627,
CC ECO:0000269|PubMed:17133624}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in epidermal and cortical
CC cells of mature roots but also barely detected in leaves.
CC {ECO:0000269|PubMed:15347787}.
CC -!- INDUCTION: Up-regulated by NaCl, K(+) starvation and abscisic acid
CC (ABA). Induced at acidic external pH. {ECO:0000269|PubMed:15341627}.
CC -!- DISRUPTION PHENOTYPE: Decreased K(+) content in roots.
CC {ECO:0000269|PubMed:15341627}.
CC -!- MISCELLANEOUS: Could complement the kha1 deletion phenotypes in
CC S.cerevisiae.
CC -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 2 (CPA2)
CC transporter (TC 2.A.37) family. CHX (TC 2.A.37.4) subfamily.
CC {ECO:0000305}.
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DR EMBL; AY926473; AAX49545.1; -; mRNA.
DR EMBL; AL035394; CAA23036.1; -; Genomic_DNA.
DR EMBL; AL161559; CAB79325.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84796.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66834.1; -; Genomic_DNA.
DR PIR; T05602; T05602.
DR RefSeq; NP_001328705.1; NM_001341626.1.
DR RefSeq; NP_194101.1; NM_118501.5.
DR AlphaFoldDB; Q9SUQ7; -.
DR SMR; Q9SUQ7; -.
DR BioGRID; 13759; 3.
DR STRING; 3702.AT4G23700.1; -.
DR TCDB; 2.A.37.4.2; the monovalent cation:proton antiporter-2 (cpa2) family.
DR iPTMnet; Q9SUQ7; -.
DR PaxDb; Q9SUQ7; -.
DR PRIDE; Q9SUQ7; -.
DR ProteomicsDB; 246917; -.
DR EnsemblPlants; AT4G23700.1; AT4G23700.1; AT4G23700.
DR EnsemblPlants; AT4G23700.2; AT4G23700.2; AT4G23700.
DR GeneID; 828470; -.
DR Gramene; AT4G23700.1; AT4G23700.1; AT4G23700.
DR Gramene; AT4G23700.2; AT4G23700.2; AT4G23700.
DR KEGG; ath:AT4G23700; -.
DR Araport; AT4G23700; -.
DR TAIR; locus:2128484; AT4G23700.
DR eggNOG; KOG1650; Eukaryota.
DR HOGENOM; CLU_005126_6_2_1; -.
DR InParanoid; Q9SUQ7; -.
DR OMA; CHPMKAT; -.
DR OrthoDB; 336706at2759; -.
DR PhylomeDB; Q9SUQ7; -.
DR PRO; PR:Q9SUQ7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SUQ7; baseline and differential.
DR Genevisible; Q9SUQ7; AT.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005770; C:late endosome; IDA:TAIR.
DR GO; GO:0015299; F:solute:proton antiporter activity; IEA:InterPro.
DR GO; GO:0006813; P:potassium ion transport; IEA:UniProtKB-KW.
DR GO; GO:0006623; P:protein targeting to vacuole; IMP:TAIR.
DR GO; GO:0006885; P:regulation of pH; IMP:TAIR.
DR Gene3D; 1.20.1530.20; -; 1.
DR InterPro; IPR006153; Cation/H_exchanger.
DR InterPro; IPR038770; Na+/solute_symporter_sf.
DR Pfam; PF00999; Na_H_Exchanger; 1.
PE 1: Evidence at protein level;
KW Antiport; Ion transport; Membrane; Phosphoprotein; Potassium;
KW Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..820
FT /note="Cation/H(+) antiporter 17"
FT /id="PRO_0000394987"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 404..424
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 817
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17869214"
FT MOD_RES 819
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17869214"
SQ SEQUENCE 820 AA; 89166 MW; 8701F7E0C415CF4E CRC64;
MGTNGTTCPG PMKATSNGVF QGENPLEHAL PLLILQICIV LLLTRLLAFL LRPLRQPRVI
AEIVGGILLG PSALGKSTKF INTVFPPKSL TVLDTLANLG LIFFLFLVGL ELDPKSLKRT
GKRALSIALA GITLPFVLGI GTSFALRSSI ADGASKAPFL VFMGVALSIT AFPVLARILA
EIKLLTTDIG KIALSAAAVN DVAAWILLAL AVALSGEGSS PLTSLWVFLS GCGFVLFCIF
VVQPGIKLIA KRCPEGEPVN ELYVCCTLGI VLAASFVTDF IGIHALFGAF VIGVIFPKEG
NFANALVEKV EDLVSGLFLP LYFVSSGLKT NVATIQGAQS WGLLVLVIFN ACFGKIIGTV
LVSLYCKVPL DQSLALGFLM NTKGLVELIV LNIGKDRGVL NDQIFAIMVL MAIFTTFMTT
PLVLAVYKPG KSLTKADYKN RTVEETNRSN KPLCLMFCFQ SIMNIPTIVN LIEASRGINR
KENLSVYAMH LMELSERSSA ILMAHKVRRN GLPFWNKDKS ENNSSSSDMV VVAFEAFRRL
SRVSVRPMTA ISPMATIHED ICQSAERKKT AMVILPFHKH VRLDRTWETT RNDYRWINKK
VMEESPCSVA ILVDRGLGGT TRVASSDFSL TITVLFFGGN DDREALAFAV RMAEHPGISL
TVVRFIPSDE FKPENVRIEI TEDQLCSGAT RLIDIEAITE LKAKIKEKES SRSNSDSESH
IIYEEKIVKC YEEVIEVIKE YSKSNLFLVG KSPEGSVASG INVRSDTPEL GPIGNLLTES
ESVSTVASVL VVQQYIASRP VGISKNVTTE ESLVEDSESP
