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Protein

Cation/H(+) antiporter 17

Gene

CHX17

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Operates as a K+/H+ antiporter that controls K+ acquisition and homeostasis.2 Publications

GO - Molecular functioni

GO - Biological processi

  • potassium ion transport Source: UniProtKB-KW
  • protein targeting to vacuole Source: TAIR
  • regulation of pH Source: TAIR
Complete GO annotation...

Keywords - Biological processi

Antiport, Ion transport, Potassium transport, Transport

Keywords - Ligandi

Potassium

Protein family/group databases

TCDBi2.A.37.4.2. the monovalent cation:proton antiporter-2 (cpa2) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Cation/H(+) antiporter 17
Alternative name(s):
Protein CATION/H+ EXCHANGER 17
Short name:
AtCHX17
Gene namesi
Name:CHX17
Ordered Locus Names:At4g23700
ORF Names:F9D16.170
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G23700.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei30 – 5021HelicalSequence analysisAdd
BLAST
Transmembranei58 – 7518HelicalSequence analysisAdd
BLAST
Transmembranei90 – 11021HelicalSequence analysisAdd
BLAST
Transmembranei124 – 14421HelicalSequence analysisAdd
BLAST
Transmembranei159 – 17921HelicalSequence analysisAdd
BLAST
Transmembranei192 – 21221HelicalSequence analysisAdd
BLAST
Transmembranei222 – 24221HelicalSequence analysisAdd
BLAST
Transmembranei276 – 29621HelicalSequence analysisAdd
BLAST
Transmembranei313 – 33321HelicalSequence analysisAdd
BLAST
Transmembranei342 – 36221HelicalSequence analysisAdd
BLAST
Transmembranei374 – 39421HelicalSequence analysisAdd
BLAST
Transmembranei404 – 42421HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • late endosome Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Disruption phenotypei

Decreased K+ content in roots.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 820820Cation/H(+) antiporter 17PRO_0000394987Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei817 – 8171PhosphoserineCombined sources
Modified residuei819 – 8191PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9SUQ7.
PRIDEiQ9SUQ7.

PTM databases

iPTMnetiQ9SUQ7.

Expressioni

Tissue specificityi

Predominantly expressed in epidermal and cortical cells of mature roots but also barely detected in leaves.1 Publication

Inductioni

Up-regulated by NaCl, K+ starvation and abscisic acid (ABA). Induced at acidic external pH.1 Publication

Gene expression databases

GenevisibleiQ9SUQ7. AT.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT4G23700.1.

Structurei

3D structure databases

ProteinModelPortaliQ9SUQ7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1650. Eukaryota.
COG0475. LUCA.
HOGENOMiHOG000131548.
InParanoidiQ9SUQ7.
OMAiMELNERS.
PhylomeDBiQ9SUQ7.

Family and domain databases

InterProiIPR006153. Cation/H_exchanger.
[Graphical view]
PfamiPF00999. Na_H_Exchanger. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9SUQ7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGTNGTTCPG PMKATSNGVF QGENPLEHAL PLLILQICIV LLLTRLLAFL
60 70 80 90 100
LRPLRQPRVI AEIVGGILLG PSALGKSTKF INTVFPPKSL TVLDTLANLG
110 120 130 140 150
LIFFLFLVGL ELDPKSLKRT GKRALSIALA GITLPFVLGI GTSFALRSSI
160 170 180 190 200
ADGASKAPFL VFMGVALSIT AFPVLARILA EIKLLTTDIG KIALSAAAVN
210 220 230 240 250
DVAAWILLAL AVALSGEGSS PLTSLWVFLS GCGFVLFCIF VVQPGIKLIA
260 270 280 290 300
KRCPEGEPVN ELYVCCTLGI VLAASFVTDF IGIHALFGAF VIGVIFPKEG
310 320 330 340 350
NFANALVEKV EDLVSGLFLP LYFVSSGLKT NVATIQGAQS WGLLVLVIFN
360 370 380 390 400
ACFGKIIGTV LVSLYCKVPL DQSLALGFLM NTKGLVELIV LNIGKDRGVL
410 420 430 440 450
NDQIFAIMVL MAIFTTFMTT PLVLAVYKPG KSLTKADYKN RTVEETNRSN
460 470 480 490 500
KPLCLMFCFQ SIMNIPTIVN LIEASRGINR KENLSVYAMH LMELSERSSA
510 520 530 540 550
ILMAHKVRRN GLPFWNKDKS ENNSSSSDMV VVAFEAFRRL SRVSVRPMTA
560 570 580 590 600
ISPMATIHED ICQSAERKKT AMVILPFHKH VRLDRTWETT RNDYRWINKK
610 620 630 640 650
VMEESPCSVA ILVDRGLGGT TRVASSDFSL TITVLFFGGN DDREALAFAV
660 670 680 690 700
RMAEHPGISL TVVRFIPSDE FKPENVRIEI TEDQLCSGAT RLIDIEAITE
710 720 730 740 750
LKAKIKEKES SRSNSDSESH IIYEEKIVKC YEEVIEVIKE YSKSNLFLVG
760 770 780 790 800
KSPEGSVASG INVRSDTPEL GPIGNLLTES ESVSTVASVL VVQQYIASRP
810 820
VGISKNVTTE ESLVEDSESP
Length:820
Mass (Da):89,166
Last modified:May 1, 2000 - v1
Checksum:i8701F7E0C415CF4E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY926473 mRNA. Translation: AAX49545.1.
AL035394 Genomic DNA. Translation: CAA23036.1.
AL161559 Genomic DNA. Translation: CAB79325.1.
CP002687 Genomic DNA. Translation: AEE84796.1.
PIRiT05602.
RefSeqiNP_194101.1. NM_118501.4.
UniGeneiAt.2564.

Genome annotation databases

EnsemblPlantsiAT4G23700.1; AT4G23700.1; AT4G23700.
GeneIDi828470.
GrameneiAT4G23700.1; AT4G23700.1; AT4G23700.
KEGGiath:AT4G23700.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY926473 mRNA. Translation: AAX49545.1.
AL035394 Genomic DNA. Translation: CAA23036.1.
AL161559 Genomic DNA. Translation: CAB79325.1.
CP002687 Genomic DNA. Translation: AEE84796.1.
PIRiT05602.
RefSeqiNP_194101.1. NM_118501.4.
UniGeneiAt.2564.

3D structure databases

ProteinModelPortaliQ9SUQ7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT4G23700.1.

Protein family/group databases

TCDBi2.A.37.4.2. the monovalent cation:proton antiporter-2 (cpa2) family.

PTM databases

iPTMnetiQ9SUQ7.

Proteomic databases

PaxDbiQ9SUQ7.
PRIDEiQ9SUQ7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G23700.1; AT4G23700.1; AT4G23700.
GeneIDi828470.
GrameneiAT4G23700.1; AT4G23700.1; AT4G23700.
KEGGiath:AT4G23700.

Organism-specific databases

TAIRiAT4G23700.

Phylogenomic databases

eggNOGiKOG1650. Eukaryota.
COG0475. LUCA.
HOGENOMiHOG000131548.
InParanoidiQ9SUQ7.
OMAiMELNERS.
PhylomeDBiQ9SUQ7.

Miscellaneous databases

PROiQ9SUQ7.

Gene expression databases

GenevisibleiQ9SUQ7. AT.

Family and domain databases

InterProiIPR006153. Cation/H_exchanger.
[Graphical view]
PfamiPF00999. Na_H_Exchanger. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Expression patterns of a novel AtCHX gene family highlight potential roles in osmotic adjustment and K+ homeostasis in pollen development."
    Sze H., Padmanaban S., Cellier F., Honys D., Cheng N.-H., Bock K.W., Conejero G., Li X., Twell D., Ward J.M., Hirschi K.D.
    Plant Physiol. 136:2532-2547(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE.
    Tissue: Pollen.
  2. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. Cited for: GENE FAMILY, NOMENCLATURE.
  5. "Characterization of AtCHX17, a member of the cation/H+ exchangers, CHX family, from Arabidopsis thaliana suggests a role in K+ homeostasis."
    Cellier F., Conejero G., Ricaud L., Luu D.T., Lepetit M., Gosti F., Casse F.
    Plant J. 39:834-846(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, INDUCTION.
  6. "Arabidopsis thaliana CHX17 gene complements the kha1 deletion phenotypes in Saccharomyces cerevisiae."
    Maresova L., Sychrova H.
    Yeast 23:1167-1171(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Novel subsets of the Arabidopsis plasmalemma phosphoproteome identify phosphorylation sites in secondary active transporters."
    Hem S., Rofidal V., Sommerer N., Rossignol M.
    Biochem. Biophys. Res. Commun. 363:375-380(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-817 AND SER-819, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCHX17_ARATH
AccessioniPrimary (citable) accession number: Q9SUQ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: May 1, 2000
Last modified: July 6, 2016
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Could complement the kha1 deletion phenotypes in S.cerevisiae.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.