CHX20_ARATH
ID CHX20_ARATH Reviewed; 842 AA.
AC Q9M353; Q58P63;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Cation/H(+) antiporter 20;
DE AltName: Full=Protein CATION/H+ EXCHANGER 20;
DE Short=AtCHX20;
GN Name=CHX20; OrderedLocusNames=At3g53720; ORFNames=F5K20_20;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 [LARGE SCALE MRNA].
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-838, 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 [7]
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 [8]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=17337534; DOI=10.1104/pp.106.092155;
RA Padmanaban S., Chanroj S., Kwak J.M., Li X., Ward J.M., Sze H.;
RT "Participation of endomembrane cation/H+ exchanger AtCHX20 in
RT osmoregulation of guard cells.";
RL Plant Physiol. 144:82-93(2007).
CC -!- FUNCTION: Operates as a K(+)/H(+) antiporter that maintains K(+)
CC homeostasis in guard cells and could regulate pH. Plays a critical role
CC in osmoregulation through the control of stomates opening.
CC {ECO:0000269|PubMed:17337534}.
CC -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000269|PubMed:17337534}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:17337534}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves and stems. Preferentially
CC expressed in guards cells. {ECO:0000269|PubMed:15347787,
CC ECO:0000269|PubMed:17337534}.
CC -!- DISRUPTION PHENOTYPE: Impaired light-induced stomatal opening.
CC {ECO:0000269|PubMed:17337534}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL132960; CAB88334.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79132.1; -; Genomic_DNA.
DR EMBL; BT002529; AAO00889.1; -; mRNA.
DR EMBL; BT010870; AAR24648.1; -; mRNA.
DR EMBL; AK227229; BAE99266.1; -; mRNA.
DR EMBL; AY926476; AAX49548.1; -; mRNA.
DR PIR; T45912; T45912.
DR RefSeq; NP_190940.1; NM_115232.3.
DR AlphaFoldDB; Q9M353; -.
DR SMR; Q9M353; -.
DR BioGRID; 9856; 7.
DR IntAct; Q9M353; 6.
DR STRING; 3702.AT3G53720.1; -.
DR TCDB; 2.A.37.4.8; the monovalent cation:proton antiporter-2 (cpa2) family.
DR iPTMnet; Q9M353; -.
DR PaxDb; Q9M353; -.
DR PRIDE; Q9M353; -.
DR ProteomicsDB; 246919; -.
DR EnsemblPlants; AT3G53720.1; AT3G53720.1; AT3G53720.
DR GeneID; 824539; -.
DR Gramene; AT3G53720.1; AT3G53720.1; AT3G53720.
DR KEGG; ath:AT3G53720; -.
DR Araport; AT3G53720; -.
DR TAIR; locus:2084370; AT3G53720.
DR eggNOG; KOG1650; Eukaryota.
DR HOGENOM; CLU_005126_6_2_1; -.
DR InParanoid; Q9M353; -.
DR OrthoDB; 336706at2759; -.
DR PhylomeDB; Q9M353; -.
DR PRO; PR:Q9M353; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M353; baseline and differential.
DR Genevisible; Q9M353; AT.
DR GO; GO:0012505; C:endomembrane system; IDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015299; F:solute:proton antiporter activity; IEA:InterPro.
DR GO; GO:0030007; P:cellular potassium ion homeostasis; IMP:TAIR.
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 GO; GO:0030104; P:water homeostasis; 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 2: Evidence at transcript level;
KW Antiport; Ion transport; Membrane; Potassium; Potassium transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..842
FT /note="Cation/H(+) antiporter 20"
FT /id="PRO_0000394990"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 380..400
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 413..433
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 585..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 842 AA; 91553 MW; AD69A1295C5491A7 CRC64;
MPFNITSVKT SSNGVWQGDN PLNFAFPLLI VQTALIIAVS RFLAVLFKPL RQPKVIAEIV
GGILLGPSAL GRNMAYMDRI FPKWSMPILE SVASIGLLFF LFLVGLELDL SSIRRSGKRA
FGIAVAGITL PFIAGVGVAF VIRNTLYTAA DKPGYAEFLV FMGVALSITA FPVLARILAE
LKLLTTQIGE TAMAAAAFND VAAWILLALA VALAGNGGEG GGEKKSPLVS LWVLLSGAGF
VVFMLVVIRP GMKWVAKRGS PENDVVRESY VCLTLAGVMV SGFATDLIGI HSIFGAFVFG
LTIPKDGEFG QRLIERIEDF VSGLLLPLYF ATSGLKTDVA KIRGAESWGM LGLVVVTACA
GKIVGTFVVA VMVKVPAREA LTLGFLMNTK GLVELIVLNI GKEKKVLNDE TFAILVLMAL
FTTFITTPTV MAIYKPARGT HRKLKDLSAS QDSTKEELRI LACLHGPANV SSLISLVESI
RTTKILRLKL FVMHLMELTE RSSSIIMVQR ARKNGLPFVH RYRHGERHSN VIGGFEAYRQ
LGRVAVRPIT AVSPLPTMHE DICHMADTKR VTMIILPFHK RWNADHGHSH HHQDGGGDGN
VPENVGHGWR LVNQRVLKNA PCSVAVLVDR GLGSIEAQTL SLDGSNVVER VCVIFFGGPD
DRESIELGGR MAEHPAVKVT VIRFLVRETL RSTAVTLRPA PSKGKEKNYA FLTTNVDPEK
EKELDEGALE DFKSKWKEMV EYKEKEPNNI IEEILSIGQS KDFDLIVVGR GRIPSAEVAA
LAERQAEHPE LGPIGDVLAS SINHIIPSIL VVQQHNKAHV EDITVSKIVS ESSLSINGDT
NV
