CHX6A_ARATH
ID CHX6A_ARATH Reviewed; 818 AA.
AC Q8GX92; Q58P72; Q67ZY0; Q9LMZ3; Q9SGE4;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Cation/H(+) antiporter 6A;
DE AltName: Full=Protein CATION/H+ EXCHANGER 6a;
DE Short=AtCHX6a;
GN Name=CHX6a; Synonyms=CHX06a; OrderedLocusNames=At1g08140;
GN ORFNames=T23G18.2, T6D22.24;
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 [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-810, 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 [6]
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).
CC -!- FUNCTION: May operate as a cation/H(+) antiporter. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Preferentially expressed in pollen.
CC {ECO:0000269|PubMed:15347787}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAF18257.1; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 4 genes: At1g08135, At1g08140, At1g08150 and At1g08160.; Evidence={ECO:0000305};
CC Sequence=AAF79832.1; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 4 genes: At1g08135, At1g08140, At1g08150 and At1g08160.; Evidence={ECO:0000305};
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DR EMBL; AC011438; AAF18257.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC026875; AAF79832.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28253.1; -; Genomic_DNA.
DR EMBL; AK118358; BAC42972.1; -; mRNA.
DR EMBL; AK175987; BAD43750.1; -; mRNA.
DR EMBL; AK175998; BAD43761.1; -; mRNA.
DR EMBL; AK229961; BAF01787.1; -; mRNA.
DR EMBL; AK229972; BAF01797.1; -; mRNA.
DR EMBL; AY926467; AAX49539.1; -; mRNA.
DR PIR; A86216; A86216.
DR RefSeq; NP_849611.1; NM_179280.4.
DR AlphaFoldDB; Q8GX92; -.
DR BioGRID; 22576; 10.
DR IntAct; Q8GX92; 9.
DR STRING; 3702.AT1G08140.1; -.
DR PaxDb; Q8GX92; -.
DR PRIDE; Q8GX92; -.
DR ProteomicsDB; 246975; -.
DR EnsemblPlants; AT1G08140.1; AT1G08140.1; AT1G08140.
DR GeneID; 837335; -.
DR Gramene; AT1G08140.1; AT1G08140.1; AT1G08140.
DR KEGG; ath:AT1G08140; -.
DR Araport; AT1G08140; -.
DR TAIR; locus:2205150; AT1G08140.
DR eggNOG; KOG1650; Eukaryota.
DR HOGENOM; CLU_005126_6_1_1; -.
DR InParanoid; Q8GX92; -.
DR OMA; DSPMACN; -.
DR OrthoDB; 336706at2759; -.
DR PRO; PR:Q8GX92; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8GX92; baseline and differential.
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:0015299; F:solute:proton antiporter activity; IEA:InterPro.
DR GO; GO:0006812; P:cation transport; IC:TAIR.
DR GO; GO:0006813; P:potassium ion transport; IEA:UniProtKB-KW.
DR GO; GO:0006885; P:regulation of pH; IBA:GO_Central.
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..818
FT /note="Cation/H(+) antiporter 6A"
FT /id="PRO_0000394976"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
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 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 147
FT /note="L -> S (in Ref. 3; BAC42972 and 4; BAD43750/
FT BAD43761/BAF01787/BAF01797)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="E -> G (in Ref. 4; BAF01797/BAD43750)"
FT /evidence="ECO:0000305"
FT CONFLICT 488
FT /note="L -> I (in Ref. 3; BAC42972 and 4; BAD43750/
FT BAD43761/BAF01787/BAF01797)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 818 AA; 93395 MW; E8F580B2152E587D CRC64;
MATEEIDMSY WDVSWGEFNE DKNSSIFCES HPHIVNSHGI WEVMTFKRGM NFWEYPLPNL
EILIFSTFFI WRLLDISFNK IGLRVPRFTY MMIAGIILGQ TCHFSNKSWI HDIFFPDDNR
PKVAETLGAF GFVLYWFLKG VTMDAELPFR TEKRSSVIGF ITVIIPLICG SLTFRYRERR
GDSSILRMEY RLIIFLQSIS AFTSIDTLLK DLQIKHSEFG RIALSGAMVT DMLAFGVTFF
NAIYYEKLYG FMQTVGFCLF VVVMICVVRP AMYWVIKQTP EGRPVKDFYL YSIFGIAFAC
FTFFNKVIHL FGPAGSFVFG LTVPNGYPLG TTLIQKFESF NLGSILPLFG SLTMMQVDLL
RLFKESGDLI RMEGQIYEVI SFILLVNTTK FVVTTITAYA FKMPLRDSFA LALVLSNKGI
FELAYYTYAV ELKLIRPEVF TILAAYTLLN SIFIPMLLEL VHDPTKRFRC YRKRNLGILK
DGAALQCLMC VYRPDHITSM TDLLETFSPS QDSPMACNIL HLVELVGQAN PMFISHQLQK
PEPGSTSLSD NVIISFRGFQ RQFFEYTSLD IFTSVSVSQH MHEDICWLAL SRSLSLIVLP
FHRTWSVDRS TVISNDDNLR MLNVNVLRRA PCSVGIFVYR KPIVESHMAK SHSKICLIFN
GGKDDREALA ITNRMRLTEK RTRLTIIRFI PKSSEMDNDE WEQQQSINLK ESVTSIVGSN
IKENDAKVTY IDKAVSDGSE TSRILRAMAN DYDLFIVGSG SGIGTEATSG ISEWTEFNEL
GPIGDLLASH EYPSSASVLV VQKQVYIHHT KSQRRKSF
