CCX1_ARATH
ID CCX1_ARATH Reviewed; 570 AA.
AC Q9FKP1; Q8W102;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Cation/calcium exchanger 1;
DE Short=AtCCX1;
DE AltName: Full=Protein CATION EXCHANGER 7;
GN Name=CCX1; Synonyms=CAX7; OrderedLocusNames=At5g17860;
GN ORFNames=MPI7.2, MVA3_210;
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=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
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 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, AND SUBCELLULAR LOCATION.
RA Chen Z., Wu Y., Di L., Shen Y., Wang G.;
RT "AtCCX1 transports Na+ and K+ in Pitch pastoris.";
RL Afr. J. Biotechnol. 10:9743-9750(2011).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX DOI=10.1007/s11240-011-0077-6;
RA Chen Z., Wu Y., Di L., Wang G., Shen Y.;
RT "The AtCCX1 transporter mediates salinity tolerance in both Arabidopsis and
RT yeast.";
RL Plant Cell Tissue Organ Cult. 0:0-0(2012).
CC -!- FUNCTION: Vacuolar membrane-localized H(+)-dependent K(+) and Na(+)
CC transporter. {ECO:0000269|Ref.5, ECO:0000269|Ref.6}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|Ref.5}; Multi-pass
CC membrane protein {ECO:0000269|Ref.5}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems and flowers.
CC {ECO:0000269|Ref.6}.
CC -!- INDUCTION: By salt stress and drought stress. {ECO:0000269|Ref.6}.
CC -!- SIMILARITY: Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19)
CC family. Cation/calcium exchanger (CCX) subfamily. {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; AB011480; BAB11219.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92479.1; -; Genomic_DNA.
DR EMBL; AF462830; AAL58918.1; -; mRNA.
DR EMBL; AY142021; AAM98285.1; -; mRNA.
DR RefSeq; NP_197288.1; NM_121792.4.
DR AlphaFoldDB; Q9FKP1; -.
DR BioGRID; 16930; 2.
DR IntAct; Q9FKP1; 2.
DR STRING; 3702.AT5G17860.1; -.
DR PaxDb; Q9FKP1; -.
DR PRIDE; Q9FKP1; -.
DR ProteomicsDB; 224382; -.
DR EnsemblPlants; AT5G17860.1; AT5G17860.1; AT5G17860.
DR GeneID; 831654; -.
DR Gramene; AT5G17860.1; AT5G17860.1; AT5G17860.
DR KEGG; ath:AT5G17860; -.
DR Araport; AT5G17860; -.
DR TAIR; locus:2175906; AT5G17860.
DR eggNOG; KOG2399; Eukaryota.
DR HOGENOM; CLU_004979_1_2_1; -.
DR InParanoid; Q9FKP1; -.
DR OMA; FKLRRAC; -.
DR OrthoDB; 478735at2759; -.
DR PhylomeDB; Q9FKP1; -.
DR PRO; PR:Q9FKP1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FKP1; baseline and differential.
DR Genevisible; Q9FKP1; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR GO; GO:0008324; F:cation transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006812; P:cation transport; IBA:GO_Central.
DR GO; GO:0006813; P:potassium ion transport; IEA:UniProtKB-KW.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1420.30; -; 2.
DR InterPro; IPR004837; NaCa_Exmemb.
DR InterPro; IPR044880; NCX_ion-bd_dom_sf.
DR Pfam; PF01699; Na_Ca_ex; 2.
PE 2: Evidence at transcript level;
KW Antiport; Ion transport; Membrane; Potassium; Potassium transport;
KW Reference proteome; Sodium; Sodium transport; Transmembrane;
KW Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..570
FT /note="Cation/calcium exchanger 1"
FT /id="PRO_0000416822"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 401..421
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 479..499
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 513..533
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 546..566
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 48
FT /note="A -> V (in Ref. 3; AAL58918)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 570 AA; 61864 MW; 5C67ECFC44BCDC5D CRC64;
MASLFSSRLG SQSLSLLINI FFIFLIFLHF ASQTPPPSGS IQTLNSFAGG DSDSCSGGLA
SLDDHRSKCS YIRSQSKCGP QGYIDYLKIF FCIFGQSPVL GHLVLSAWLF VLFYLLGDTA
ASYFCPSLDS LSKVLKLSPT MAGVTLLSLG NGAPDLFSSV VSFTRSNNGD FGLNSILGGA
FFVSSFVVGT ICVLIGSRDV AIDRNSFIRD VVFLLVALCC LGLIIFIGKV TIWVALCYLS
IYLLYVGFLS VSHFFDRKKR MSDQILRSRE DLAEMGVSLL GYIAEEKLAL PEKTTQEFKI
VFEDSPKRHR SCFSVLVSII GLPLYLPRRL TIPVVCEEKW SKPCAVVSTA IAPVLLTELY
CSHYSGSQRN LILYIISGSI GLIVGILAYL TTEKSHPPKK FSLVWLLGGF TMSVTWTYMI
AQELVSLLIS LGNIFGISPS VLGLTVLAWG NSLGDLIANV TVAFHGGNDG AQIALSGCYA
GPLFNTVIGL GVPLVISSLA EYPGVYIIPS DNSLLETLGF LMVGLLWALV IMPKKKMRLD
KLVGGGLLAI YLCFLSLRLA RVFGVLDTDR