CAX3_ARATH
ID CAX3_ARATH Reviewed; 459 AA.
AC Q93Z81; O65022; Q0WUY4; Q9LKW8;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Vacuolar cation/proton exchanger 3;
DE AltName: Full=Ca(2+)/H(+) antiporter CAX3;
DE AltName: Full=Ca(2+)/H(+) exchanger 3;
DE AltName: Full=Protein CATION EXCHANGER 3;
GN Name=CAX3; OrderedLocusNames=At3g51860; ORFNames=ATEM1.11;
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, AND INDUCTION.
RX PubMed=11080595; DOI=10.1016/s0378-1119(00)00390-5;
RA Shigaki T., Hirschi K.D.;
RT "Characterization of CAX-like genes in plants: implications for functional
RT diversity.";
RL Gene 257:291-298(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10645728; DOI=10.1023/a:1006395324818;
RA Comella P., Wu H.-J., Laudie M., Berger C., Cooke R., Delseny M.,
RA Grellet F.;
RT "Fine sequence analysis of 60 kb around the Arabidopsis thaliana AtEm1
RT locus on chromosome III.";
RL Plant Mol. Biol. 41:687-700(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 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-459.
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 [7]
RP ACTIVITY REGULATION, AND MUTAGENESIS OF 87-LYS--ARG-95.
RX PubMed=11562366; DOI=10.1074/jbc.m106637200;
RA Shigaki T., Cheng N.-H., Pittman J.K., Hirschi K.D.;
RT "Structural determinants of Ca2+ transport in the Arabidopsis H+/Ca2+
RT antiporter CAX1.";
RL J. Biol. Chem. 276:43152-43159(2001).
RN [8]
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 [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16055687; DOI=10.1104/pp.105.061218;
RA Cheng N.-H., Pittman J.K., Shigaki T., Lachmansingh J., LeClere S.,
RA Lahner B., Salt D.E., Hirschi K.D.;
RT "Functional association of Arabidopsis CAX1 and CAX3 is required for normal
RT growth and ion homeostasis.";
RL Plant Physiol. 138:2048-2060(2005).
CC -!- FUNCTION: Vacuolar cation/proton exchanger (CAX). Translocates Ca(2+)
CC and other metal ions into vacuoles using the proton gradient formed by
CC H(+)-ATPase and H(+)-pyrophosphatase (By similarity). Involved in ion
CC homeostasis in association with CAX1. {ECO:0000250,
CC ECO:0000269|PubMed:16055687}.
CC -!- ACTIVITY REGULATION: Inhibited by excess of Ca(2+).
CC {ECO:0000269|PubMed:11562366}.
CC -!- INTERACTION:
CC Q93Z81; Q39253: CAX1; NbExp=4; IntAct=EBI-2292420, EBI-2292388;
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000305|PubMed:16055687};
CC Multi-pass membrane protein {ECO:0000305|PubMed:16055687}.
CC Note=Tonoplast.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems and flowers.
CC {ECO:0000269|PubMed:11080595}.
CC -!- INDUCTION: By Ca(2+), Mg(2+) and Na(+). {ECO:0000269|PubMed:11080595}.
CC -!- SIMILARITY: Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19)
CC family. Cation/proton exchanger (CAX) 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; AF256228; AAF91349.1; -; mRNA.
DR EMBL; AF049236; AAC14413.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78853.1; -; Genomic_DNA.
DR EMBL; AY058054; AAL24162.1; -; mRNA.
DR EMBL; BT020374; AAV85729.1; -; mRNA.
DR EMBL; AK226999; BAE99064.1; -; mRNA.
DR PIR; T51157; T51157.
DR RefSeq; NP_190754.2; NM_115045.4.
DR AlphaFoldDB; Q93Z81; -.
DR SMR; Q93Z81; -.
DR BioGRID; 9667; 1.
DR ComplexPortal; CPX-1326; CAX1-CAX3 complex.
DR ComplexPortal; CPX-1600; CAX3 homodimer.
DR IntAct; Q93Z81; 1.
DR STRING; 3702.AT3G51860.1; -.
DR TCDB; 2.A.19.2.5; the ca(2+):cation antiporter (caca) family.
DR iPTMnet; Q93Z81; -.
DR PaxDb; Q93Z81; -.
DR PRIDE; Q93Z81; -.
DR ProteomicsDB; 222789; -.
DR EnsemblPlants; AT3G51860.1; AT3G51860.1; AT3G51860.
DR GeneID; 824349; -.
DR Gramene; AT3G51860.1; AT3G51860.1; AT3G51860.
DR KEGG; ath:AT3G51860; -.
DR Araport; AT3G51860; -.
DR TAIR; locus:2074348; AT3G51860.
DR eggNOG; KOG1397; Eukaryota.
DR HOGENOM; CLU_008721_2_0_1; -.
DR InParanoid; Q93Z81; -.
DR OMA; WHVSRAF; -.
DR PhylomeDB; Q93Z81; -.
DR PRO; PR:Q93Z81; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q93Z81; baseline and differential.
DR Genevisible; Q93Z81; AT.
DR GO; GO:0061993; C:calcium:proton antiporter complex; IPI:ComplexPortal.
DR GO; GO:0009705; C:plant-type vacuole membrane; IDA:TAIR.
DR GO; GO:0005774; C:vacuolar membrane; IDA:TAIR.
DR GO; GO:0005773; C:vacuole; IDA:TAIR.
DR GO; GO:0015369; F:calcium:proton antiporter activity; IDA:TAIR.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006812; P:cation transport; IMP:ComplexPortal.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:ComplexPortal.
DR GO; GO:0030026; P:cellular manganese ion homeostasis; IGI:TAIR.
DR GO; GO:0006882; P:cellular zinc ion homeostasis; IGI:TAIR.
DR GO; GO:0010351; P:lithium ion transport; IMP:ComplexPortal.
DR GO; GO:0055062; P:phosphate ion homeostasis; IGI:TAIR.
DR GO; GO:0006793; P:phosphorus metabolic process; IGI:TAIR.
DR GO; GO:0010119; P:regulation of stomatal movement; IMP:ComplexPortal.
DR GO; GO:0051592; P:response to calcium ion; IMP:TAIR.
DR GO; GO:0009624; P:response to nematode; HEP:TAIR.
DR Gene3D; 1.20.1420.30; -; 2.
DR InterPro; IPR004713; CaH_exchang.
DR InterPro; IPR004798; CAX-like.
DR InterPro; IPR004837; NaCa_Exmemb.
DR InterPro; IPR044880; NCX_ion-bd_dom_sf.
DR PANTHER; PTHR31503; PTHR31503; 1.
DR Pfam; PF01699; Na_Ca_ex; 2.
DR TIGRFAMs; TIGR00378; cax; 1.
PE 1: Evidence at protein level;
KW Antiport; Calcium; Calcium transport; Ion transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..459
FT /note="Vacuolar cation/proton exchanger 3"
FT /id="PRO_0000270152"
FT TOPO_DOM 1..67
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..95
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..129
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 151..161
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 183..195
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..238
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..283
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 305..327
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 349..362
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 384..386
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 387..407
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 408..417
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 439..459
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 137..172
FT /note="Cation selection"
FT /evidence="ECO:0000255"
FT REGION 335..370
FT /note="Cation selection"
FT /evidence="ECO:0000255"
FT MUTAGEN 87..95
FT /note="LANSYNYGR->ICTYCGVSQ: Facilitates Ca(2+)/H(+)
FT exchange activity."
FT /evidence="ECO:0000269|PubMed:11562366"
FT CONFLICT 126
FT /note="P -> R (in Ref. 1; AAF91349)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 459 AA; 49851 MW; 33B8AB06C3101FE1 CRC64;
MGSIVEPWAA IAENGNANVT AKGSSRELRH GRTAHNMSSS SLRKKSDLRL VQKVPCKTLK
NILSNLQEVI LGTKLTLLFL AIPLAILANS YNYGRPLIFG LSLIGLTPLA ERVSFLTEQL
AFYTGPTVGG LLNATCGNAT ELIIAILALA NNKVAVVKYS LLGSILSNLL LVLGTSLFFG
GIANIRREQR FDRKQADVNF FLLLMGLLCH LLPLLLKYAA TGEVSTSMIN KMSLTLSRTS
SIVMLIAYIA YLIFQLWTHR QLFEAQQDDD DAYDDEVSVE ETPVIGFWSG FAWLVGMTIV
IALLSEYVVD TIEDASDSWG LSVSFISIIL LPIVGNAAEH AGAIIFAFKN KLDISLGVAL
GSATQISLFV VPLSVIVAWI LGIKMDLNFN ILETSSLALA IIITAFTLQD GTSHYMKGLV
LLLCYVIIAA CFFVDQIPQP NDLDVGLQPM NNLGEVFSA
