CAX2_ARATH
ID CAX2_ARATH Reviewed; 441 AA.
AC Q39254; Q944Q1; Q9LTT6;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Vacuolar cation/proton exchanger 2;
DE AltName: Full=Ca(2+)/H(+) antiporter CAX2;
DE AltName: Full=Ca(2+)/H(+) exchanger 2;
DE AltName: Full=Protein CATION EXCHANGER 2;
GN Name=CAX2; OrderedLocusNames=At3g13320; ORFNames=MDC11.10, MDC11.19;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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 [MRNA] OF 43-441.
RC STRAIN=cv. Columbia;
RX PubMed=8710949; DOI=10.1073/pnas.93.16.8782;
RA Hirschi K.D., Zhen R.-G., Cunningham K.W., Rea P.A., Fink G.R.;
RT "CAX1, an H+/Ca2+ antiporter from Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:8782-8786(1996).
RN [5]
RP ACTIVITY REGULATION, AND MUTAGENESIS OF 89-LEU--LYS-97.
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 [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).
RN [7]
RP FUNCTION, ACTIVITY REGULATION, AND MUTAGENESIS OF 65-SER--ASN-75;
RP 152-LYS--THR-162 AND 177-CYS--PHE-186.
RX PubMed=12496310; DOI=10.1074/jbc.m209952200;
RA Shigaki T., Pittman J.K., Hirschi K.D.;
RT "Manganese specificity determinants in the Arabidopsis metal/H+ antiporter
RT CAX2.";
RL J. Biol. Chem. 278:6610-6617(2003).
RN [8]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF HIS-222 AND HIS-226.
RX PubMed=15862304; DOI=10.1016/j.febslet.2005.03.085;
RA Pittman J.K., Shigaki T., Hirschi K.D.;
RT "Evidence of differential pH regulation of the Arabidopsis vacuolar Ca2+/H+
RT antiporters CAX1 and CAX2.";
RL FEBS Lett. 579:2648-2656(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. {ECO:0000269|PubMed:12496310}.
CC -!- ACTIVITY REGULATION: Inhibited by excess of Ca(2+) and Cd(2+), Mn(2+),
CC and Zn(2+). {ECO:0000269|PubMed:11562366, ECO:0000269|PubMed:12496310}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0 for cytosolic pH. {ECO:0000269|PubMed:15862304};
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}. Note=Tonoplast.
CC -!- SIMILARITY: Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19)
CC family. Cation/proton exchanger (CAX) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02801.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB024034; BAB02801.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75333.1; -; Genomic_DNA.
DR EMBL; AF424628; AAL11621.1; -; mRNA.
DR EMBL; AY097343; AAM19859.1; -; mRNA.
DR EMBL; U57412; AAB05914.1; -; mRNA.
DR RefSeq; NP_566452.1; NM_112177.3.
DR AlphaFoldDB; Q39254; -.
DR SMR; Q39254; -.
DR BioGRID; 5866; 5.
DR IntAct; Q39254; 5.
DR STRING; 3702.AT3G13320.1; -.
DR TCDB; 2.A.19.2.4; the ca(2+):cation antiporter (caca) family.
DR PaxDb; Q39254; -.
DR PRIDE; Q39254; -.
DR ProteomicsDB; 223885; -.
DR EnsemblPlants; AT3G13320.1; AT3G13320.1; AT3G13320.
DR GeneID; 820532; -.
DR Gramene; AT3G13320.1; AT3G13320.1; AT3G13320.
DR KEGG; ath:AT3G13320; -.
DR Araport; AT3G13320; -.
DR TAIR; locus:2088130; AT3G13320.
DR eggNOG; KOG1397; Eukaryota.
DR HOGENOM; CLU_008721_2_1_1; -.
DR InParanoid; Q39254; -.
DR OMA; NENEETC; -.
DR OrthoDB; 727723at2759; -.
DR PhylomeDB; Q39254; -.
DR PRO; PR:Q39254; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q39254; baseline and differential.
DR Genevisible; Q39254; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009705; C:plant-type vacuole 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:0006816; P:calcium ion transport; IDA:TAIR.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central.
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..441
FT /note="Vacuolar cation/proton exchanger 2"
FT /id="PRO_0000270151"
FT TOPO_DOM 1..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..97
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..129
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 151..166
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..196
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218..231
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 253..286
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..311
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 333..354
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 376..384
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 406..412
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 413..433
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 434..441
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 139..174
FT /note="Cation selection"
FT /evidence="ECO:0000255"
FT REGION 333..368
FT /note="Cation selection"
FT /evidence="ECO:0000255"
FT MUTAGEN 67..75
FT /note="SIKIVIFCN->NLQEVILGT: Loss of Mn(2+) transport."
FT MUTAGEN 89..97
FT /note="LVHYMIDSK->ICTYCGVSQ: Facilitates Ca(2+)/H(+)
FT exchange activity."
FT /evidence="ECO:0000269|PubMed:11562366"
FT MUTAGEN 152..162
FT /note="KNGMIRVVQLT->TNNKVAVVKYS: Loss of Mn(2+) transport."
FT /evidence="ECO:0000269|PubMed:12496310"
FT MUTAGEN 177..186
FT /note="CAFFCGGLVF->TSLFCGGIAN: Loss of Mn(2+) transport."
FT /evidence="ECO:0000269|PubMed:12496310"
FT MUTAGEN 222
FT /note="H->A: Loss of transport activity."
FT /evidence="ECO:0000269|PubMed:15862304"
FT MUTAGEN 222
FT /note="H->D: Loss of transport activity."
FT /evidence="ECO:0000269|PubMed:15862304"
FT MUTAGEN 222
FT /note="H->K: No effect on transport activity."
FT /evidence="ECO:0000269|PubMed:15862304"
FT MUTAGEN 226
FT /note="H->A: No effect on transport activity."
FT /evidence="ECO:0000269|PubMed:15862304"
FT CONFLICT 135
FT /note="N -> G (in Ref. 4; AAB05914)"
FT /evidence="ECO:0000305"
FT CONFLICT 177..178
FT /note="CA -> LR (in Ref. 4; AAB05914)"
FT /evidence="ECO:0000305"
FT CONFLICT 369..372
FT /note="VPFC -> RPIL (in Ref. 4; AAB05914)"
FT /evidence="ECO:0000305"
FT CONFLICT 393
FT /note="A -> P (in Ref. 4; AAB05914)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 441 AA; 48215 MW; 9CDA37D374184605 CRC64;
MSCCKVPVLI EAQVEMVSAN ELENKSLFRQ EEDATQTKEA SLMEQGSLST SFPQHTPKAP
KNSVLNSIKI VIFCNKLNLL LPFGPLAILV HYMIDSKGWV FLLTLVGITP LAERLGYATE
QLACYTGPTV GGLLNATFGN VTELIISIFA LKNGMIRVVQ LTLLGSILSN MLLVLGCAFF
CGGLVFYQKD QVFDKGIATV NSGLLLMAVM GILFPAVLHY THSEVHAGSS ELALSRFSSC
IMLIAYAAYL FFQLKSQSNS YSPLDEESNQ NEETSAEDED PEISKWEAII WLSILTAWVS
LLSGYLVDAI EGASVSWNIP IAFISTILLP IVGNAAEHAG AIMFAMKDKL DLSLGVAIGS
SIQISMFAVP FCVVIGWMMG QQMDLNFQLF ETAMLFITVI VVAFFLQEGS SNYFKGLMLI
LCYLIVAASF FVHEDPHQDG I
