CAX5_ARATH
ID CAX5_ARATH Reviewed; 441 AA.
AC Q8L783; Q9LFZ7;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Vacuolar cation/proton exchanger 5;
DE AltName: Full=Ca(2+)/H(+) antiporter CAX5;
DE AltName: Full=Ca(2+)/H(+) exchanger 5;
DE AltName: Full=Protein CATION EXCHANGER 5;
GN Name=CAX5; OrderedLocusNames=At1g55730;
GN ORFNames=F20N2.14, F20N2.16, F20N2.30;
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=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).
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). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}. Vacuole membrane {ECO:0000305}; Lipid-
CC anchor {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=AAF79504.1; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 2 genes: At1g55730 and At1g55740.; Evidence={ECO:0000305};
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DR EMBL; AC002328; AAF79504.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33290.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33291.1; -; Genomic_DNA.
DR EMBL; AY136416; AAM97082.1; -; mRNA.
DR EMBL; BT006591; AAP31935.1; -; mRNA.
DR PIR; C96599; C96599.
DR RefSeq; NP_001031196.1; NM_001036119.2.
DR RefSeq; NP_175969.2; NM_104449.3.
DR AlphaFoldDB; Q8L783; -.
DR SMR; Q8L783; -.
DR BioGRID; 27247; 1.
DR STRING; 3702.AT1G55730.1; -.
DR CAZy; GH36; Glycoside Hydrolase Family 36.
DR iPTMnet; Q8L783; -.
DR PaxDb; Q8L783; -.
DR PRIDE; Q8L783; -.
DR ProteomicsDB; 223953; -.
DR EnsemblPlants; AT1G55730.1; AT1G55730.1; AT1G55730.
DR EnsemblPlants; AT1G55730.2; AT1G55730.2; AT1G55730.
DR GeneID; 842022; -.
DR Gramene; AT1G55730.1; AT1G55730.1; AT1G55730.
DR Gramene; AT1G55730.2; AT1G55730.2; AT1G55730.
DR KEGG; ath:AT1G55730; -.
DR Araport; AT1G55730; -.
DR TAIR; locus:2020462; AT1G55730.
DR eggNOG; KOG1397; Eukaryota.
DR HOGENOM; CLU_008721_2_1_1; -.
DR OMA; VWHISET; -.
DR OrthoDB; 727723at2759; -.
DR PhylomeDB; Q8L783; -.
DR PRO; PR:Q8L783; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8L783; baseline and differential.
DR Genevisible; Q8L783; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009705; C:plant-type vacuole membrane; IBA:GO_Central.
DR GO; GO:0015369; F:calcium:proton antiporter activity; IBA:GO_Central.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Antiport; Calcium; Calcium transport; Ion transport; Lipoprotein; Membrane;
KW Myristate; Palmitate; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Vacuole.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..441
FT /note="Vacuolar cation/proton exchanger 5"
FT /id="PRO_0000270154"
FT TOPO_DOM 2..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..165
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 187..197
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 219..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 LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 4
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 441 AA; 48096 MW; C0319778C9C6476F CRC64;
MGCCKVPALI QAQVEMGLVN DVEHKSLFRR DTDSPERKAA SLMEQGSLSA SFRECSTKTP
NNSVLQSFKI VILSNKLNLL LPFGPLAILL HYLTDNKGWI FLLSLVGITP LAERLGYATE
QLACYTGSTV GGLLNATFGN VTELIISIFA LKSGMIRVVQ LTLLGSILSN MLLVLGCAFF
CGGLVFSQKE QVFDKGNAVV NSGLLLMAVM GLLFPAVLHY THSEVHAGSS ELALSRFSSC
IMLVAYAAYL FFQLKSQPSS YTPLTEETNQ NEETSDDDED PEISKWEAII WLSILTAWVS
LLSGYLVDAI EGASVSWKIP ISFISVILLP IVGNAAEHAG AIMFAMKDKL DLSLGVAIGS
SIQISMFAVP FCVVIGWMMG AQMDLNFQLF ETATLFITVI VVAFFLQEGT SNYFKGLMLI
LCYLIVAASF FVHEDPHQDD I
