ID   ACA4_ARATH              Reviewed;        1030 AA.
AC   O22218;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   24-JAN-2024, entry version 192.
DE   RecName: Full=Calcium-transporting ATPase 4, plasma membrane-type;
DE            EC=7.2.2.10;
DE   AltName: Full=Ca(2+)-ATPase isoform 4;
GN   Name=ACA4; OrderedLocusNames=At2g41560; ORFNames=T32G6.8;
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], AND SUBCELLULAR LOCATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=11115896; DOI=10.1104/pp.124.4.1814;
RA   Geisler M., Frangne N., Gomes E., Martinoia E., Palmgren M.G.;
RT   "The ACA4 gene of Arabidopsis encodes a vacuolar membrane calcium pump that
RT   improves salt tolerance in yeast.";
RL   Plant Physiol. 124:1814-1827(2000).
RN   [2]
RP   ERRATUM OF PUBMED:11115896.
RA   Geisler M., Frangne N., Gomes E., Martinoia E., Palmgren M.G.;
RL   Plant Physiol. 126:1341-1342(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [4]
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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=17151019; DOI=10.1074/mcp.m600250-mcp200;
RA   Jaquinod M., Villiers F., Kieffer-Jaquinod S., Hugouvieux V., Bruley C.,
RA   Garin J., Bourguignon J.;
RT   "A proteomics dissection of Arabidopsis thaliana vacuoles isolated from
RT   cell culture.";
RL   Mol. Cell. Proteomics 6:394-412(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
CC   -!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of
CC       ATP coupled with the translocation of calcium from the cytosol into
CC       small vacuoles.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate;
CC         Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; EC=7.2.2.10;
CC   -!- ACTIVITY REGULATION: Activated by calmodulin.
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:11115896,
CC       ECO:0000269|PubMed:17151019}; Multi-pass membrane protein
CC       {ECO:0000255}. Note=Tonoplast. Small vacuoles.
CC       {ECO:0000269|PubMed:11115896}.
CC   -!- DOMAIN: The N-terminus contains an autoinhibitory calmodulin-binding
CC       domain, which binds calmodulin in a calcium-dependent fashion.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IIB subfamily. {ECO:0000305}.
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DR   EMBL; AF200739; AAG35585.1; -; mRNA.
DR   EMBL; AC002510; AAB84338.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC10000.1; -; Genomic_DNA.
DR   PIR; T00812; T00812.
DR   RefSeq; NP_181687.1; NM_129719.4.
DR   AlphaFoldDB; O22218; -.
DR   SMR; O22218; -.
DR   BioGRID; 4091; 1.
DR   STRING; 3702.O22218; -.
DR   iPTMnet; O22218; -.
DR   PaxDb; 3702-AT2G41560-1; -.
DR   ProteomicsDB; 244534; -.
DR   EnsemblPlants; AT2G41560.1; AT2G41560.1; AT2G41560.
DR   GeneID; 818754; -.
DR   Gramene; AT2G41560.1; AT2G41560.1; AT2G41560.
DR   KEGG; ath:AT2G41560; -.
DR   Araport; AT2G41560; -.
DR   TAIR; AT2G41560; ACA4.
DR   eggNOG; KOG0204; Eukaryota.
DR   HOGENOM; CLU_002360_9_0_1; -.
DR   InParanoid; O22218; -.
DR   OrthoDB; 847at2759; -.
DR   PhylomeDB; O22218; -.
DR   BioCyc; ARA:AT2G41560-MONOMER; -.
DR   PRO; PR:O22218; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O22218; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0000325; C:plant-type vacuole; IDA:TAIR.
DR   GO; GO:0009705; C:plant-type vacuole membrane; IDA:TAIR.
DR   GO; GO:0005774; C:vacuolar membrane; HDA:TAIR.
DR   GO; GO:0005773; C:vacuole; HDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0005516; F:calmodulin binding; IDA:TAIR.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005388; F:P-type calcium transporter activity; ISS:TAIR.
DR   GO; GO:0042742; P:defense response to bacterium; IGI:TAIR.
DR   GO; GO:0055081; P:monoatomic anion homeostasis; IMP:TAIR.
DR   GO; GO:0043069; P:negative regulation of programmed cell death; IGI:TAIR.
DR   GO; GO:0009624; P:response to nematode; HEP:TAIR.
DR   CDD; cd02081; P-type_ATPase_Ca_PMCA-like; 1.
DR   Gene3D; 1.20.5.170; -; 1.
DR   Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR   Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR   Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR   InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR   InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR   InterPro; IPR024750; Ca_ATPase_N_dom.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR006408; P-type_ATPase_IIB.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01517; ATPase-IIB_Ca; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 3.
DR   PANTHER; PTHR24093:SF438; CALCIUM-TRANSPORTING ATPASE 4, PLASMA MEMBRANE-TYPE; 1.
DR   PANTHER; PTHR24093; CATION TRANSPORTING ATPASE; 1.
DR   Pfam; PF12515; CaATP_NAI; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF00689; Cation_ATPase_C; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00120; HATPASE.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SMART; SM00831; Cation_ATPase_N; 1.
DR   SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR   SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   Genevisible; O22218; AT.
PE   1: Evidence at protein level;
KW   ATP-binding; Calcium; Calcium transport; Calmodulin-binding; Ion transport;
KW   Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW   Transport; Vacuole.
FT   CHAIN           1..1030
FT                   /note="Calcium-transporting ATPase 4, plasma membrane-type"
FT                   /id="PRO_0000046412"
FT   TOPO_DOM        1..157
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        158..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        179..196
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        197..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        218..345
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        346..365
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        366..395
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        396..413
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        414..804
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        805..823
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        824..834
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        835..855
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        856..875
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        876..898
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        899..910
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        911..932
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        933..950
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        951..972
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        973..982
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        983..1004
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1005..1030
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          19..30
FT                   /note="Interaction with calmodulin"
FT   ACT_SITE        451
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         749
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         753
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         28
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19376835"
SQ   SEQUENCE   1030 AA;  112749 MW;  BD31D923E6AE2D13 CRC64;
     MSNLLRDFEV EAKNPSLEAR QRWRSSVSIV KNRTRRFRNI RDLDKLADYE NKKHQIQEKI
     RVAFFVQKAA LHFIDAAARP EYKLTDEVKK AGFSIEADEL ASMVRKNDTK SLAQKGGVEE
     LAKKVSVSLS EGIRSSEVPI REKIFGENRY TEKPARSFLM FVWEALHDIT LIILMVCAVV
     SIGVGVATEG FPRGMYDGTG ILLSILLVVM VTAISDYKQS LQFRDLDREK KKIIVQVTRD
     GSRQEISIHD LVVGDVVHLS IGDQVPADGI FISGYNLEID ESSLSGESEP SHVNKEKPFL
     LSGTKVQNGS AKMLVTTVGM RTEWGKLMET LVDGGEDETP LQVKLNGVAT IIGKIGLSFA
     VLTFVVLCIR FVLDKATSGS FTNWSSEDAL TLLDYFAISV TIIVVAVPEG LPLAVTLSLA
     FAMKKLMSDR ALVRHLAACE TMGSSTCICT DKTGTLTTNH MVVNKVWICD KVQERQEGSK
     ESFELELSEE VQSTLLQGIF QNTGSEVVKD KDGNTQILGS PTERAILEFG LLLGGDFNTQ
     RKEHKILKIE PFNSDKKKMS VLIALPGGGA RAFCKGASEI VLKMCENVVD SNGESVPLTE
     ERITSISDII EGFASEALRT LCLVYKDLDE APSGELPDGG YTMVAVVGIK DPVRPGVREA
     VQTCQAAGIT VRMVTGDNIS TAKAIAKECG IYTEGGLAIE GSEFRDLSPH EMRAIIPKIQ
     VMARSLPLDK HTLVSNLRKI GEVVAVTGDG TNDAPALHEA DIGLAMGIAG TEVAKENADV
     IIMDDNFKTI VNVARWGRAV YINIQKFVQF QLTVNVVALI INFVSACITG SAPLTAVQLL
     WVNMIMDTLG ALALATEPPN EGLMKRAPIA RTASFITKTM WRNIAGQSVY QLIVLGILNF
     AGKSLLKLDG PDSTAVLNTV IFNSFVFCQV FNEINSREIE KINVFKGMFN SWVFTWVMTV
     TVVFQVIIVE FLGAFASTVP LSWQHWLLSI LIGSLNMIVA VILKCVPVES RHHHDGYDLL
     PSGPSSSNSA
//