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 Genevisible; O22218; AT.
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.
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
//
