ID   ACA7_ARATH              Reviewed;        1015 AA.
AC   O64806;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 2.
DT   27-MAR-2024, entry version 194.
DE   RecName: Full=Putative calcium-transporting ATPase 7, plasma membrane-type;
DE            EC=7.2.2.10;
DE   AltName: Full=Ca(2+)-ATPase isoform 7;
GN   Name=ACA7; OrderedLocusNames=At2g22950; ORFNames=T20K9.16;
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=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   [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).
CC   -!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of
CC       ATP coupled with the translocation of calcium from the cytosol out of
CC       the cell or into organelles. {ECO:0000250}.
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- DOMAIN: The N-terminus contains an autoinhibitory calmodulin-binding
CC       domain, which binds calmodulin in a calcium-dependent fashion.
CC       {ECO:0000250}.
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; AC004401; AAF18608.2; -; Genomic_DNA.
DR   EMBL; AC004786; AAM15005.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC07380.1; -; Genomic_DNA.
DR   PIR; H84618; H84618.
DR   RefSeq; NP_179879.1; NM_127860.2.
DR   AlphaFoldDB; O64806; -.
DR   SMR; O64806; -.
DR   BioGRID; 2179; 1.
DR   STRING; 3702.O64806; -.
DR   iPTMnet; O64806; -.
DR   PaxDb; 3702-AT2G22950-1; -.
DR   ProteomicsDB; 244379; -.
DR   EnsemblPlants; AT2G22950.1; AT2G22950.1; AT2G22950.
DR   GeneID; 816826; -.
DR   Gramene; AT2G22950.1; AT2G22950.1; AT2G22950.
DR   KEGG; ath:AT2G22950; -.
DR   Araport; AT2G22950; -.
DR   TAIR; AT2G22950; ACA7.
DR   eggNOG; KOG0204; Eukaryota.
DR   HOGENOM; CLU_002360_9_2_1; -.
DR   InParanoid; O64806; -.
DR   OMA; QWGYSIV; -.
DR   OrthoDB; 847at2759; -.
DR   PhylomeDB; O64806; -.
DR   BioCyc; ARA:AT2G22950-MONOMER; -.
DR   PRO; PR:O64806; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O64806; baseline and differential.
DR   GO; GO:0005886; C:plasma membrane; IDA: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; IEA:UniProtKB-KW.
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:0009555; P:pollen development; IMP: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; 2.
DR   PANTHER; PTHR24093:SF444; CALCIUM-TRANSPORTING ATPASE 7, PLASMA MEMBRANE-TYPE-RELATED; 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   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; O64806; AT.
PE   3: Inferred from homology;
KW   Acetylation; ATP-binding; Calcium; Calcium transport; Calmodulin-binding;
KW   Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..1015
FT                   /note="Putative calcium-transporting ATPase 7, plasma
FT                   membrane-type"
FT                   /id="PRO_0000046413"
FT   TOPO_DOM        1..161
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        162..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        183..200
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        201..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        222..349
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        350..369
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        370..399
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        400..417
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        418..811
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        812..830
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        831..841
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        842..862
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        863..882
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        883..905
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        906..917
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        918..939
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        940..957
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        958..979
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        980..989
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        990..1011
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1012..1015
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          20..31
FT                   /note="Interaction with calmodulin"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        455
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         756
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         760
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:O81108"
FT   MOD_RES         45
FT                   /note="Phosphoserine; by CPK"
FT                   /evidence="ECO:0000250|UniProtKB:O81108"
SQ   SEQUENCE   1015 AA;  110773 MW;  57DEE2028316CFC0 CRC64;
     MESYLNSNFD VKAKHSSEEV LEKWRNLCSV VKNPKRRFRF TANLSKRYEA AAMRRTNQEK
     LRIAVLVSKA AFQFISGVSP SDYKVPEEVK AAGFDICADE LGSIVEGHDV KKLKFHGGVD
     GLSGKLKACP NAGLSTGEPE QLSKRQELFG INKFAESELR SFWVFVWEAL QDMTLMILGV
     CAFVSLIVGI ATEGWPQGSH DGLGIVASIL LVVFVTATSD YRQSLQFRDL DKEKKKITVQ
     VTRNGFRQKM SIYDLLPGDV VHLAIGDQVP ADGLFLSGFS VVIDESSLTG ESEPVMVTAQ
     NPFLLSGTKV QDGSCKMLVT TVGMRTQWGK LMATLSEGGD DETPLQVKLN GVATIIGKIG
     LSFAIVTFAV LVQGMFMRKL SLGPHWWWSG DDALELLEYF AIAVTIVVVA VPEGLPLAVT
     LSLAFAMKKM MNDKALVRHL AACETMGSAT TICSDKTGTL TTNHMTVVKS CICMNVQDVA
     SKSSSLQSDI PEAALKLLLQ LIFNNTGGEV VVNERGKTEI LGTPTETAIL ELGLSLGGKF
     QEERQSNKVI KVEPFNSTKK RMGVVIELPE GGRIRAHTKG ASEIVLAACD KVINSSGEVV
     PLDDESIKFL NVTIDEFANE ALRTLCLAYM DIESGFSADE GIPEKGFTCI GIVGIKDPVR
     PGVRESVELC RRAGIMVRMV TGDNINTAKA IARECGILTD DGIAIEGPVF REKNQEEMLE
     LIPKIQVMAR SSPMDKHTLV KQLRTTFDEV VAVTGDGTND APALHEADIG LAMGIAGTEV
     AKEIADVIIL DDNFSTIVTV AKWGRSVYIN IQKFVQFQLT VNVVALIVNF SSACLTGSAP
     LTAVQLLWVN MIMDTLGALA LATEPPNNEL MKRMPVGRRG NFITNAMWRN ILGQAVYQFI
     IIWILQAKGK SMFGLVGSDS TLVLNTLIFN CFVFCQVFNE VSSREMEEID VFKGILDNYV
     FVVVIGATVF FQIIIIEFLG TFASTTPLTI VQWFFSIFVG FLGMPIAAGL KKIPV
//