ID   ACA8_ARATH              Reviewed;        1074 AA.
AC   Q9LF79; Q9LU75;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 196.
DE   RecName: Full=Calcium-transporting ATPase 8, plasma membrane-type;
DE            EC=7.2.2.10;
DE   AltName: Full=Ca(2+)-ATPase isoform 8;
GN   Name=ACA8; OrderedLocusNames=At5g57110; ORFNames=MUL3.5;
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], PARTIAL PROTEIN SEQUENCE, AND
RP   CALMODULIN-BINDING DOMAIN.
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=10938365; DOI=10.1104/pp.123.4.1495;
RA   Bonza M.C., Morandini P., Luoni L., Geisler M., Palmgren M.G.,
RA   De Michelis M.I.;
RT   "At-ACA8 encodes a plasma membrane-localized Ca2+-ATPase of Arabidopsis
RT   with a calmodulin-binding domain at the N-terminus.";
RL   Plant Physiol. 123:1495-1506(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT   features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:31-63(2000).
RN   [3]
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   [4]
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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA   Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT   "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT   phosphorylation site database.";
RL   Plant Cell 16:2394-2405(2004).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Seedling;
RX   PubMed=17586839; DOI=10.1074/mcp.m700164-mcp200;
RA   Niittylae T., Fuglsang A.T., Palmgren M.G., Frommer W.B., Schulze W.X.;
RT   "Temporal analysis of sucrose-induced phosphorylation changes in plasma
RT   membrane proteins of Arabidopsis.";
RL   Mol. Cell. Proteomics 6:1711-1726(2007).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=cv. Columbia;
RX   PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA   Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA   Rathjen J.P., Peck S.C.;
RT   "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT   thaliana.";
RL   J. Proteomics 72:439-451(2009).
RN   [8]
RP   IDENTIFICATION BY 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 out of
CC       the cell.
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   -!- INTERACTION:
CC       Q9LF79; P62157: CALM; Xeno; NbExp=14; IntAct=EBI-980643, EBI-397403;
CC   -!- SUBCELLULAR LOCATION: Cell 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   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IIB subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA97361.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AJ249352; CAB96189.1; -; mRNA.
DR   EMBL; AB023042; BAA97361.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED96847.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED96848.1; -; Genomic_DNA.
DR   EMBL; CP002688; ANM69618.1; -; Genomic_DNA.
DR   EMBL; AY069869; AAL47426.1; -; mRNA.
DR   PIR; T52654; T52654.
DR   RefSeq; NP_001331281.1; NM_001345242.1.
DR   RefSeq; NP_200521.3; NM_125093.6.
DR   RefSeq; NP_851200.1; NM_180869.3.
DR   PDB; 2M73; NMR; -; A=43-67.
DR   PDB; 4AQR; X-ray; 1.95 A; D=40-95.
DR   PDBsum; 2M73; -.
DR   PDBsum; 4AQR; -.
DR   AlphaFoldDB; Q9LF79; -.
DR   BMRB; Q9LF79; -.
DR   SASBDB; Q9LF79; -.
DR   SMR; Q9LF79; -.
DR   BioGRID; 21059; 4.
DR   IntAct; Q9LF79; 1.
DR   STRING; 3702.Q9LF79; -.
DR   TCDB; 3.A.3.2.10; the p-type atpase (p-atpase) superfamily.
DR   iPTMnet; Q9LF79; -.
DR   SwissPalm; Q9LF79; -.
DR   PaxDb; 3702-AT5G57110-2; -.
DR   ProteomicsDB; 244372; -.
DR   EnsemblPlants; AT5G57110.1; AT5G57110.1; AT5G57110.
DR   EnsemblPlants; AT5G57110.2; AT5G57110.2; AT5G57110.
DR   EnsemblPlants; AT5G57110.3; AT5G57110.3; AT5G57110.
DR   GeneID; 835815; -.
DR   Gramene; AT5G57110.1; AT5G57110.1; AT5G57110.
DR   Gramene; AT5G57110.2; AT5G57110.2; AT5G57110.
DR   Gramene; AT5G57110.3; AT5G57110.3; AT5G57110.
DR   KEGG; ath:AT5G57110; -.
DR   Araport; AT5G57110; -.
DR   TAIR; AT5G57110; ACA8.
DR   eggNOG; KOG0204; Eukaryota.
DR   HOGENOM; CLU_002360_9_2_1; -.
DR   InParanoid; Q9LF79; -.
DR   OMA; MINVHDI; -.
DR   OrthoDB; 847at2759; -.
DR   PhylomeDB; Q9LF79; -.
DR   BioCyc; ARA:AT5G57110-MONOMER; -.
DR   BRENDA; 7.2.2.10; 399.
DR   PRO; PR:Q9LF79; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LF79; baseline and differential.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR   GO; GO:0009536; C:plastid; 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; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005388; F:P-type calcium transporter activity; IDA:TAIR.
DR   GO; GO:0043621; F:protein self-association; IDA: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; 2.
DR   PANTHER; PTHR24093:SF439; CALCIUM-TRANSPORTING ATPASE 8, 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   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; Q9LF79; AT.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Calcium; Calcium transport; Calmodulin-binding;
KW   Cell membrane; Direct protein sequencing; Ion transport; Magnesium;
KW   Membrane; Metal-binding; Nucleotide-binding; Reference proteome;
KW   Translocase; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..1074
FT                   /note="Calcium-transporting ATPase 8, plasma membrane-type"
FT                   /id="PRO_0000046414"
FT   TOPO_DOM        1..180
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        181..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        202..219
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        220..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        241..369
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        370..389
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        390..426
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        427..444
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        445..840
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        841..859
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        860..870
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        871..891
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        892..911
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        912..934
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        935..949
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        950..971
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        972..989
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        990..1011
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1012..1021
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1022..1043
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1044..1074
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          43..54
FT                   /note="Interaction with calmodulin"
FT   COMPBIAS        11..30
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        482
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         785
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         789
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   HELIX           40..94
FT                   /evidence="ECO:0007829|PDB:4AQR"
SQ   SEQUENCE   1074 AA;  116174 MW;  2E86572F44DEA8A5 CRC64;
     MTSLLKSSPG RRRGGDVESG KSEHADSDSD TFYIPSKNAS IERLQQWRKA ALVLNASRRF
     RYTLDLKKEQ ETREMRQKIR SHAHALLAAN RFMDMGRESG VEKTTGPATP AGDFGITPEQ
     LVIMSKDHNS GALEQYGGTQ GLANLLKTNP EKGISGDDDD LLKRKTIYGS NTYPRKKGKG
     FLRFLWDACH DLTLIILMVA AVASLALGIK TEGIKEGWYD GGSIAFAVIL VIVVTAVSDY
     KQSLQFQNLN DEKRNIHLEV LRGGRRVEIS IYDIVVGDVI PLNIGNQVPA DGVLISGHSL
     ALDESSMTGE SKIVNKDANK DPFLMSGCKV ADGNGSMLVT GVGVNTEWGL LMASISEDNG
     EETPLQVRLN GVATFIGSIG LAVAAAVLVI LLTRYFTGHT KDNNGGPQFV KGKTKVGHVI
     DDVVKVLTVA VTIVVVAVPE GLPLAVTLTL AYSMRKMMAD KALVRRLSAC ETMGSATTIC
     SDKTGTLTLN QMTVVESYAG GKKTDTEQLP ATITSLVVEG ISQNTTGSIF VPEGGGDLEY
     SGSPTEKAIL GWGVKLGMNF ETARSQSSIL HAFPFNSEKK RGGVAVKTAD GEVHVHWKGA
     SEIVLASCRS YIDEDGNVAP MTDDKASFFK NGINDMAGRT LRCVALAFRT YEAEKVPTGE
     ELSKWVLPED DLILLAIVGI KDPCRPGVKD SVVLCQNAGV KVRMVTGDNV QTARAIALEC
     GILSSDADLS EPTLIEGKSF REMTDAERDK ISDKISVMGR SSPNDKLLLV QSLRRQGHVV
     AVTGDGTNDA PALHEADIGL AMGIAGTEVA KESSDIIILD DNFASVVKVV RWGRSVYANI
     QKFIQFQLTV NVAALVINVV AAISSGDVPL TAVQLLWVNL IMDTLGALAL ATEPPTDHLM
     GRPPVGRKEP LITNIMWRNL LIQAIYQVSV LLTLNFRGIS ILGLEHEVHE HATRVKNTII
     FNAFVLCQAF NEFNARKPDE KNIFKGVIKN RLFMGIIVIT LVLQVIIVEF LGKFASTTKL
     NWKQWLICVG IGVISWPLAL VGKFIPVPAA PISNKLKVLK FWGKKKNSSG EGSL
//