ACA8_ARATH
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 03-AUG-2022, entry version 188.
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.AT5G57110.2; -.
DR TCDB; 3.A.3.2.10; the p-type atpase (p-atpase) superfamily.
DR iPTMnet; Q9LF79; -.
DR SwissPalm; Q9LF79; -.
DR PaxDb; Q9LF79; -.
DR PRIDE; Q9LF79; -.
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; locus:2175579; AT5G57110.
DR eggNOG; KOG0204; Eukaryota.
DR HOGENOM; CLU_002360_9_2_1; -.
DR InParanoid; Q9LF79; -.
DR OMA; GMVYKDF; -.
DR OrthoDB; 115892at2759; -.
DR PhylomeDB; Q9LF79; -.
DR BioCyc; ARA:AT5G57110-MON; -.
DR BRENDA; 7.2.2.10; 399.
DR PRO; PR:Q9LF79; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LF79; baseline and differential.
DR Genevisible; Q9LF79; AT.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
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:0019829; F:ATPase-coupled cation transmembrane transporter activity; IBA:GO_Central.
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 Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 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 Pfam; PF12515; CaATP_NAI; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01517; ATPase-IIB_Ca; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
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
