ID ACA10_ARATH Reviewed; 1069 AA.
AC Q9SZR1; Q9M0D3;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 27-MAR-2024, entry version 197.
DE RecName: Full=Calcium-transporting ATPase 10, plasma membrane-type;
DE EC=7.2.2.10;
DE AltName: Full=Ca(2+)-ATPase isoform 10;
GN Name=ACA10; OrderedLocusNames=At4g29900; ORFNames=F27B13.140;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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).
RN [3]
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 [4]
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).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of
CC ATP coupled with the translocation of calcium from the cytosol into the
CC endoplasmic reticulum. {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB43665.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL050352; CAB43665.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161575; CAB79748.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85690.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66062.1; -; Genomic_DNA.
DR PIR; C85349; C85349.
DR PIR; T08551; T08551.
DR RefSeq; NP_001327988.1; NM_001341980.1.
DR RefSeq; NP_194719.1; NM_119136.4.
DR AlphaFoldDB; Q9SZR1; -.
DR SMR; Q9SZR1; -.
DR BioGRID; 14399; 4.
DR IntAct; Q9SZR1; 1.
DR STRING; 3702.Q9SZR1; -.
DR iPTMnet; Q9SZR1; -.
DR SwissPalm; Q9SZR1; -.
DR PaxDb; 3702-AT4G29900-1; -.
DR ProteomicsDB; 244346; -.
DR EnsemblPlants; AT4G29900.1; AT4G29900.1; AT4G29900.
DR EnsemblPlants; AT4G29900.2; AT4G29900.2; AT4G29900.
DR GeneID; 829112; -.
DR Gramene; AT4G29900.1; AT4G29900.1; AT4G29900.
DR Gramene; AT4G29900.2; AT4G29900.2; AT4G29900.
DR KEGG; ath:AT4G29900; -.
DR Araport; AT4G29900; -.
DR TAIR; AT4G29900; ACA10.
DR eggNOG; KOG0204; Eukaryota.
DR HOGENOM; CLU_002360_9_2_1; -.
DR InParanoid; Q9SZR1; -.
DR OMA; IAFRTFE; -.
DR OrthoDB; 847at2759; -.
DR PhylomeDB; Q9SZR1; -.
DR BioCyc; ARA:AT4G29900-MONOMER; -.
DR PRO; PR:Q9SZR1; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SZR1; baseline and differential.
DR Genevisible; Q9SZR1; AT.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; 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; ISS: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:SF529; CALCIUM-TRANSPORTING ATPASE 10, 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; PR00121; NAKATPASE.
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 Acetylation; ATP-binding; Calcium; Calcium transport; Calmodulin-binding;
KW Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..1069
FT /note="Calcium-transporting ATPase 10, plasma membrane-
FT type"
FT /id="PRO_0000046416"
FT TOPO_DOM 2..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="Lumenal"
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="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 427..444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 445..844
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 845..863
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 864..874
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 875..895
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 896..915
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 916..938
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 939..951
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 952..973
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 974..991
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 992..1013
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1014..1023
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1024..1045
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1046..1069
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 42..53
FT /note="Interaction with calmodulin"
FT /evidence="ECO:0000250"
FT ACT_SITE 482
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 789
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 793
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 1069 AA; 116858 MW; 48CE4A4B218E2656 CRC64;
MSGQFNNSPR GEDKDVEAGT SSFTEYEDSP FDIASTKNAP VERLRRWRQA ALVLNASRRF
RYTLDLKREE DKKQMLRKMR AHAQAIRAAH LFKAAASRVT GIASPLPTPG GGDFGIGQEQ
IVSISRDQNI GALQELGGVR GLSDLLKTNL EKGIHGDDDD ILKRKSAFGS NTYPQKKGRS
FWRFVWEASQ DLTLIILIVA AVASLALGIK TEGIEKGWYD GISIAFAVLL VIVVTATSDY
RQSLQFQNLN EEKRNIRLEV TRDGRRVEIS IYDIVVGDVI PLNIGDQVPA DGVLVAGHSL
AVDESSMTGE SKIVQKNSTK HPFLMSGCKV ADGNGTMLVT GVGVNTEWGL LMASVSEDNG
GETPLQVRLN GVATFIGIVG LTVAGVVLFV LVVRYFTGHT KNEQGGPQFI GGKTKFEHVL
DDLVEIFTVA VTIVVVAVPE GLPLAVTLTL AYSMRKMMAD KALVRRLSAC ETMGSATTIC
SDKTGTLTLN EMTVVECYAG LQKMDSPDSS SKLPSAFTSI LVEGIAHNTT GSVFRSESGE
IQVSGSPTER AILNWAIKLG MDFDALKSES SAVQFFPFNS EKKRGGVAVK SPDSSVHIHW
KGAAEIVLGS CTHYMDESES FVDMSEDKMG GLKDAIDDMA ARSLRCVAIA FRTFEADKIP
TDEEQLSRWE LPEDDLILLA IVGIKDPCRP GVKNSVLLCQ QAGVKVRMVT GDNIQTAKAI
ALECGILASD SDASEPNLIE GKVFRSYSEE ERDRICEEIS VMGRSSPNDK LLLVQSLKRR
GHVVAVTGDG TNDAPALHEA DIGLAMGIQG TEVAKEKSDI IILDDNFESV VKVVRWGRSV
YANIQKFIQF QLTVNVAALV INVVAAISAG EVPLTAVQLL WVNLIMDTLG ALALATEPPT
DHLMDRAPVG RREPLITNIM WRNLFIQAMY QVTVLLILNF RGISILHLKS KPNAERVKNT
VIFNAFVICQ VFNEFNARKP DEINIFRGVL RNHLFVGIIS ITIVLQVVIV EFLGTFASTT
KLDWEMWLVC IGIGSISWPL AVIGKLIPVP ETPVSQYFRI NRWRRNSSG
//
