ACA10_ORYSJ
ID ACA10_ORYSJ Reviewed; 1020 AA.
AC Q2QMX9; A0A0P0YBR1; Q0IM87;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Calcium-transporting ATPase 10, plasma membrane-type {ECO:0000305};
DE Short=OsACA10 {ECO:0000303|PubMed:24286292};
DE EC=7.2.2.10;
DE AltName: Full=Ca(2+)-ATPase isoform 10 {ECO:0000305};
DE AltName: Full=Plastid envelope ATPase 1 {ECO:0000305};
GN Name=ACA10 {ECO:0000303|PubMed:24286292};
GN OrderedLocusNames=Os12g0586600, LOC_Os12g39660; ORFNames=OsJ_36685;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG The rice chromosomes 11 and 12 sequencing consortia;
RT "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT genes and recent gene duplications.";
RL BMC Biol. 3:20-20(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=24286292; DOI=10.1111/febs.12656;
RA Singh A., Kanwar P., Yadav A.K., Mishra M., Jha S.K., Baranwal V.,
RA Pandey A., Kapoor S., Tyagi A.K., Pandey G.K.;
RT "Genome-wide expressional and functional analysis of calcium transport
RT elements during abiotic stress and development in rice.";
RL FEBS J. 281:894-915(2014).
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, into the endoplasmic reticulum, or into organelles.
CC {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 {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
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; DP000011; ABA99736.1; -; Genomic_DNA.
DR EMBL; AP008218; BAF30178.1; -; Genomic_DNA.
DR EMBL; AP014968; BAT17855.1; -; Genomic_DNA.
DR EMBL; CM000149; EAZ21038.1; -; Genomic_DNA.
DR EMBL; AK066259; BAG89887.1; -; mRNA.
DR RefSeq; XP_015620081.1; XM_015764595.1.
DR AlphaFoldDB; Q2QMX9; -.
DR SMR; Q2QMX9; -.
DR STRING; 4530.OS12T0586600-01; -.
DR PaxDb; Q2QMX9; -.
DR PRIDE; Q2QMX9; -.
DR EnsemblPlants; Os12t0586600-01; Os12t0586600-01; Os12g0586600.
DR GeneID; 4352664; -.
DR Gramene; Os12t0586600-01; Os12t0586600-01; Os12g0586600.
DR KEGG; osa:4352664; -.
DR eggNOG; KOG0204; Eukaryota.
DR InParanoid; Q2QMX9; -.
DR OMA; SKKYHEG; -.
DR OrthoDB; 115892at2759; -.
DR Proteomes; UP000000763; Chromosome 12.
DR Proteomes; UP000007752; Chromosome 12.
DR Proteomes; UP000059680; Chromosome 12.
DR ExpressionAtlas; Q2QMX9; baseline and differential.
DR Genevisible; Q2QMX9; OS.
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: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; IBA:GO_Central.
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; 3.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 2: Evidence at transcript 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.
FT CHAIN 1..1020
FT /note="Calcium-transporting ATPase 10, plasma membrane-
FT type"
FT /id="PRO_0000247300"
FT TOPO_DOM 1..175
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 220..263
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 373..400
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 401..421
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 843..863
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 864..887
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 888..907
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 924..944
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 945..961
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 962..982
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 995..1015
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1016..1020
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 21..32
FT /note="Interaction with calmodulin"
FT /evidence="ECO:0000250"
FT ACT_SITE 456
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 758
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 762
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1020 AA; 111151 MW; B340D8999927D4F5 CRC64;
MESYLEENFG GVKAKNSSEE ALRRWRKLCG VVKNPKRRFR FTANLDKRGE AQAIKHANHE
KLRVAVLVSK AALQFIQGLS LRSEYVVPEE VKAAGFQICA DELGSIVEGH DSKKLITHGG
VTGIADKLAT SPADGLSTAE ESIKRRQDVY GLNKFTESEV RSFWVFVWEA LQDTTLIILA
VCAFVSLVVG IAMEGWPKGA HDGLGIVASI LLVVFVTATS DYRQSLQFKD LDKEKKKIQV
QVTRNGFRQR LSIYDLLPGD VVHLAIGDQV PADGLFISGF SLLINESSLT GESEPVVVNE
DNPFLLSGTK VQDGSCKMLI TTVGMRTQWG KLMATLSEGG DDETPLQVKL NGVATIIGKI
GLFFAVITFI VLSQGLISKK YHEGLLLSWS GDDALEMLEH FAIAVTIVVV AVPEGLPLAV
TLSLAFAMKK MMNDKALVRH LAACETMGSA TTICSDKTGT LTTNHMTVVK ACICGNIKEV
NNPKNASDLC SELPETVVKT LLESIFNNTG GEVVIDQDGK YQILGTPTET ALLEFALSLG
GNFKAKRDET KIVKMEPFNS TKKRMCVVLK LPGGGCRAHC KGASEIVLAA CDKFMDETGA
VVPLDKTTAD KLNGIIESFA NEALRTLCLG YREMEEGFSV EEQIPLQGYT CIGIVGIKDP
VRPGVRESVA TCRSAGIMVR MVTGDNINTA KAIARECGIL TEDGLAIEGP EFREKSLDEL
LKLIPKIQVM ARSSPLDKHT LVKHLRTTFN EVVAVTGDGT NDAPALHEAD IGLAMGIAGT
EVAKESADVI ILDDNFSTIV TVAKWGRSVY VNIQKFVQFQ LTVNVVALLV NFSSACFTGN
APLTAVQLLW VNMIMDTLGA LALATEPPND DLMKREPVGR TGKFITNVMW RNILGQSFYQ
FIVMWYLQTQ GKSMFGLDGP DAEVVLNTII FNSFVFCQVF NEISSREMEK INVLRGILKN
YVFLGVLTST VVFQFIMVQF LGEFANTIPL TRLQWIASVL LGLIGMPISA IIKLLPVGSS
