ID   ACA9_ORYSJ              Reviewed;        1039 AA.
AC   Q2QY12; A0A0P0Y711; Q0IQ91;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Probable calcium-transporting ATPase 9, plasma membrane-type {ECO:0000305};
DE            Short=OsACA9 {ECO:0000303|PubMed:24286292};
DE            EC=7.2.2.10;
DE   AltName: Full=Ca(2+)-ATPase isoform 9 {ECO:0000305};
GN   Name=ACA9 {ECO:0000303|PubMed:24286292};
GN   OrderedLocusNames=Os12g0136900 {ECO:0000312|EMBL:BAF29124.1},
GN   LOC_Os12g04220 {ECO:0000312|EMBL:ABA95758.1};
GN   ORFNames=OsJ_35157 {ECO:0000312|EMBL:EAZ19580.1};
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   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; BX000502; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DP000011; ABA95758.1; -; Genomic_DNA.
DR   EMBL; AP008218; BAF29124.1; -; Genomic_DNA.
DR   EMBL; AP014968; BAT15803.1; -; Genomic_DNA.
DR   EMBL; CM000149; EAZ19580.1; -; Genomic_DNA.
DR   RefSeq; XP_015620481.1; XM_015764995.1.
DR   AlphaFoldDB; Q2QY12; -.
DR   SMR; Q2QY12; -.
DR   STRING; 4530.OS12T0136900-00; -.
DR   PaxDb; Q2QY12; -.
DR   PRIDE; Q2QY12; -.
DR   EnsemblPlants; Os12t0136900-00; Os12t0136900-00; Os12g0136900.
DR   GeneID; 4351449; -.
DR   Gramene; Os12t0136900-00; Os12t0136900-00; Os12g0136900.
DR   KEGG; osa:4351449; -.
DR   eggNOG; KOG0204; Eukaryota.
DR   HOGENOM; CLU_002360_9_2_1; -.
DR   InParanoid; Q2QY12; -.
DR   OMA; KTAHVGF; -.
DR   OrthoDB; 115892at2759; -.
DR   Proteomes; UP000000763; Chromosome 12.
DR   Proteomes; UP000007752; Chromosome 12.
DR   Proteomes; UP000059680; Chromosome 12.
DR   Genevisible; Q2QY12; 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; 2.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   3: Inferred from homology;
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..1039
FT                   /note="Probable calcium-transporting ATPase 9, plasma
FT                   membrane-type"
FT                   /id="PRO_0000247303"
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..250
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        251..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        353..373
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        374..406
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        407..427
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        825..845
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        846..847
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        848..868
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        892..912
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        913..960
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        961..981
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        995..1015
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1016..1039
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
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   1039 AA;  113842 MW;  63E8DAEB9A6729B1 CRC64;
     MEKLDRYLQE NFDVPAKNPS EEAQRRWRQA VGTIVKNRRR RFRWVPDLER RSLDKAKVRS
     TQEKIRVALY VQQAALIFSD GAKKKEYKLT GDIIKAGYAI NPDELALITS KHDSKALKMH
     GGVDGISIKV RSSFDHGIYA SELDTRQNIY GVNRYAEKPS RSFWMFVWDA LQDMTLIILM
     VCALLSVAVG LATEGWPKGM YDGLGIILSI FLVVMVTAVS DYKQSLQFKE LDNEKKKIFI
     HVTRDGRRQK ISIYDLVVGD IVHLSIGDQV PADGLYIHGY SLLIDESSLS GESDPVYVSQ
     DKPFILAGTK VQDGSAKMIV TAVGMRTEWG KLMSTLSEGG EDETPLQVKL NGVATIIGKI
     GLVFAILTFL VLLVRFLIDK GMTVGLLKWY STDALTIVNY FATAVTIIVV AVPEGLPLAV
     TLSLAFAMKK LMNDKALVRH LSACETMGSA GTICTDKTGT LTTNHMVVDK IWISEVSKSV
     TSNTISGELN SVVSSSTLSL LLQGIFENTS AEVVKEKDGK QTVLGTPTER AILEFGLGLK
     GDHDAEYRAC TKVKVEPFNS VKKKMAVLIS LPNGTSRWFC KGASEIILQM CDMMVDGDGN
     AIPLSEAQRK NILDTINSFA SDALRTLCLA YKEVDDDIDD NADSPTSGFT LIAIFGIKDP
     VRPGVKDAVK TCMSAGITVR MVTGDNINTA KAIAKECGIL TEDGVAIEGP EFHSKSTEEM
     RDLILNIQVM ARSLPLDKHT LVTNLRGMFD EVVSVTGDGT NDAPALHEAD IGLAMGIAGT
     EVAKESADVI VLDDNFTTII NVARWGRAVY INIQKFVQFQ LTVNIVALVI NFVSACIIGS
     APLTAVQLLW VNMIMDTLGA LALATEPPND EMMKRPPVRK GESFITKFMW RNIMGQSLYQ
     LFVLGALMFG GERLLNIKGA DSKSIINTLI FNSFVFCQVF NEINSREMQK INVFRGIISN
     WIFIAVIAAT VAFQVVIIEF LGTFASTVPL NWQHWLLSVG LGSISLIVGV ILKCIPVGSG
     ETSATPNGYR PLANGPDDI