ACA3_ORYSJ
ID ACA3_ORYSJ Reviewed; 1033 AA.
AC Q6ATV4; A0A0P0W069; Q10GR4;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Calcium-transporting ATPase 3, plasma membrane-type {ECO:0000305};
DE Short=OsACA3 {ECO:0000303|PubMed:24286292};
DE EC=7.2.2.10;
DE AltName: Full=Ca(2+)-ATPase isoform 3 {ECO:0000305};
GN Name=ACA3 {ECO:0000303|PubMed:24286292};
GN OrderedLocusNames=Os03g0616400 {ECO:0000312|EMBL:BAF12575.1},
GN LOC_Os03g42020 {ECO:0000312|EMBL:ABF97637.1}; ORFNames=OJ1285_H07.3;
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=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(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 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 [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.
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 -!- 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; AC135557; AAT81659.1; -; Genomic_DNA.
DR EMBL; DP000009; ABF97637.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF12575.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS85276.1; -; Genomic_DNA.
DR EMBL; AK065088; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; Q6ATV4; -.
DR SMR; Q6ATV4; -.
DR STRING; 4530.OS03T0616400-01; -.
DR PaxDb; Q6ATV4; -.
DR PRIDE; Q6ATV4; -.
DR EnsemblPlants; Os03t0616400-01; Os03t0616400-01; Os03g0616400.
DR Gramene; Os03t0616400-01; Os03t0616400-01; Os03g0616400.
DR eggNOG; KOG0204; Eukaryota.
DR HOGENOM; CLU_002360_9_2_1; -.
DR InParanoid; Q6ATV4; -.
DR OMA; CKRAHRE; -.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR ExpressionAtlas; Q6ATV4; baseline and differential.
DR Genevisible; Q6ATV4; 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; 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; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDF00027; p-type_atpase; 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 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..1033
FT /note="Calcium-transporting ATPase 3, plasma membrane-type"
FT /id="PRO_0000247301"
FT TOPO_DOM 1..180
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..268
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 383..405
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 823..843
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 844..846
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 847..867
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 928..948
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 949..965
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 966..986
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 999..1019
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1020..1033
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 461
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 762
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 766
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT CONFLICT 750
FT /note="R -> P (in Ref. 5; AK065088)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1033 AA; 111729 MW; 933D0F0CAB993BF6 CRC64;
MHSGVNGCCP LRLPAAAAVH GRRIPPLLPP RGAWPGCIAA PALHRKPGRG GGGALSSCRR
ASHHEKLQVA ALPSKATLEF EHGVSLRSAY IVPEDVQAAG FQIDADELAS IVESRDTKKL
TVHGQLNGIA DKLGTSLTNG IVTDKDLLNQ RQDIYGVNKF AETEIRSFWE FVWEALEDTT
LIILSACAIF SLVVGITTEG WPQGAHDGVG IVASILLVVS VTGTSNYQQS LQFRDLDKEK
RKILVQVTRN GLRQRVLIDD LLPGDAVHLA VGDQVPADGL FISGFSVLVD ESSLTGESEP
VFVNEDNPYL LSGTKVLDGS CKMLVTAVGM RTQWGKLMAV LTDGGDDETP LQTRLNGVAN
TIGKIGLFFA VLTFIVLSQG IIGQKYLDGL LLSWSGDDVL EILDHFAVAV TIVVVAVPEG
LPLAVTLSLA FAMKKMMNDK ALVRQLAACE TMGSATVICS DKTGTLTTNR MTVVKACICG
NTIQVNNPQT PNMSSNFPEV AVETLLESIF NNTSGEVVTN QDGKYQILGT PTETALLEFA
LLLDGDCKEK QLGSKIVKVE PFNSTKKRMS TILELPGGGY RAHCKGASEI VLAACDKFID
ERGCIVPLDD KTSSKLNDII KAFSSEALRT LCLAYREMEE GFSTQEQIPL QGYTCIGIVG
IKDPVRPGVR QSVATCRSAG ISVRMITGDN IDTAKAIARE CGILTKDGIA IEGAEFREKS
AEELHDLIPK MQVLARSSPL DKHTLVKHLR TAFNEVVAVT GDGTNDAPAL READIGLAMG
IAGTEVAKES ADVVILDDNF STIVTVAKWG RSVYVNIQKF VQFQLTVNVV ALLVNFTSAC
FTGDAPLTAV QLLWVNMIMD TLGALALATE PPNNNLMKKA PVGRKGKFIT NVMWRNIVGQ
SLYQFAVMWY LQTQGKHLFG LEGYHADIVL NTIIFNTFVF CQVFNEISSR EMEDINVLRG
MAGNSIFLGV LTGTIFFQFI LVQFLGDFAN TTPLTQQQWL ISILFGFLGM PIAAAIKLIA
VEPHEKADTR RTP
