ACA5_ORYSJ
ID ACA5_ORYSJ Reviewed; 1088 AA.
AC Q7X8B5; U3N024;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Calcium-transporting ATPase 5, plasma membrane-type {ECO:0000305};
DE Short=OsACA5 {ECO:0000303|PubMed:24286292};
DE EC=7.2.2.10 {ECO:0000305};
DE AltName: Full=Ca(2+)-ATPase isoform 5 {ECO:0000305};
DE AltName: Full=OsACA6 {ECO:0000303|PubMed:24128296};
GN Name=ACA5 {ECO:0000303|PubMed:24286292};
GN OrderedLocusNames=Os04g0605500 {ECO:0000312|EMBL:BAF15709.1},
GN LOC_Os04g51610 {ECO:0000305};
GN ORFNames=OsJ_16068 {ECO:0000312|EMBL:EEE61631.1},
GN OSJNBa0035M09.2 {ECO:0000312|EMBL:CAD41784.2},
GN OSJNBb0015N08.12 {ECO:0000312|EMBL:CAE03884.2};
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=24128296; DOI=10.1111/tpj.12352;
RA Huda K.M., Banu M.S., Garg B., Tula S., Tuteja R., Tuteja N.;
RT "OsACA6, a P-type IIB Ca(2+) ATPase promotes salinity and drought stress
RT tolerance in tobacco by ROS scavenging and enhancing the expression of
RT stress-responsive genes.";
RL Plant J. 76:997-1015(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
RN [3]
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 [4]
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 [5]
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 [6]
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 [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).
RN [8]
RP FUNCTION, AND INTERACTION WITH NOH1.
RX PubMed=24992889; DOI=10.1016/j.plaphy.2014.06.007;
RA Kamrul Huda K.M., Akhter Banu M.S., Yadav S., Sahoo R.K., Tuteja R.,
RA Tuteja N.;
RT "Salinity and drought tolerant OsACA6 enhances cold tolerance in transgenic
RT tobacco by interacting with stress-inducible proteins.";
RL Plant Physiol. Biochem. 82:229-238(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 (By
CC similarity). Involved in salt and drought stress tolerance
CC (PubMed:24128296). Involved in cold stress tolerance (PubMed:24992889).
CC {ECO:0000250, ECO:0000269|PubMed:24128296,
CC ECO:0000269|PubMed:24992889}.
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; Evidence={ECO:0000305};
CC -!- ACTIVITY REGULATION: Activated by calmodulin. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with NOH1. {ECO:0000269|PubMed:24992889}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24128296};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Induced by salt, drought and heat stresses, and abscisic
CC acid (ABA). {ECO:0000269|PubMed:24128296}.
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; KF240826; AGW24530.1; -; mRNA.
DR EMBL; AL662968; CAD41784.2; -; Genomic_DNA.
DR EMBL; AL662996; CAE03884.2; -; Genomic_DNA.
DR EMBL; AP008210; BAF15709.1; -; Genomic_DNA.
DR EMBL; AP014960; BAS90883.1; -; Genomic_DNA.
DR EMBL; CM000141; EEE61631.1; -; Genomic_DNA.
DR RefSeq; XP_015636669.1; XM_015781183.1.
DR AlphaFoldDB; Q7X8B5; -.
DR SMR; Q7X8B5; -.
DR STRING; 4530.OS04T0605500-02; -.
DR PaxDb; Q7X8B5; -.
DR PRIDE; Q7X8B5; -.
DR EnsemblPlants; Os04t0605500-01; Os04t0605500-01; Os04g0605500.
DR EnsemblPlants; Os04t0605500-02; Os04t0605500-02; Os04g0605500.
DR GeneID; 4336912; -.
DR Gramene; Os04t0605500-01; Os04t0605500-01; Os04g0605500.
DR Gramene; Os04t0605500-02; Os04t0605500-02; Os04g0605500.
DR KEGG; osa:4336912; -.
DR eggNOG; KOG0204; Eukaryota.
DR HOGENOM; CLU_002360_9_0_1; -.
DR InParanoid; Q7X8B5; -.
DR OMA; GMVYKDF; -.
DR OrthoDB; 115892at2759; -.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000007752; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR ExpressionAtlas; Q7X8B5; baseline and differential.
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:UniProtKB.
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 GO; GO:0009409; P:response to cold; IMP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IMP:UniProtKB.
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 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 ATP-binding; Calcium; Calcium transport; Calmodulin-binding; Cell membrane;
KW Glycoprotein; Ion transport; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Reference proteome; Stress response; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1088
FT /note="Calcium-transporting ATPase 5, plasma membrane-type"
FT /id="PRO_0000439551"
FT TOPO_DOM 1..198
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 220..221
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 243..338
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 360..375
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 397..425
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 426..446
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 447..851
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 852..872
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 873..880
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 881..901
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 902..919
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 920..940
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 941..1000
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1001..1021
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1022..1030
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1031..1051
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1052..1088
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 486
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 794
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 798
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT CARBOHYD 532
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 569
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 737
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 107
FT /note="E -> G (in Ref. 1; AGW24530)"
FT /evidence="ECO:0000305"
FT CONFLICT 702
FT /note="V -> I (in Ref. 1; AGW24530)"
FT /evidence="ECO:0000305"
FT CONFLICT 962
FT /note="D -> G (in Ref. 1; AGW24530)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1088 AA; 117663 MW; B07C65EFDC3CAB2E CRC64;
MESASSSLAT SGRRRSSSGG GGGSWGSIGS AADPFDIPAK GAPVESLKKW RQAALVLNAS
RRFRYTLDLK REEQREEVIS KIRAQAHVVR AAFRFKEAGQ VHVQQKEVAA PPVDGALGFG
IKEDQLTALT RDHNYSALQQ YGGISGVARM LKTDTEKGIS GDDSDLTARR NAFGSNTYPR
KKGRSFLAFL WDACKDLTLI ILMVAAAVSL ALGITTEGIK EGWYDGASIA FAVLLVVVVT
ATSDYKQSLQ FQNLNEEKQN IKLEVVRGGR RISVSIYDLV AGDVVPLKIG DQVPADGILI
SGHSLSVDES SMTGESKIVH KDQKSPFLMS GCKVADGYGT MLVTAVGINT EWGLLMASIS
EDSGEETPLQ VRLNGVATFI GMVGLSVALA VLVVLLARYF TGHTYNPDGS VQYVKGKMGV
GQTIRGIVGI FTVAVTIVVV AVPEGLPLAV TLTLAFSMRK MMRDKALVRR LSACETMGSA
TTICSDKTGT LTLNQMTVVE AYFGGKKMDP PDNVQVLSAS ISSLIVEGIA QNTSGSIFEP
ENGQDPEVTG SPTEKAILSW GLKLGMRFND TRTKSSILHV FPFNSEKKRG GVAVHLGGSE
SEVHIHWKGA AEIILDSCKS WLAADGSKHS MTPEKISEFK KFIEDMAASS LRCVAFAYRT
YEMVDVPSED RRADWILPED DLIMLGIVGI KDPCRPGVKD SVRLCAAAGI KVRMVTGDNL
QTARAIALEC GILSDPNVSE PVIIEGKAFR ALSDLEREEA AEKISVMGRS SPNDKLLLVK
ALRKRGHVVA VTGDGTNDAP ALHEADIGLS MGIQGTEVAK ESSDIIILDD NFASVVRVVR
WGRSVYANIQ KFIQFQLTVN VAALIINVVA AVSSGNVPLN AVQLLWVNLI MDTLGALALA
TEPPTDHLMQ RPPVGRREPL ITNVMWRNLI IMALFQVIVL LTLNFRGTSL LQLKNDNQAH
ADKVKNTFIF NTFVLCQVFN EFNARKPDEL NIFKGITGNH LFMAIVAITV VLQALIVEFL
GKFTSTTRLT WQLWLVSIGL AFFSWPLAFV GKLIPVPERP LGDFFACCCP GSKQAADAKG
DDADHSDV
