ACA8_ORYSJ
ID ACA8_ORYSJ Reviewed; 1017 AA.
AC Q2RAS0;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Probable calcium-transporting ATPase 8, plasma membrane-type {ECO:0000305};
DE Short=OsACA8 {ECO:0000303|PubMed:24286292};
DE EC=7.2.2.10;
DE AltName: Full=Ca(2+)-ATPase isoform 8 {ECO:0000305};
GN Name=ACA8 {ECO:0000303|PubMed:24286292};
GN OrderedLocusNames=Os11g0140400, LOC_Os11g04460;
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 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; DP000010; ABA91401.1; -; Genomic_DNA.
DR EMBL; AP008217; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP014967; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015617350.1; XM_015761864.1.
DR AlphaFoldDB; Q2RAS0; -.
DR SMR; Q2RAS0; -.
DR STRING; 39947.Q2RAS0; -.
DR PaxDb; Q2RAS0; -.
DR PRIDE; Q2RAS0; -.
DR GeneID; 4349735; -.
DR KEGG; osa:4349735; -.
DR InParanoid; Q2RAS0; -.
DR OrthoDB; 115892at2759; -.
DR Proteomes; UP000000763; Chromosome 11.
DR Proteomes; UP000059680; Chromosome 11.
DR Genevisible; Q2RAS0; 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..1017
FT /note="Probable calcium-transporting ATPase 8, plasma
FT membrane-type"
FT /id="PRO_0000247304"
FT TOPO_DOM 1..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..228
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 331..351
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 352..384
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 803..823
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 824..825
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 826..846
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 875..895
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 896..938
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 939..959
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 973..993
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 994..1017
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 434
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 736
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 740
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1017 AA; 111286 MW; 65910150C99609D8 CRC64;
MEKLDRYLQE HFDVPAKNPS EEAQRRWRQA VGTIVKNRRR RFRWVPDLDR RSLDKAKVRS
TQEKIRVALY VQQAALIFSD DELALITSKH DSKALKMHGG VDGISKKVRS SFDHGICASD
LDTRQNIYGV NRYAEKPSRS FWMFVWDAFQ DMTLIILMVC ALLSVAVGLA TEGWPKGMYD
GLGIILSIFL VVMVTAVSDY KQSLQFKELD NEKKKIFIHV TRDGRRQKIS IYDLVVGDIV
HLSIGDQVPA DGLYIHGYSL LIDESSLSGE SDPVYVSQDK PFILAGTKVQ DGSAKMIVTA
VGMRTEWGKL MSTLSEGGED ETPLQVKLNG VATVIGKIGL VFAILTFLVL LVRFLIDKGM
TVGLLKWYST DALTIVNYFA TAVTIIVVAV PEGLPLAVTL SLAFAMKKLM NDKALVRHLS
ACETMGSAGT ICTDKTGTLT TNYMVVDKIW ISEVSKSVTS NTISGELNSV VSSRTLSLLL
QGIFENTSAE VVKEKDGKQT VLGTPTERAI LEFGLGLEGV HDAEYSACTK VKVEPFNSVK
KKMAVLISLP SGTSRWFCKG ASEIILQMCD MMVDGDGNAI PLSEAQRKNI LDTINSFASD
ALRTLCLAYK EVDDDIDDNA DSPTSGFTLI AIFGIKDPVR PGVKDAVKTC MSAGITVRMV
TGDNINTAKA IAKECGILTE DGVAIEGPEF HSKSPEEMRD LIPNIQVMAR SLPLDKHTLV
TNLRGMFDEV VSVTGDGTND APALHEADIG LAMGIAGTEV AKESADVIVL DDNFTTIINV
ARWGRAVYIN IQKFVQFQLT VNIVALVINF VSACITGSAP LTAVQLLWVN MIMDTLGALA
LATEPPNDEM MKRPPVRKGE SFITKVMWRN IMGQSLYQLF VLGALMFGGE SLLNIKGADS
KSIINTLIFN SFVFCQVFNE INSREMQKIN VFRGIISNWI FIAVIAATVA FQVVIIEFLG
TFASTVPLNW QHWLLSVGLG SISLIVGVIL KCIPVGSGET SATPNGYRPL ANGPDDI
