ACA7_ORYSJ
ID ACA7_ORYSJ Reviewed; 1035 AA.
AC Q7XEK4; B9G5R9; Q0IXN9; Q8S856;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Calcium-transporting ATPase 7, plasma membrane-type {ECO:0000305};
DE Short=OsACA7 {ECO:0000303|PubMed:24286292};
DE EC=7.2.2.10 {ECO:0000305};
DE AltName: Full=Ca(2+)-ATPase isoform 7 {ECO:0000305};
GN Name=ACA7 {ECO:0000303|PubMed:24286292};
GN OrderedLocusNames=Os10g0418100 {ECO:0000312|EMBL:BAT10869.1},
GN LOC_Os10g28240 {ECO:0000312|EMBL:AAP53785.1};
GN ORFNames=OsJ_31537 {ECO:0000312|EMBL:EEE50966.1},
GN OSJNBa0061K21.21 {ECO:0000312|EMBL:AAM08790.1};
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=12791992; DOI=10.1126/science.1083523;
RA Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S.,
RA Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D.,
RA Oates R., Palmer M., Pries G., Gibson J., Anderson H., Paradkar M.,
RA Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F.,
RA Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M.,
RA Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R.,
RA Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F.,
RA Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D.,
RA Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R.,
RA Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S.,
RA Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S.,
RA Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R.,
RA Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M.,
RA Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R.,
RA Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E.,
RA Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.;
RT "In-depth view of structure, activity, and evolution of rice chromosome
RT 10.";
RL Science 300:1566-1569(2003).
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 FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY COLD STRESS, GENE FAMILY, AND
RP 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 (By
CC similarity). Involved in salt stress tolerance (PubMed:24286292).
CC {ECO:0000250, ECO:0000269|PubMed:24286292}.
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 -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:24286292}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Induced by cold stress. {ECO:0000269|PubMed:24286292}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF26526.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAT10869.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=EEE50966.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC016780; AAM08790.1; -; Genomic_DNA.
DR EMBL; DP000086; AAP53785.1; -; Genomic_DNA.
DR EMBL; AP008216; BAF26526.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP014966; BAT10869.1; ALT_INIT; Genomic_DNA.
DR EMBL; CM000147; EEE50966.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_015613068.1; XM_015757582.1.
DR AlphaFoldDB; Q7XEK4; -.
DR SMR; Q7XEK4; -.
DR STRING; 4530.OS10T0418100-01; -.
DR PRIDE; Q7XEK4; -.
DR EnsemblPlants; Os10t0418100-01; Os10t0418100-01; Os10g0418100.
DR GeneID; 4348639; -.
DR Gramene; Os10t0418100-01; Os10t0418100-01; Os10g0418100.
DR KEGG; osa:4348639; -.
DR eggNOG; KOG0204; Eukaryota.
DR OrthoDB; 115892at2759; -.
DR Proteomes; UP000000763; Chromosome 10.
DR Proteomes; UP000007752; Chromosome 10.
DR Proteomes; UP000059680; Chromosome 10.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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 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 2: Evidence at transcript level;
KW ATP-binding; Calcium; Calcium transport; Calmodulin-binding; Glycoprotein;
KW Golgi apparatus; Ion transport; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Reference proteome; Stress response; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1035
FT /note="Calcium-transporting ATPase 7, plasma membrane-type"
FT /id="PRO_0000439591"
FT TOPO_DOM 1..166
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..194
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..348
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 370..395
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 396..416
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 417..818
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 819..839
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 840..845
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 846..866
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 867..887
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 888..910
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 911..919
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 920..940
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 941..960
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 961..981
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 982..990
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 991..1011
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1012..1035
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT ACT_SITE 460
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 761
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 765
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1035 AA; 111249 MW; 3E735445411F728A CRC64;
MECADYFIGS GRRCSPSTST STSREAWRPE KQWRKATNVI RGCHRLLRLG VLSAAAGIMR
RNPSYVEIKV HDEGELDVSS GGDGEAPVAF TVAADDESFK GLVKNKREDC FRLLGGGAGV
AAVLASGAER GIRGDDADVA RRKKAFGSNT YPKPKPKGFF RHVWDALADV FLIVLLVCAA
VSLAFGIKEH GIKDGWYDGV SIFLAVFLVA AVSAVSNHSQ GKRFDKLARE SENIMVSVVR
AARRQEVSIF DVVVGDVVVL KIGDVVPADG VFLDGHALQV DESSMTGEPH PVEVDAVKSP
FLASGVKVVD GYGKMVVTAV GTDTAWGEMM RTITRENTDP TPLQERLEGL TSSIGKVGIA
VAVLVFAVLT ARHFTGSTRD EQGNALFDKR NVTFNAVFSG LVGIFQQAVT IIVVAIPEGL
PLAVTLTLAF SMKRMVRENA LVRRLSACET MGSVTAICTD KTGTLTLNQM KVTEFWVGAD
RPRSAAAVNG GVVRLLCQGA GLNTTGSVYK PDNVSPPEIT GSPTEKALLS WAVEELPMDA
DALKRKCKVV RVEAFNSDKK RSGVMLRDAA TGAVTAHWKG AAEMVLARCT VYVGADGAAR
ELGVEQRRKL EQVINDMAAA SLRCIAFAYK QVVDGGDSDN AKIDDEGLTL LGFVGLKDPC
RPEVKSAIEA CTKAGIAVKM VTGDNVLTAR AIAKECGIIS GNDDDAAGVV IEGHEFRAMS
EQEQLAIVDN IRVMARSLPL DKLVLVQRLK QKGHVVAVTG DGTNDAPALK EADVGLSMGV
QGTEVAKESS DIVILNDNFD TVVTATRWGR CVYNNIQKFI QFQLTVNVAA LVINFVSAVT
TGRMPLTTVQ LLWVNLIMDT MGALALATDT PTAGLMRRPP IGRAAPLISN AMWRNLAAQA
AYQVAVLLAL QYRGFGGAGA GERANGTMIF NAFVLCQVFN EFNAREIERR NVFAGVHRNR
MFLGIVAVTV ALQVVMVELL TKFAGTERLG WGQWGACVGI AAVSWPIGWA VKCIPVPERP
FHEIITARRR RRRST
