ACA1_ORYSJ
ID ACA1_ORYSJ Reviewed; 1043 AA.
AC Q8RUN1; A0A0P0VCM3; Q0JG69;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Calcium-transporting ATPase 1, plasma membrane-type {ECO:0000305};
DE Short=OsACA1 {ECO:0000303|PubMed:24286292};
DE EC=7.2.2.10;
DE AltName: Full=Ca(2+)-ATPase isoform 1 {ECO:0000305};
GN Name=ACA1 {ECO:0000303|PubMed:24286292};
GN OrderedLocusNames=Os01g0939100, LOC_Os01g71240;
GN ORFNames=B1150F11.11, P0504E02.35;
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=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
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. {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; AP003269; BAB89725.1; -; Genomic_DNA.
DR EMBL; AP003412; BAB90248.1; -; Genomic_DNA.
DR EMBL; AP008207; BAF07259.1; -; Genomic_DNA.
DR EMBL; AP014957; BAS76138.1; -; Genomic_DNA.
DR EMBL; AK070064; BAG91749.1; -; mRNA.
DR RefSeq; XP_015621941.1; XM_015766455.1.
DR AlphaFoldDB; Q8RUN1; -.
DR SMR; Q8RUN1; -.
DR STRING; 4530.OS01T0939100-01; -.
DR PaxDb; Q8RUN1; -.
DR PRIDE; Q8RUN1; -.
DR EnsemblPlants; Os01t0939100-01; Os01t0939100-01; Os01g0939100.
DR GeneID; 4326507; -.
DR Gramene; Os01t0939100-01; Os01t0939100-01; Os01g0939100.
DR KEGG; osa:4326507; -.
DR eggNOG; KOG0204; Eukaryota.
DR HOGENOM; CLU_002360_9_2_1; -.
DR InParanoid; Q8RUN1; -.
DR OMA; PNDAMMK; -.
DR OrthoDB; 115892at2759; -.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR Genevisible; Q8RUN1; 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; 4.
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..1043
FT /note="Calcium-transporting ATPase 1, plasma membrane-type"
FT /id="PRO_0000247302"
FT TOPO_DOM 1..178
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..258
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 377..395
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 396..416
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 824..844
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 845
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 846..866
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 891..911
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 912..955
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 956..976
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 998..1018
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1019..1043
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1023..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
SQ SEQUENCE 1043 AA; 112842 MW; A16B82561803AF56 CRC64;
MSFIRKKSME FLKSFEVPAK NPSEEAQRRW RDAVGTLVKN RRRRFRMVPD LDKRSQAETQ
RRKIQEKLRV ALFVQKAALQ FIDAVRKTEH PLPELARQCG FSVSAEELAS IVRGHDTKSL
RFHNGVDGIA RKVAVSLADG VKSDDAGLRA EVYGANQYTE KPPRTFWMFL WDASQDMTLL
LLAFCAAVSV AIGLATEGWP SGMYDGVGIM LTILLVVMIT AASDYKQSLQ FRDLDKEKKK
IDVQVTRDGY RQKVSIYDIV VGDIVHLSIG DQVPADGLFI DGYSFVVDES NLSGESEPVH
VSTANRFLLG GTKVQDGSAR MLVTAVGMRT EWGNLMETLS QGGEDETPLQ VKLNGVATII
GKIGLAFAVL TFTVLMARFL LGKAGAPGGL LRWRMVDALA VLNFFAVAVT IIVVAVPEGL
PLAVTLSLAF AMKKLMQERA LVRHLSACET MGSASCICTD KTGTLTTNHM VVEKIWASGA
AQTMSNAKGF DQLTSSMSET FAKVLLEGVF HCSGSEVVRG KDGRHTIMGT PTETAILEFG
LAVEKRARIE HTGAGKLKVE PFNSVKKTMA VVIASPSAGG RPRAFLKGAS EVVLSRCSLV
LDGTGNVEKL TDAKAKRVAS AIDAFACEAL RTLCLAYQDV DGGGGDIPGE GYTLIAVFGI
KDPLRPGVRE AVATCHAAGI NVRMVTGDNI NTAKAIAREC GILTDDGIAI EGPEFRNKDP
DQMREIIPKI QVMARSLPLD KHTLVTNLRG MFNEVVAVTG DGTNDAPALH EADIGLAMGI
AGTEVAKENA DVIIMDDNFS TIINVAKWGR SVYINIQKFV QFQLTVNVVA LMVNFISASF
TGSAPLTIVQ LLWVNLIMDT LGALALATEP PNDAMMKRPP VGRGDNFITK VMWRNIVGQS
IYQLVVLGVL LLRGKSLLQI NGPQADSLLN TFVFNTFVFC QVFNEVNSRE MEKINVFSGI
FSSWIFSAVV GVTAGFQVIM VELLGTFANT VHLSGKLWLT SVLIGSVGLV IGAILKCIPV
ESGSDASDRH DGYRPIPTGP SAV