ACA12_ARATH
ID ACA12_ARATH Reviewed; 1033 AA.
AC Q9LY77; Q8GZ18;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Calcium-transporting ATPase 12, plasma membrane-type;
DE EC=7.2.2.10;
DE AltName: Full=Ca(2+)-ATPase isoform 12;
GN Name=ACA12; OrderedLocusNames=At3g63380; ORFNames=MAA21_10;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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 or into organelles. {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; Multi-pass membrane protein.
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; AL163818; CAB87791.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80473.1; -; Genomic_DNA.
DR EMBL; AK117260; BAC41935.1; -; mRNA.
DR EMBL; BT005977; AAO64912.1; -; mRNA.
DR PIR; T49179; T49179.
DR RefSeq; NP_191897.1; NM_116203.3.
DR AlphaFoldDB; Q9LY77; -.
DR SMR; Q9LY77; -.
DR BioGRID; 10827; 19.
DR IntAct; Q9LY77; 16.
DR STRING; 3702.AT3G63380.1; -.
DR TCDB; 3.A.3.2.42; the p-type atpase (p-atpase) superfamily.
DR PaxDb; Q9LY77; -.
DR PRIDE; Q9LY77; -.
DR ProteomicsDB; 244340; -.
DR EnsemblPlants; AT3G63380.1; AT3G63380.1; AT3G63380.
DR GeneID; 825513; -.
DR Gramene; AT3G63380.1; AT3G63380.1; AT3G63380.
DR KEGG; ath:AT3G63380; -.
DR Araport; AT3G63380; -.
DR TAIR; locus:2087363; AT3G63380.
DR eggNOG; KOG0204; Eukaryota.
DR HOGENOM; CLU_002360_9_3_1; -.
DR InParanoid; Q9LY77; -.
DR OMA; CKITITL; -.
DR OrthoDB; 115892at2759; -.
DR PhylomeDB; Q9LY77; -.
DR BioCyc; ARA:AT3G63380-MON; -.
DR PRO; PR:Q9LY77; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LY77; baseline and differential.
DR Genevisible; Q9LY77; AT.
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; ISS:TAIR.
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; 3.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Calcium; Calcium transport; Calmodulin-binding;
KW Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1033
FT /note="Calcium-transporting ATPase 12, plasma membrane-
FT type"
FT /id="PRO_0000046418"
FT TOPO_DOM 1..152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..191
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..341
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 362..397
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 398..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 416..806
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 807..825
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 826..836
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 837..857
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 858..877
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 878..900
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 901..909
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 910..930
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 931..948
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 949..970
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 971..980
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 981..1002
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1003..1006
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 25..36
FT /note="Interaction with calmodulin"
FT /evidence="ECO:0000305"
FT ACT_SITE 453
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 751
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 755
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O81108"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O81108"
FT CONFLICT 239
FT /note="Q -> R (in Ref. 3; BAC41935 and 4; AAO64912)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1033 AA; 113707 MW; D0898F370970D451 CRC64;
MRDLKEYDYS ALLLNLTTSS LNKAQRRWRF AYAAIYSMRA MLSLVKEIVP ARIDPKTSDA
SLSLSYTALE SGEGAKINSM PLSYVPAIDQ EQLVEIMKGK DLPGIQALGG VEGVAASLRT
NPTKGIHGNE QEVSRRRDLF GSNTYHKPPP KGLLFFVYEA FKDLTILILL VCAIFSLGFG
IKEHGIKEGW YEGGSIFVAV FLVIVVSALS NFRQERQFDK LSKISNNIKV EVLRDSRRQH
ISIFDVVVGD VVFLKIGDQI PADGLFLEGH SLQVDESSMT GESDHLEVDH KDNPFLFSGT
KIVDGFAQML VVSVGMSTTW GQTMSSINQD SSERTPLQVR LDTLTSTIGK IGLTVAALVL
VVLLVRYFTG NTEKEGKREY NGSKTPVDTV VNSVVRIVAA AVTIVVVAIP EGLPLAVTLT
LAYSMKRMMS DQAMVRKLSA CETMGSATVI CTDKTGTLTL NEMKVTKFWL GQESIHEDST
KMISPDVLDL LYQGTGLNTT GSVCVSDSGS TPEFSGSPTE KALLSWTVLN LGMDMESVKQ
KHEVLRVETF SSAKKRSGVL VRRKSDNTVH VHWKGAAEMV LAMCSHYYTS TGSVDLMDST
AKSRIQAIIQ GMAASSLRCI AFAHKIASND SVLEEDGLTL MGIVGLKDPC RPGVSKAVET
CKLAGVTIKM ITGDNVFTAK AIAFECGILD HNDKDEEDAV VEGVQFRNYT DEERMQKVDK
IRVMARSSPS DKLLMVKCLR LKGHVVAVTG DGTNDAPALK EADIGLSMGI QGTEVAKESS
DIVILDDNFA SVATVLKWGR CVYNNIQKFI QFQLTVNVAA LVINFIAAIS AGEVPLTAVQ
LLWVNLIMDT LGALALATER PTNELLKRKP VGRTEALITN VMWRNLLVQS LYQIAVLLIL
QFKGMSIFSV RKEVKDTLIF NTFVLCQVFN EFNAREMEKK NVFKGLHRNR LFIGIIAITI
VLQVIMVEFL KKFADTVRLN GWQWGTCIAL ASLSWPIGFF TKFIPVSETP FLSYFKNPRS
LFKGSRSPSL KKP
