ACA1_ARATH
ID ACA1_ARATH Reviewed; 1020 AA.
AC Q37145; Q37146; Q42571; Q42587; Q9SFY1;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 30-APR-2003, sequence version 3.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Calcium-transporting ATPase 1;
DE EC=7.2.2.10;
DE AltName: Full=Ca(2+)-ATPase isoform 1;
DE AltName: Full=Plastid envelope ATPase 1;
GN Name=ACA1; Synonyms=PEA1; OrderedLocusNames=At1g27770;
GN ORFNames=F28L5.1, T22C5.23;
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 PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND PARTIAL PROTEIN
RP SEQUENCE.
RC STRAIN=cv. Columbia;
RX PubMed=8234257; DOI=10.1073/pnas.90.21.10066;
RA Huang L., Berkelman T., Franklin A.E., Hoffman N.E.;
RT "Characterization of a gene encoding a Ca(2+)-ATPase-like protein in the
RT plastid envelope.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:10066-10070(1993).
RN [2]
RP ERRATUM OF PUBMED:8234257, AND SEQUENCE REVISION.
RA Huang L., Berkelman T., Franklin A.E., Hoffman N.E.;
RL Proc. Natl. Acad. Sci. U.S.A. 91:9664-9664(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
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).
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.
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: Plastid, chloroplast inner membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q37145-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed at higher levels in roots than in leaves.
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=AAF24958.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA49558.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; L08468; AAD10211.1; -; mRNA.
DR EMBL; L08469; AAD10212.1; -; Genomic_DNA.
DR EMBL; D13983; BAA03090.1; ALT_SEQ; mRNA.
DR EMBL; D13984; BAA03091.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X69940; CAA49558.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X69941; CAA49559.1; ALT_SEQ; mRNA.
DR EMBL; AC012375; AAF24958.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC079280; AAG50579.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30878.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59134.1; -; Genomic_DNA.
DR PIR; D86402; D86402.
DR PIR; S71168; S71168.
DR PIR; T51925; T51925.
DR PIR; T51926; T51926.
DR RefSeq; NP_001321522.1; NM_001332787.1. [Q37145-1]
DR RefSeq; NP_849716.1; NM_179385.2. [Q37145-1]
DR AlphaFoldDB; Q37145; -.
DR SMR; Q37145; -.
DR STRING; 3702.AT1G27770.1; -.
DR TCDB; 3.A.3.2.11; the p-type atpase (p-atpase) superfamily.
DR iPTMnet; Q37145; -.
DR SwissPalm; Q37145; -.
DR PaxDb; Q37145; -.
DR PRIDE; Q37145; -.
DR ProteomicsDB; 244363; -. [Q37145-1]
DR EnsemblPlants; AT1G27770.1; AT1G27770.1; AT1G27770. [Q37145-1]
DR EnsemblPlants; AT1G27770.4; AT1G27770.4; AT1G27770. [Q37145-1]
DR GeneID; 839670; -.
DR Gramene; AT1G27770.1; AT1G27770.1; AT1G27770. [Q37145-1]
DR Gramene; AT1G27770.4; AT1G27770.4; AT1G27770. [Q37145-1]
DR KEGG; ath:AT1G27770; -.
DR Araport; AT1G27770; -.
DR TAIR; locus:2029794; AT1G27770.
DR eggNOG; KOG0204; Eukaryota.
DR HOGENOM; CLU_002360_9_2_1; -.
DR InParanoid; Q37145; -.
DR PhylomeDB; Q37145; -.
DR BioCyc; ARA:AT1G27770-MON; -.
DR BioCyc; MetaCyc:MON-14612; -.
DR PRO; PR:Q37145; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q37145; baseline and differential.
DR Genevisible; Q37145; AT.
DR GO; GO:0009706; C:chloroplast inner membrane; IDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
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:0005634; C:nucleus; HDA:TAIR.
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:0005262; F:calcium channel activity; TAS:TAIR.
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; 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 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Calcium; Calcium transport;
KW Calmodulin-binding; Chloroplast; Direct protein sequencing; Ion transport;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Plastid; Plastid inner membrane; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1020
FT /note="Calcium-transporting ATPase 1"
FT /id="PRO_0000046410"
FT TOPO_DOM 1..162
FT /note="Stromal"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..201
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..350
FT /note="Stromal"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 371..400
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 401..418
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 419..813
FT /note="Stromal"
FT /evidence="ECO:0000255"
FT TRANSMEM 814..832
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 833..843
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 844..864
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 865..884
FT /note="Stromal"
FT /evidence="ECO:0000255"
FT TRANSMEM 885..907
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 908..919
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 920..941
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 942..959
FT /note="Stromal"
FT /evidence="ECO:0000255"
FT TRANSMEM 960..981
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 982..991
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 992..1013
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1014..1020
FT /note="Stromal"
FT /evidence="ECO:0000255"
FT REGION 21..32
FT /note="Interaction with calmodulin"
FT /evidence="ECO:0000250"
FT ACT_SITE 456
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 758
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 762
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 46
FT /note="Phosphoserine; by CPK"
FT /evidence="ECO:0000250|UniProtKB:O81108"
FT CONFLICT 88
FT /note="P -> S (in Ref. 1; AAD10211 and 2; BAA03090/
FT CAA49559)"
FT /evidence="ECO:0000305"
FT CONFLICT 801
FT /note="T -> I (in Ref. 1; AAD10211/AAD10212 and 2;
FT BAA03090/CAA49559)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1020 AA; 111261 MW; BDD81AF7EC4AED6E CRC64;
MESYLNENFG DVKPKNSSDE ALQRWRKLCW IVKNPKRRFR FTANLSKRSE AEAIRRSNQE
KFRVAVLVSQ AALQFINSLK LSSEYTLPEE VRKAGFEICP DELGSIVEGH DLKKLKIHGG
TEGLTEKLST SIASGISTSE DLLSVRKEIY GINQFTESPS RGFWLFVWEA LQDTTLMILA
ACAFVSLIVG ILMEGWPIGA HDGLGIVASI LLVVFVTATS DYRQSLQFKD LDAEKKKIVV
QVTRDKLRQK ISIYDLLPGD VVHLGIGDQI PADGLFISGF SVLINESSLT GESEPVSVSV
EHPFLLSGTK VQDGSCKMLV TTVGMRTQWG KLMATLSEGG DDETPLQVKL NGVATIIGKI
GLFFAVITFA VLVQGLANQK RLDNSHWIWT ADELMAMLEY FAVAVTIVVV AVPEGLPLAV
TLSLAFAMKK MMNDKALVRN LAACETMGSA TTICSDKTGT LTTNHMTVVK ACICEQAKEV
NGPDAAMKFA SGIPESAVKL LLQSIFTNTG GEIVVGKGNK TEILGTPTET ALLEFGLSLG
GDFQEVRQAS NVVKVEPFNS TKKRMGVVIE LPERHFRAHC KGASEIVLDS CDKYINKDGE
VVPLDEKSTS HLKNIIEEFA SEALRTLCLA YFEIGDEFSL EAPIPSGGYT CIGIVGIKDP
VRPGVKESVA ICKSAGITVR MVTGDNLTTA KAIARECGIL TDDGIAIEGP EFREKSDEEL
LKLIPKLQVM ARSSPMDKHT LVRLLRTMFQ EVVAVTGDGT NDAPALHEAD IGLAMGISGT
EVAKESADVI ILDDNFSTIV TVAKWGRSVY INIQKFVQFQ LTVNVVALIV NFLSACLTGN
APLTAVQLLW VNMIMDTLGA LALATEPPQD DLMKRSPVGR KGNFISNVMW RNILGQSLYQ
LVIIWCLQTK GKTMFGLDGP DSDLTLNTLI FNIFVFCQVF NEISSREMEK IDVFKGILKN
YVFVAVLTCT VVFQVIIIEL LGTFADTTPL NLGQWLVSII LGFLGMPVAA ALKMIPVGSH
