ECA1_ARATH
ID ECA1_ARATH Reviewed; 1061 AA.
AC P92939; O04987;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Calcium-transporting ATPase 1, endoplasmic reticulum-type;
DE EC=7.2.2.10 {ECO:0000269|PubMed:9238019};
GN Name=ECA1; Synonyms=ACA3; OrderedLocusNames=At1g07810; ORFNames=F24B9.9;
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 [MRNA], AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Columbia;
RX PubMed=9238019; DOI=10.1073/pnas.94.16.8579;
RA Liang F., Cunningham K.W., Harper J.F., Sze H.;
RT "ECA1 complements yeast mutants defective in Ca2+ pumps and encodes an
RT endoplasmic reticulum-type Ca2+-ATPase in Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:8579-8584(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Hong B., Wang Y., Young J., Sussman M.R., Harper J.F.;
RT "Primary structure and genetic disruption of an ER-type Ca2+-pump (ACA3) in
RT Arabidopsis.";
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
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).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 630-1061.
RC STRAIN=cv. Landsberg erecta;
RA Roberts P.E., Long A.R., Williams L.E., Evans D.E.;
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP CHARACTERIZATION.
RX PubMed=12226493; DOI=10.1104/pp.004440;
RA Wu Z., Liang F., Hong B., Young J.C., Sussman M.R., Harper J.F., Sze H.;
RT "An endoplasmic reticulum-bound Ca(2+)/Mn(2+) pump, ECA1, supports plant
RT growth and confers tolerance to Mn(2+) stress.";
RL Plant Physiol. 130:128-137(2002).
CC -!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of
CC ATP coupled with the translocation of calcium from the cytosol to the
CC endoplasmic reticulum lumen. Also regulates manganese ion homeostasis
CC by pumping it into endomembrane compartments. Can also transport zinc.
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 Evidence={ECO:0000269|PubMed:9238019};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIA subfamily. {ECO:0000305}.
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DR EMBL; U96455; AAC68819.1; -; mRNA.
DR EMBL; U93845; AAB52420.1; -; mRNA.
DR EMBL; AC007583; AAF75073.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28186.1; -; Genomic_DNA.
DR EMBL; AF116533; AAF36087.1; -; Genomic_DNA.
DR EMBL; Y09817; CAA70946.1; -; mRNA.
DR PIR; E86213; E86213.
DR RefSeq; NP_172259.1; NM_100655.4.
DR AlphaFoldDB; P92939; -.
DR SMR; P92939; -.
DR BioGRID; 22537; 3.
DR STRING; 3702.AT1G07810.1; -.
DR TCDB; 3.A.3.2.13; the p-type atpase (p-atpase) superfamily.
DR iPTMnet; P92939; -.
DR PaxDb; P92939; -.
DR PRIDE; P92939; -.
DR ProteomicsDB; 222046; -.
DR EnsemblPlants; AT1G07810.1; AT1G07810.1; AT1G07810.
DR GeneID; 837296; -.
DR Gramene; AT1G07810.1; AT1G07810.1; AT1G07810.
DR KEGG; ath:AT1G07810; -.
DR Araport; AT1G07810; -.
DR TAIR; locus:2026580; AT1G07810.
DR eggNOG; KOG0202; Eukaryota.
DR HOGENOM; CLU_002360_3_2_1; -.
DR InParanoid; P92939; -.
DR OMA; NRPVQCG; -.
DR OrthoDB; 100699at2759; -.
DR PhylomeDB; P92939; -.
DR BioCyc; ARA:AT1G07810-MON; -.
DR BioCyc; MetaCyc:MON-14600; -.
DR BRENDA; 7.2.2.10; 399.
DR BRENDA; 7.2.2.22; 399.
DR PRO; PR:P92939; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P92939; baseline and differential.
DR Genevisible; P92939; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:TAIR.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0000325; C:plant-type vacuole; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005388; F:P-type calcium transporter activity; IDA:TAIR.
DR GO; GO:0015662; F:P-type ion transporter activity; IBA:GO_Central.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006816; P:calcium ion transport; IGI:UniProtKB.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0010042; P:response to manganese ion; IMP: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; 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 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; TIGR01494; ATPase_P-type; 3.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Calcium; Calcium transport; Endoplasmic reticulum;
KW Ion transport; Magnesium; Manganese; Membrane; Metal-binding;
KW Nucleotide-binding; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1061
FT /note="Calcium-transporting ATPase 1, endoplasmic
FT reticulum-type"
FT /id="PRO_0000046405"
FT TOPO_DOM 1..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..115
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 136..278
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..327
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..345
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 346..786
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 787..806
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 807..816
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 817..837
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 838..857
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 858..880
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 881..950
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 951..970
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 971..983
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 984..1002
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1003..1017
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1018..1038
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1039..1061
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 383
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 336
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 339
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 341
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 731
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 735
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 797
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 800
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 825
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 828
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 829
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 829
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 961
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT VARIANT 684
FT /note="I -> K (in strain: cv. Landsberg erecta)"
SQ SEQUENCE 1061 AA; 116366 MW; 4281842216E1340F CRC64;
MGKGSEDLVK KESLNSTPVN SDTFPAWAKD VAECEEHFVV SREKGLSSDE VLKRHQIYGL
NELEKPEGTS IFKLILEQFN DTLVRILLAA AVISFVLAFF DGDEGGEMGI TAFVEPLVIF
LILIVNAIVG IWQETNAEKA LEALKEIQSQ QATVMRDGTK VSSLPAKELV PGDIVELRVG
DKVPADMRVV ALISSTLRVE QGSLTGESEA VSKTTKHVDE NADIQGKKCM VFAGTTVVNG
NCICLVTDTG MNTEIGRVHS QIQEAAQHEE DTPLKKKLNE FGEVLTMIIG LICALVWLIN
VKYFLSWEYV DGWPRNFKFS FEKCTYYFEI AVALAVAAIP EGLPAVITTC LALGTRKMAQ
KNALVRKLPS VETLGCTTVI CSDKTGTLTT NQMAVSKLVA MGSRIGTLRS FNVEGTSFDP
RDGKIEDWPM GRMDANLQMI AKIAAICNDA NVEQSDQQFV SRGMPTEAAL KVLVEKMGFP
EGLNEASSDG DVLRCCRLWS ELEQRIATLE FDRDRKSMGV MVDSSSGNKL LLVKGAVENV
LERSTHIQLL DGSKRELDQY SRDLILQSLR DMSLSALRCL GFAYSDVPSD FATYDGSEDH
PAHQQLLNPS NYSSIESNLI FVGFVGLRDP PRKEVRQAIA DCRTAGIRVM VITGDNKSTA
EAICREIGVF EADEDISSRS LTGIEFMDVQ DQKNHLRQTG GLLFSRAEPK HKQEIVRLLK
EDGEVVAMTG DGVNDAPALK LADIGVAMGI SGTEVAKEAS DMVLADDNFS TIVAAVGEGR
SIYNNMKAFI RYMISSNIGE VASIFLTAAL GIPEGMIPVQ LLWVNLVTDG PPATALGFNP
PDKDIMKKPP RRSDDSLITA WILFRYMVIG LYVGVATVGV FIIWYTHSSF MGIDLSQDGH
SLVSYSQLAH WGQCSSWEGF KVSPFTAGSQ TFSFDSNPCD YFQQGKIKAS TLSLSVLVAI
EMFNSLNALS EDGSLVTMPP WVNPWLLLAM AVSFGLHFVI LYVPFLAQVF GIVPLSLNEW
LLVLAVSLPV ILIDEVLKFV GRCTSGYRYS PRTLSTKQKE E
