ECA3_ARATH
ID ECA3_ARATH Reviewed; 998 AA.
AC Q9SY55; Q0WP80; Q6DQH3; Q9SAV5; Q9SMX2; Q9SWS8;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 3.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Calcium-transporting ATPase 3, endoplasmic reticulum-type {ECO:0000305};
DE Short=AtECA3 {ECO:0000303|Ref.1};
DE EC=7.2.2.10;
GN Name=ECA3 {ECO:0000303|Ref.1}; Synonyms=ACA6;
GN OrderedLocusNames=At1g10130 {ECO:0000312|Araport:AT1G10130};
GN ORFNames=F14N23.1 {ECO:0000312|EMBL:AAD32863.1},
GN T27I1.16 {ECO:0000312|EMBL:AAC34328.2};
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].
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RA Liang F., Sze H.;
RT "AtECA3 encodes a homolog of endoplasmic reticulum-type Ca2+-ATPase from
RT Arabidopsis thaliana.";
RL (er) Plant Gene Register PGR99-077(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=10433975; DOI=10.1016/s0378-1119(99)00242-5;
RA Pittman J.K., Mills R.F., O'Connor C.D., Williams L.E.;
RT "Two additional type IIA Ca(2+)-ATPases are expressed in Arabidopsis
RT thaliana: evidence that type IIA sub-groups exist.";
RL Gene 236:137-147(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=18024560; DOI=10.1104/pp.107.110817;
RA Mills R.F., Doherty M.L., Lopez-Marques R.L., Weimar T., Dupree P.,
RA Palmgren M.G., Pittman J.K., Williams L.E.;
RT "ECA3, a Golgi-localized P2A-type ATPase, plays a crucial role in manganese
RT nutrition in Arabidopsis.";
RL Plant Physiol. 146:116-128(2008).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=18567829; DOI=10.1104/pp.108.119909;
RA Li X., Chanroj S., Wu Z., Romanowsky S.M., Harper J.F., Sze H.;
RT "A distinct endosomal Ca2+/Mn2+ pump affects root growth through the
RT secretory process.";
RL Plant Physiol. 147:1675-1689(2008).
RN [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of
CC ATP coupled with the translocation of calcium from the cytosol to an
CC endomembrane compartment (Probable). Involved in calcium-enhanced root
CC growth, in tolerance to toxic levels of manganese and in secretory
CC processes (PubMed:18567829). Has a crucial role in manganese nutrition,
CC but is not involved in transporting copper, iron or zinc
CC (PubMed:18024560). {ECO:0000269|PubMed:18024560,
CC ECO:0000269|PubMed:18567829, ECO:0000305|PubMed:18567829}.
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:18567829};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18106;
CC Evidence={ECO:0000269|PubMed:18567829};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:18024560}; Multi-pass membrane protein
CC {ECO:0000255}. Endosome membrane {ECO:0000269|PubMed:18567829}; Multi-
CC pass membrane protein {ECO:0000255}. Prevacuolar compartment membrane
CC {ECO:0000269|PubMed:18567829}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in root cap, in elongation and
CC differentiation zones of roots, in vascular tissues of roots, leaves,
CC floral pedicels and style, in leaves, including hydathodes and guard
CC cells, in stamens, in petals, in sepals and in siliques.
CC {ECO:0000269|PubMed:18024560, ECO:0000269|PubMed:18567829}.
CC -!- INDUCTION: Not induced by manganese or zinc.
CC {ECO:0000269|PubMed:18024560}.
CC -!- MISCELLANEOUS: ECA3 is functionally distinct from ECA1 and is localized
CC to a separate compartment.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIA subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD32863.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF117296; AAD29961.1; -; mRNA.
DR EMBL; AJ132388; CAA10660.1; -; mRNA.
DR EMBL; EU082212; ABU53680.1; -; mRNA.
DR EMBL; AY650902; AAT68271.1; -; mRNA.
DR EMBL; AC004122; AAC34328.2; -; Genomic_DNA.
DR EMBL; AC005489; AAD32863.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28545.1; -; Genomic_DNA.
DR EMBL; AK229199; BAF01069.1; -; mRNA.
DR PIR; T00633; T00633.
DR PIR; T52581; T52581.
DR RefSeq; NP_563860.1; NM_100887.3.
DR AlphaFoldDB; Q9SY55; -.
DR SMR; Q9SY55; -.
DR STRING; 3702.AT1G10130.1; -.
DR TCDB; 3.A.3.2.19; the p-type atpase (p-atpase) superfamily.
DR PaxDb; Q9SY55; -.
DR PRIDE; Q9SY55; -.
DR ProteomicsDB; 224717; -.
DR EnsemblPlants; AT1G10130.1; AT1G10130.1; AT1G10130.
DR GeneID; 837550; -.
DR Gramene; AT1G10130.1; AT1G10130.1; AT1G10130.
DR KEGG; ath:AT1G10130; -.
DR Araport; AT1G10130; -.
DR TAIR; locus:2201916; AT1G10130.
DR eggNOG; KOG0202; Eukaryota.
DR HOGENOM; CLU_002360_3_2_1; -.
DR InParanoid; Q9SY55; -.
DR OMA; PLWNNMM; -.
DR OrthoDB; 100699at2759; -.
DR PhylomeDB; Q9SY55; -.
DR BioCyc; ARA:AT1G10130-MON; -.
DR BioCyc; MetaCyc:MON-14610; -.
DR BRENDA; 7.2.2.10; 399.
DR PRO; PR:Q9SY55; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SY55; baseline and differential.
DR Genevisible; Q9SY55; AT.
DR GO; GO:0012505; C:endomembrane system; IDA:TAIR.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
DR GO; GO:0015410; F:ABC-type manganese transporter activity; IMP: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; IMP: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; ISS:TAIR.
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:0055071; P:manganese ion homeostasis; IMP:TAIR.
DR GO; GO:0048364; P:root development; 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; IPR005782; P-type_ATPase_IIA.
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; TIGR01116; ATPase-IIA1_Ca; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Calcium; Calcium transport; Endosome; Golgi apparatus;
KW Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..998
FT /note="Calcium-transporting ATPase 3, endoplasmic
FT reticulum-type"
FT /id="PRO_0000046407"
FT TOPO_DOM 1..48
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..89
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 110..250
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 271..291
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..746
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 747..766
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 767..776
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 777..797
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 798..817
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 818..840
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 841..883
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 884..903
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 904..916
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 917..935
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 936..950
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 951..971
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 972..998
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 347
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 301
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 303
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 305
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 692
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 696
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 757
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 760
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 785
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 788
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 789
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 789
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 894
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT CONFLICT 46
FT /note="R -> G (in Ref. 2; CAA10660)"
FT /evidence="ECO:0000305"
FT CONFLICT 55..56
FT /note="KQ -> NS (in Ref. 1; AAD29961)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="D -> N (in Ref. 4; AAT68271)"
FT /evidence="ECO:0000305"
FT CONFLICT 378..381
FT /note="TVSG -> LLVE (in Ref. 1; AAD29961)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="A -> T (in Ref. 4; AAT68271)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="S -> R (in Ref. 2; CAA10660)"
FT /evidence="ECO:0000305"
FT CONFLICT 586
FT /note="Missing (in Ref. 4; AAT68271)"
FT /evidence="ECO:0000305"
FT CONFLICT 747
FT /note="K -> R (in Ref. 1; AAD29961)"
FT /evidence="ECO:0000305"
FT CONFLICT 943..944
FT /note="FS -> CA (in Ref. 1; AAD29961)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 998 AA; 109060 MW; 214C9865833BA7C0 CRC64;
MEDAYARSVS EVLDFFGVDP TKGLSDSQVV HHSRLYGRNV LPEEKRTPFW KLVLKQFDDL
LVKILIVAAI VSFVLALANG ETGLTAFLEP FVILLILAAN AAVGVITETN AEKALEELRA
YQANIATVLR NGCFSILPAT ELVPGDIVEV TVGCKIPADL RMIEMSSNTF RVDQAILTGE
SCSVEKDVDC TLTTNAVYQD KKNILFSGTD VVAGRGRAVV IGVGSNTAMG SIHDSMLQTD
DEATPLKKKL DEFGSFLAKV IAGICVLVWV VNIGHFSDPS HGGFFKGAIH YFKIAVALAV
AAIPEGLPAV VTTCLALGTK KMARLNAIVR SLPSVETLGC TTVICSDKTG TLTTNMMSVS
KICVVQSAEH GPMINEFTVS GTTYAPEGTV FDSNGMQLDL PAQSPCLHHL AMCSSLCNDS
ILQYNPDKDS YEKIGESTEV ALRVLAEKVG LPGFDSMPSA LNMLSKHERA SYCNHYWENQ
FKKVYVLEFT RDRKMMSVLC SHKQMDVMFS KGAPESIIAR CNKILCNGDG SVVPLTAAGR
AELESRFYSF GDETLRCLAL AFKTVPHGQQ TISYDNENDL TFIGLVGMLD PPREEVRDAM
LACMTAGIRV IVVTGDNKST AESLCRKIGA FDNLVDFSGM SYTASEFERL PAVQQTLALR
RMTLFSRVEP SHKRMLVEAL QKQNEVVAMT GDGVNDAPAL KKADIGIAMG SGTAVAKSAS
DMVLADDNFA SIVAAVAEGR AIYNNTKQFI RYMISSNIGE VVCIFVAAVL GIPDTLAPVQ
LLWVNLVTDG LPATAIGFNK QDSDVMKAKP RKVGEAVVTG WLFFRYLVIG VYVGLATVAG
FIWWFVYSDG GPKLTYSELM NFETCALRET TYPCSIFEDR HPSTVAMTVL VVVEMFNALN
NLSENQSLLV ITPRSNLWLV GSIILTMLLH VLILYVHPLA VLFSVTPLSW AEWTAVLYLS
FPVIIIDELL KFLSRNTGMR FRFRLRKADL LPKDRRDK
