ECA4_ARATH
ID ECA4_ARATH Reviewed; 1061 AA.
AC Q9XES1; Q9LQP2;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Calcium-transporting ATPase 4, endoplasmic reticulum-type;
DE EC=7.2.2.10;
GN Name=ECA4; OrderedLocusNames=At1g07670; ORFNames=F24B9.24;
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=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 [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 [MRNA] OF 283-1061.
RC STRAIN=cv. Columbia;
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 [4]
RP INDUCTION BY CADMIUM.
RC STRAIN=cv. Columbia;
RX PubMed=16502469; DOI=10.1002/pmic.200500543;
RA Sarry J.-E., Kuhn L., Ducruix C., Lafaye A., Junot C., Hugouvieux V.,
RA Jourdain A., Bastien O., Fievet J.B., Vailhen D., Amekraz B., Moulin C.,
RA Ezan E., Garin J., Bourguignon J.;
RT "The early responses of Arabidopsis thaliana cells to cadmium exposure
RT explored by protein and metabolite profiling analyses.";
RL Proteomics 6:2180-2198(2006).
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.
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 -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- INDUCTION: Induced by cadmium. {ECO:0000269|PubMed:16502469}.
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; AC007583; AAF75088.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28160.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58604.1; -; Genomic_DNA.
DR EMBL; AF117125; AAD29957.1; -; mRNA.
DR PIR; F86211; F86211.
DR PIR; T52332; T52332.
DR RefSeq; NP_001321027.1; NM_001331716.1.
DR RefSeq; NP_172246.3; NM_100640.4.
DR AlphaFoldDB; Q9XES1; -.
DR SMR; Q9XES1; -.
DR BioGRID; 22521; 1.
DR STRING; 3702.AT1G07670.1; -.
DR SwissPalm; Q9XES1; -.
DR PaxDb; Q9XES1; -.
DR PRIDE; Q9XES1; -.
DR ProteomicsDB; 222047; -.
DR EnsemblPlants; AT1G07670.1; AT1G07670.1; AT1G07670.
DR EnsemblPlants; AT1G07670.2; AT1G07670.2; AT1G07670.
DR GeneID; 837280; -.
DR Gramene; AT1G07670.1; AT1G07670.1; AT1G07670.
DR Gramene; AT1G07670.2; AT1G07670.2; AT1G07670.
DR KEGG; ath:AT1G07670; -.
DR Araport; AT1G07670; -.
DR TAIR; locus:2026555; AT1G07670.
DR eggNOG; KOG0202; Eukaryota.
DR HOGENOM; CLU_002360_3_2_1; -.
DR InParanoid; Q9XES1; -.
DR OMA; GQHYVAS; -.
DR OrthoDB; 100699at2759; -.
DR PhylomeDB; Q9XES1; -.
DR BioCyc; ARA:AT1G07670-MON; -.
DR BRENDA; 7.2.2.10; 399.
DR PRO; PR:Q9XES1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9XES1; baseline and differential.
DR Genevisible; Q9XES1; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005388; F:P-type calcium transporter activity; ISS: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:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:0034220; P:ion transmembrane transport; 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; 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 2: Evidence at transcript level;
KW ATP-binding; Calcium; Calcium transport; Ion transport; Magnesium;
KW Membrane; Metal-binding; Nucleotide-binding; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1061
FT /note="Calcium-transporting ATPase 4, endoplasmic
FT reticulum-type"
FT /id="PRO_0000046408"
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 REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 CONFLICT 314
FT /note="P -> H (in Ref. 3; AAD29957)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="T -> M (in Ref. 3; AAD29957)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="M -> S (in Ref. 3; AAD29957)"
FT /evidence="ECO:0000305"
FT CONFLICT 659
FT /note="T -> I (in Ref. 3; AAD29957)"
FT /evidence="ECO:0000305"
FT CONFLICT 859
FT /note="T -> P (in Ref. 3; AAD29957)"
FT /evidence="ECO:0000305"
FT CONFLICT 1046
FT /note="G -> V (in Ref. 3; AAD29957)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1061 AA; 116180 MW; 55B6126E5D539822 CRC64;
MGKGGEDCGN KQTNSSELVK SDTFPAWGKD VSECEEKFGV SREKGLSTDE 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
RDGKIEDWPT GRMDANLQMI AKIAAICNDA NVEKSDQQFV SRGMPTEAAL KVLVEKMGFP
EGLNEASSDG NVLRCCRLWS ELEQRIATLE FDRDRKSMGV MVDSSSGKKL LLVKGAVENV
LERSTHIQLL DGSTRELDQY SRDLILQSLH DMSLSALRCL GFAYSDVPSD FATYDGSEDH
PAHQQLLNPS NYSSIESNLV FVGFVGLRDP PRKEVRQAIA DCRTAGIRVM VITGDNKSTA
EAICREIGVF EADEDISSRS LTGKEFMDVK DQKNHLRQTG GLLFSRAEPK HKQEIVRLLK
EDGEVVAMTG DGVNDAPALK LADIGVAMGI SGTEVAKEAS DLVLADDNFS TIVAAVGEGR
SIYNNMKAFI RYMISSNIGE VASIFLTAAL GIPEGMIPVQ LLWVNLVTDG PPATALGFNP
PDKDIMKKPP RRSDDSLITA WILFRYMVIG LYVGVATVGV FIIWYTHNSF MGIDLSQDGH
SLVSYSQLAH WGQCSSWEGF KVSPFTAGSQ TFSFDSNPCD YFQQGKIKAS TLSLSVLVAI
EMFNSLNALS EDGSLVTMPP WVNPWLLLAM AVSFGLHFVI LYVPFLAQVF GIVPLSLNEW
LLVLAVSLPV ILIDEVLKFV GRCTSGYRYS PRTPSAKQKE E
