ECA2_ARATH
ID ECA2_ARATH Reviewed; 1054 AA.
AC O23087;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Calcium-transporting ATPase 2, endoplasmic reticulum-type;
DE EC=7.2.2.10;
GN Name=ECA2; Synonyms=ACA5; OrderedLocusNames=At4g00900;
GN ORFNames=A_TM018A10.4;
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;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
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 -!- 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; AJ132387; CAA10659.1; -; mRNA.
DR EMBL; AF013294; AAB62850.1; -; Genomic_DNA.
DR EMBL; AL161472; CAB80899.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE81953.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67918.1; -; Genomic_DNA.
DR PIR; T01556; T01556.
DR RefSeq; NP_001329712.1; NM_001340276.1.
DR RefSeq; NP_191999.1; NM_116317.4.
DR AlphaFoldDB; O23087; -.
DR SMR; O23087; -.
DR BioGRID; 13275; 4.
DR IntAct; O23087; 2.
DR STRING; 3702.AT4G00900.1; -.
DR SwissPalm; O23087; -.
DR PaxDb; O23087; -.
DR PRIDE; O23087; -.
DR ProteomicsDB; 224716; -.
DR EnsemblPlants; AT4G00900.1; AT4G00900.1; AT4G00900.
DR EnsemblPlants; AT4G00900.2; AT4G00900.2; AT4G00900.
DR GeneID; 827984; -.
DR Gramene; AT4G00900.1; AT4G00900.1; AT4G00900.
DR Gramene; AT4G00900.2; AT4G00900.2; AT4G00900.
DR KEGG; ath:AT4G00900; -.
DR Araport; AT4G00900; -.
DR TAIR; locus:2134623; AT4G00900.
DR eggNOG; KOG0202; Eukaryota.
DR HOGENOM; CLU_002360_3_3_1; -.
DR InParanoid; O23087; -.
DR OMA; FISWDVV; -.
DR OrthoDB; 100699at2759; -.
DR PhylomeDB; O23087; -.
DR BioCyc; ARA:AT4G00900-MON; -.
DR BioCyc; MetaCyc:MON-14601; -.
DR BRENDA; 7.2.2.10; 399.
DR PRO; PR:O23087; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O23087; baseline and differential.
DR Genevisible; O23087; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; 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: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 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; Ion transport; Magnesium;
KW Membrane; Metal-binding; Nucleotide-binding; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1054
FT /note="Calcium-transporting ATPase 2, endoplasmic
FT reticulum-type"
FT /id="PRO_0000046406"
FT TOPO_DOM 1..53
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..98
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..262
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..282
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 283..312
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 331..782
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 783..802
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 803..812
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 813..833
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 834..853
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 854..876
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 877..949
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 950..969
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 970..982
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 983..1001
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1002..1016
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1017..1037
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1038..1054
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 368
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 321
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 322
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 324
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 326
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 727
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 731
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 793
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 796
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 821
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 824
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="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 960
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1054 AA; 115830 MW; B0D7F7237A3496AF CRC64;
MEEEKSFSAW SWSVEQCLKE YKTRLDKGLT SEDVQIRRQK YGFNELAKEK GKPLWHLVLE
QFDDTLVKIL LGAAFISFVL AFLGEEHGSG SGFEAFVEPF VIVLILILNA VVGVWQESNA
EKALEALKEM QCESAKVLRD GNVLPNLPAR ELVPGDIVEL NVGDKVPADM RVSGLKTSTL
RVEQSSLTGE AMPVLKGANL VVMDDCELQG KENMVFAGTT VVNGSCVCIV TSIGMDTEIG
KIQRQIHEAS LEESETPLKK KLDEFGSRLT TAICIVCVLV WMINYKNFVS WDVVDGYKPV
NIKFSFEKCT YYFKIAVALA VAAIPEGLPA VITTCLALGT RKMAQKNAIV RKLPSVETLG
CTTVICSDKT GTLTTNQMSA TEFFTLGGKT TTTRVFSVSG TTYDPKDGGI VDWGCNNMDA
NLQAVAEICS ICNDAGVFYE GKLFRATGLP TEAALKVLVE KMGIPEKKNS ENIEEVTNFS
DNGSSVKLAC CDWWNKRSKK VATLEFDRVR KSMSVIVSEP NGQNRLLVKG AAESILERSS
FAQLADGSLV ALDESSREVI LKKHSEMTSK GLRCLGLAYK DELGEFSDYS SEEHPSHKKL
LDPSSYSNIE TNLIFVGVVG LRDPPREEVG RAIEDCRDAG IRVMVITGDN KSTAEAICCE
IRLFSENEDL SQSSFTGKEF MSLPASRRSE ILSKSGGKVF SRAEPRHKQE IVRMLKEMGE
IVAMTGDGVN DAPALKLADI GIAMGITGTE VAKEASDMVL ADDNFSTIVS AVAEGRSIYN
NMKAFIRYMI SSNVGEVISI FLTAALGIPE CMIPVQLLWV NLVTDGPPAT ALGFNPADID
IMKKPPRKSD DCLIDSWVLI RYLVIGSYVG VATVGIFVLW YTQASFLGIS LISDGHTLVS
FTQLQNWSEC SSWGTNFTAT PYTVAGGLRT IAFENNPCDY FTLGKVKPMT LSLTVLVAIE
MFNSLNALSE DNSLLTMPPW RNPWLLVAMT VSFALHCVIL YVPFLANVFG IVPLSFREWF
VVILVSFPVI LIDEALKFIG RCRRTRIKKK IKTM
