ACA2_ARATH
ID ACA2_ARATH Reviewed; 1014 AA.
AC O81108;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Calcium-transporting ATPase 2, plasma membrane-type;
DE EC=7.2.2.10;
DE AltName: Full=Ca(2+)-ATPase isoform 2;
GN Name=ACA2; OrderedLocusNames=At4g37640; ORFNames=F19F18.130;
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 CALMODULIN-BINDING DOMAIN.
RC STRAIN=cv. Columbia;
RX PubMed=9422775; DOI=10.1074/jbc.273.2.1099;
RA Harper J.F., Hong B., Hwang I., Guo H.Q., Stoddard R., Huang J.F.,
RA Palmgren M.G., Sze H.;
RT "A novel calmodulin-regulated Ca2+-ATPase (ACA2) from Arabidopsis with an
RT N-terminal autoinhibitory domain.";
RL J. Biol. Chem. 273:1099-1106(1998).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP PHOSPHORYLATION AT SER-45 BY CPK1.
RX PubMed=10823962; DOI=10.1073/pnas.97.11.6224;
RA Hwang I., Sze H., Harper J.F.;
RT "A calcium-dependent protein kinase can inhibit a calmodulin-stimulated
RT Ca2+ pump (ACA2) located in the endoplasmic reticulum of Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:6224-6229(2000).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of
CC ATP coupled with the translocation of calcium from the cytosol into the
CC endoplasmic reticulum.
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.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein.
CC -!- DOMAIN: The N-terminus contains an autoinhibitory calmodulin-binding
CC domain, which binds calmodulin in a calcium-dependent fashion.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIB subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF025842; AAC26997.1; -; mRNA.
DR EMBL; AL035605; CAB38303.1; -; Genomic_DNA.
DR EMBL; AL161591; CAB80429.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86819.1; -; Genomic_DNA.
DR EMBL; AY062484; AAL32562.1; -; mRNA.
DR PIR; T04721; T04721.
DR RefSeq; NP_195479.1; NM_119927.3.
DR PDB; 2M7E; NMR; -; A=20-45.
DR PDBsum; 2M7E; -.
DR AlphaFoldDB; O81108; -.
DR BMRB; O81108; -.
DR SMR; O81108; -.
DR BioGRID; 15199; 6.
DR IntAct; O81108; 2.
DR STRING; 3702.AT4G37640.1; -.
DR TCDB; 3.A.3.2.12; the p-type atpase (p-atpase) superfamily.
DR iPTMnet; O81108; -.
DR PaxDb; O81108; -.
DR PRIDE; O81108; -.
DR ProteomicsDB; 244631; -.
DR EnsemblPlants; AT4G37640.1; AT4G37640.1; AT4G37640.
DR GeneID; 829918; -.
DR Gramene; AT4G37640.1; AT4G37640.1; AT4G37640.
DR KEGG; ath:AT4G37640; -.
DR Araport; AT4G37640; -.
DR TAIR; locus:2120096; AT4G37640.
DR eggNOG; KOG0204; Eukaryota.
DR HOGENOM; CLU_002360_9_2_1; -.
DR InParanoid; O81108; -.
DR OMA; GECLVIA; -.
DR OrthoDB; 115892at2759; -.
DR PhylomeDB; O81108; -.
DR BioCyc; ARA:AT4G37640-MON; -.
DR BioCyc; MetaCyc:MON-14659; -.
DR PRO; PR:O81108; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O81108; baseline and differential.
DR Genevisible; O81108; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA: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:0016020; C:membrane; IDA: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:0015085; F:calcium ion transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0005516; F:calmodulin binding; IDA:TAIR.
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:0070588; P:calcium ion transmembrane transport; IDA: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; 3.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Calcium; Calcium transport;
KW Calmodulin-binding; Endoplasmic reticulum; Ion transport; Magnesium;
KW Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..1014
FT /note="Calcium-transporting ATPase 2, plasma membrane-type"
FT /id="PRO_0000046411"
FT TOPO_DOM 1..160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..199
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..348
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 369..398
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..416
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 417..810
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 811..829
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 830..840
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 841..861
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 862..881
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 882..904
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 905..916
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 917..938
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 939..956
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 957..978
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 979..988
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 989..1010
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1011..1014
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 20..31
FT /note="Interaction with calmodulin"
FT ACT_SITE 454
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 755
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 759
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:0007744|PubMed:22223895"
FT MOD_RES 45
FT /note="Phosphoserine; by CPK1"
FT /evidence="ECO:0000269|PubMed:10823962"
FT HELIX 22..31
FT /evidence="ECO:0007829|PDB:2M7E"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:2M7E"
SQ SEQUENCE 1014 AA; 110439 MW; 996DEFD26AFE9F03 CRC64;
MESYLNENFD VKAKHSSEEV LEKWRNLCGV VKNPKRRFRF TANLSKRYEA AAMRRTNQEK
LRIAVLVSKA AFQFISGVSP SDYTVPEDVK AAGFEICADE LGSIVESHDV KKLKFHGGVD
GLAGKLKASP TDGLSTEAAQ LSQRQELFGI NKFAESEMRG FWVFVWEALQ DMTLMILGVC
AFVSLIVGIA TEGWPKGSHD GLGIAASILL VVFVTATSDY RQSLQFRDLD KEKKKITVQV
TRNGFRQKLS IYDLLPGDIV HLAIGDQVPA DGLFLSGFSV VIDESSLTGE SEPVMVNAQN
PFLMSGTKVQ DGSCKMMITT VGMRTQWGKL MATLTEGGDD ETPLQVKLNG VATIIGKIGL
FFAVVTFAVL VQGMFMRKLS TGTHWVWSGD EALELLEYFA IAVTIVVVAV PEGLPLAVTL
SLAFAMKKMM NDKALVRHLA ACETMGSATT ICSDKTGTLT TNHMTVVKSC ICMNVQDVAN
KGSSLQSEIP ESAVKLLIQS IFNNTGGEVV VNKHGKTELL GTPTETAILE LGLSLGGKFQ
EERKSYKVIK VEPFNSTKKR MGVVIELPEG GRMRAHTKGA SEIVLAACDK VVNSSGEVVP
LDEESIKYLN VTINEFANEA LRTLCLAYMD IEGGFSPDDA IPASGFTCVG IVGIKDPVRP
GVKESVELCR RAGITVRMVT GDNINTAKAI ARECGILTDD GIAIEGPVFR EKNQEELLEL
IPKIQVMARS SPMDKHTLVK QLRTTFDEVV AVTGDGTNDA PALHEADIGL AMGIAGTEVA
KESADVIILD DNFSTIVTVA KWGRSVYINI QKFVQFQLTV NVVALVVNFS SACLTGSAPL
TAVQLLWVNM IMDTLGALAL ATEPPNDELM KRLPVGRRGN FITNAMWRNI LGQAVYQFIV
IWILQAKGKA MFGLDGPDST LMLNTLIFNC FVFCQVFNEI SSREMEEIDV FKGILDNYVF
VVVIGATVFF QIIIIEFLGT FASTTPLTIT QWIFSIFIGF LGMPIAAGLK TIPV
