ACA11_ARATH
ID ACA11_ARATH Reviewed; 1025 AA.
AC Q9M2L4;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Putative calcium-transporting ATPase 11, plasma membrane-type;
DE EC=7.2.2.10;
DE AltName: Full=Ca(2+)-ATPase isoform 11;
GN Name=ACA11; OrderedLocusNames=At3g57330; ORFNames=F28O9.180;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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).
CC -!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of
CC ATP coupled with the translocation of calcium from the cytosol out of
CC the cell or into organelles. {ECO:0000250}.
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. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9M2L4; P25854: CAM4; NbExp=2; IntAct=EBI-7522268, EBI-1235664;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- DOMAIN: The N-terminus contains an autoinhibitory calmodulin-binding
CC domain, which binds calmodulin in a calcium-dependent fashion.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIB subfamily. {ECO:0000305}.
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DR EMBL; AL137080; CAB68139.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79642.1; -; Genomic_DNA.
DR PIR; T45811; T45811.
DR RefSeq; NP_191292.1; NM_115593.7.
DR AlphaFoldDB; Q9M2L4; -.
DR SMR; Q9M2L4; -.
DR IntAct; Q9M2L4; 1.
DR MINT; Q9M2L4; -.
DR STRING; 3702.AT3G57330.1; -.
DR iPTMnet; Q9M2L4; -.
DR SwissPalm; Q9M2L4; -.
DR PaxDb; Q9M2L4; -.
DR PRIDE; Q9M2L4; -.
DR ProteomicsDB; 244539; -.
DR EnsemblPlants; AT3G57330.1; AT3G57330.1; AT3G57330.
DR GeneID; 824900; -.
DR Gramene; AT3G57330.1; AT3G57330.1; AT3G57330.
DR KEGG; ath:AT3G57330; -.
DR Araport; AT3G57330; -.
DR TAIR; locus:2082528; AT3G57330.
DR eggNOG; KOG0204; Eukaryota.
DR HOGENOM; CLU_002360_9_2_1; -.
DR InParanoid; Q9M2L4; -.
DR OrthoDB; 115892at2759; -.
DR PhylomeDB; Q9M2L4; -.
DR BioCyc; ARA:AT3G57330-MON; -.
DR PRO; PR:Q9M2L4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M2L4; baseline and differential.
DR Genevisible; Q9M2L4; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA: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:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009705; C:plant-type vacuole membrane; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005773; C: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:0019829; F:ATPase-coupled cation transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
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:0055081; P:anion homeostasis; IMP:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IGI:TAIR.
DR GO; GO:0043069; P:negative regulation of programmed cell death; IGI: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 ATP-binding; Calcium; Calcium transport; Calmodulin-binding; Ion transport;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1025
FT /note="Putative calcium-transporting ATPase 11, plasma
FT membrane-type"
FT /id="PRO_0000046417"
FT TOPO_DOM 1..157
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..196
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218..345
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..365
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 366..395
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 396..413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 414..801
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 802..820
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 821..831
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 832..852
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 853..872
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 873..895
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 896..907
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 908..929
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 930..947
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 948..969
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 970..979
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 980..1001
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1002..1025
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 19..30
FT /note="Interaction with calmodulin"
FT /evidence="ECO:0000305"
FT ACT_SITE 451
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 746
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 750
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1025 AA; 111945 MW; 5488C4046D7F308F CRC64;
MSNLLKDFEV ASKNPSLEAR QRWRSSVGLV KNRARRFRMI SNLDKLAENE KKRCQIQEKI
RVVFYVQKAA FQFIDAGARP EYKLTDEVKK AGFYVEADEL ASMVRNHDTK SLTKIGGPEG
IAQKVSVSLA EGVRSSELHI REKIYGENRY TEKPARSFLT FVWEALQDIT LIILMVCAVV
SIGVGVATEG FPKGMYDGTG ILLSIILVVM VTAISDYKQS LQFRDLDREK KKIIIQVTRD
GSRQEVSIHD LVVGDVVHLS IGDQVPADGI FISGYNLEID ESSLSGESEP SHVNKEKPFL
LSGTKVQNGS AKMLVTTVGM RTEWGKLMDT LSEGGEDETP LQVKLNGVAT IIGKIGLGFA
VLTFVVLCIR FVVEKATAGS ITEWSSEDAL TLLDYFAIAV TIIVVAVPEG LPLAVTLSLA
FAMKQLMSDR ALVRHLAACE TMGSSTCICT DKTGTLTTNH MVVNKVWICE NIKERQEENF
QLNLSEQVKN ILIQAIFQNT GSEVVKDKEG KTQILGSPTE RAILEFGLLL GGDVDTQRRE
HKILKIEPFN SDKKKMSVLT SHSGGKVRAF CKGASEIVLK MCEKVVDSNG ESVPLSEEKI
ASISDVIEGF ASEALRTLCL VYTDLDEAPR GDLPNGGYTL VAVVGIKDPV RPGVREAVQT
CQAAGITVRM VTGDNISTAK AIAKECGILT AGGVAIEGSD FRNLPPHEMR AILPKIQVMA
RSLPLDKHTL VNNLRKMGEV VAVTGDGTND APALHEADIG LAMGIAGTEV AKENADVIIM
DDNFATIVNV AKWGRAVYIN IQKFVQFQLT VNVVALIINF VSACITGSAP LTAVQLLWVN
MIMDTLGALA LATEPPNEGL MKRQPIGRTA SFITRAMWRN IIGQSIYQLI VLGILNFAGK
QILNLNGPDS TIVLNTIIFN SFVFCQVFNE VNSREIEKIN VFEGMFKSWV FVAVMTATVG
FQVIIVEFLG AFASTVPLSW QHWLLCILIG SVSMILAVGL KCIPVESNRH HDGYELLPSG
PSDSA
