ACA7_ARATH
ID ACA7_ARATH Reviewed; 1015 AA.
AC O64806;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Putative calcium-transporting ATPase 7, plasma membrane-type;
DE EC=7.2.2.10;
DE AltName: Full=Ca(2+)-ATPase isoform 7;
GN Name=ACA7; OrderedLocusNames=At2g22950; ORFNames=T20K9.16;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 -!- 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; AC004401; AAF18608.2; -; Genomic_DNA.
DR EMBL; AC004786; AAM15005.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07380.1; -; Genomic_DNA.
DR PIR; H84618; H84618.
DR RefSeq; NP_179879.1; NM_127860.2.
DR AlphaFoldDB; O64806; -.
DR SMR; O64806; -.
DR BioGRID; 2179; 1.
DR STRING; 3702.AT2G22950.1; -.
DR iPTMnet; O64806; -.
DR PaxDb; O64806; -.
DR PRIDE; O64806; -.
DR ProteomicsDB; 244379; -.
DR EnsemblPlants; AT2G22950.1; AT2G22950.1; AT2G22950.
DR GeneID; 816826; -.
DR Gramene; AT2G22950.1; AT2G22950.1; AT2G22950.
DR KEGG; ath:AT2G22950; -.
DR Araport; AT2G22950; -.
DR TAIR; locus:2059201; AT2G22950.
DR eggNOG; KOG0204; Eukaryota.
DR HOGENOM; CLU_002360_9_2_1; -.
DR InParanoid; O64806; -.
DR OMA; NFASACV; -.
DR OrthoDB; 115892at2759; -.
DR PhylomeDB; O64806; -.
DR BioCyc; ARA:AT2G22950-MON; -.
DR PRO; PR:O64806; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64806; baseline and differential.
DR Genevisible; O64806; AT.
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:0005886; C:plasma 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: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:0009555; P:pollen 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; 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 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; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW Acetylation; ATP-binding; Calcium; Calcium transport; Calmodulin-binding;
KW Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1015
FT /note="Putative calcium-transporting ATPase 7, plasma
FT membrane-type"
FT /id="PRO_0000046413"
FT TOPO_DOM 1..161
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 183..200
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..349
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..369
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 370..399
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 400..417
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 418..811
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 812..830
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 831..841
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 842..862
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 863..882
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 883..905
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 906..917
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 918..939
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 940..957
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 958..979
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 980..989
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 990..1011
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1012..1015
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 20..31
FT /note="Interaction with calmodulin"
FT /evidence="ECO:0000250"
FT ACT_SITE 455
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 756
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 760
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:0000250|UniProtKB:O81108"
FT MOD_RES 45
FT /note="Phosphoserine; by CPK"
FT /evidence="ECO:0000250|UniProtKB:O81108"
SQ SEQUENCE 1015 AA; 110773 MW; 57DEE2028316CFC0 CRC64;
MESYLNSNFD VKAKHSSEEV LEKWRNLCSV VKNPKRRFRF TANLSKRYEA AAMRRTNQEK
LRIAVLVSKA AFQFISGVSP SDYKVPEEVK AAGFDICADE LGSIVEGHDV KKLKFHGGVD
GLSGKLKACP NAGLSTGEPE QLSKRQELFG INKFAESELR SFWVFVWEAL QDMTLMILGV
CAFVSLIVGI ATEGWPQGSH DGLGIVASIL LVVFVTATSD YRQSLQFRDL DKEKKKITVQ
VTRNGFRQKM SIYDLLPGDV VHLAIGDQVP ADGLFLSGFS VVIDESSLTG ESEPVMVTAQ
NPFLLSGTKV QDGSCKMLVT TVGMRTQWGK LMATLSEGGD DETPLQVKLN GVATIIGKIG
LSFAIVTFAV LVQGMFMRKL SLGPHWWWSG DDALELLEYF AIAVTIVVVA VPEGLPLAVT
LSLAFAMKKM MNDKALVRHL AACETMGSAT TICSDKTGTL TTNHMTVVKS CICMNVQDVA
SKSSSLQSDI PEAALKLLLQ LIFNNTGGEV VVNERGKTEI LGTPTETAIL ELGLSLGGKF
QEERQSNKVI KVEPFNSTKK RMGVVIELPE GGRIRAHTKG ASEIVLAACD KVINSSGEVV
PLDDESIKFL NVTIDEFANE ALRTLCLAYM DIESGFSADE GIPEKGFTCI GIVGIKDPVR
PGVRESVELC RRAGIMVRMV TGDNINTAKA IARECGILTD DGIAIEGPVF REKNQEEMLE
LIPKIQVMAR SSPMDKHTLV KQLRTTFDEV VAVTGDGTND APALHEADIG LAMGIAGTEV
AKEIADVIIL DDNFSTIVTV AKWGRSVYIN IQKFVQFQLT VNVVALIVNF SSACLTGSAP
LTAVQLLWVN MIMDTLGALA LATEPPNNEL MKRMPVGRRG NFITNAMWRN ILGQAVYQFI
IIWILQAKGK SMFGLVGSDS TLVLNTLIFN CFVFCQVFNE VSSREMEEID VFKGILDNYV
FVVVIGATVF FQIIIIEFLG TFASTTPLTI VQWFFSIFVG FLGMPIAAGL KKIPV
