ACA13_ARATH
ID ACA13_ARATH Reviewed; 1017 AA.
AC Q9LIK7;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Putative calcium-transporting ATPase 13, plasma membrane-type;
DE EC=7.2.2.10;
DE AltName: Full=Ca(2+)-ATPase isoform 13;
GN Name=ACA13; OrderedLocusNames=At3g22910; ORFNames=F5N5.8;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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 -!- 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; AP001300; BAB03036.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76690.1; -; Genomic_DNA.
DR RefSeq; NP_188931.1; NM_113191.2.
DR AlphaFoldDB; Q9LIK7; -.
DR SMR; Q9LIK7; -.
DR BioGRID; 7195; 1.
DR STRING; 3702.AT3G22910.1; -.
DR iPTMnet; Q9LIK7; -.
DR PaxDb; Q9LIK7; -.
DR PRIDE; Q9LIK7; -.
DR ProteomicsDB; 244511; -.
DR EnsemblPlants; AT3G22910.1; AT3G22910.1; AT3G22910.
DR GeneID; 821863; -.
DR Gramene; AT3G22910.1; AT3G22910.1; AT3G22910.
DR KEGG; ath:AT3G22910; -.
DR Araport; AT3G22910; -.
DR TAIR; locus:2084578; AT3G22910.
DR eggNOG; KOG0204; Eukaryota.
DR HOGENOM; CLU_002360_9_2_1; -.
DR InParanoid; Q9LIK7; -.
DR OMA; CFTLYFA; -.
DR OrthoDB; 115892at2759; -.
DR PhylomeDB; Q9LIK7; -.
DR BioCyc; ARA:AT3G22910-MON; -.
DR PRO; PR:Q9LIK7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LIK7; baseline and differential.
DR Genevisible; Q9LIK7; 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: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 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; IPR006408; P-type_ATPase_IIB.
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 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 3: Inferred from homology;
KW Acetylation; ATP-binding; Calcium; Calcium transport; Calmodulin-binding;
KW Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..1017
FT /note="Putative calcium-transporting ATPase 13, plasma
FT membrane-type"
FT /id="PRO_0000046419"
FT TOPO_DOM 1..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..186
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..336
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 337..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 357..393
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 394..411
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 412..802
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 803..821
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 822..832
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 833..853
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 854..873
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 874..896
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 897..905
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 906..926
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 927..944
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 945..966
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 967..976
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 977..998
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 999..1002
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 20..31
FT /note="Interaction with calmodulin"
FT /evidence="ECO:0000305"
FT ACT_SITE 449
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 747
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 751
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"
SQ SEQUENCE 1017 AA; 112528 MW; 2F0265CCE8862916 CRC64;
MRRNVSDHAE KKDKVGVEVL LELPKTLSKS NKKWQLALIK LYCSRTLLNC AKHAIRKPGL
FPRSLSYTAI DLDHHHGDDH FKIDTETLND LVKNKNQEKL ESLGGPNGLV SALKSNTRLG
INEEGDEIQR RRSTFGSNTY TRQPSKGLFH FVVEAFKDLT ILILLGCATL SLGFGIKEHG
LKEGWYDGGS IFVAVFLVVA VSAVSNFRQN RQFDKLSKVS SNIKIDVVRN GRRQEISIFD
IVVGDIVCLN IGDQVPADGV FVEGHLLHVD ESSMTGESDH VEVSLTGNTF LFSGTKIADG
FGKMAVTSVG MNTAWGQMMS HISRDTNEQT PLQSRLDKLT SSIGKVGLLV AFLVLLVLLI
RYFTGTTKDE SGNREYNGKT TKSDEIVNAV VKMVAAAVTI IVVAIPEGLP LAVTLTLAYS
MKRMMKDNAM VRKLSACETM GSATVICTDK TGTLTLNQMK VTDFWFGLES GKASSVSQRV
VELFHQGVAM NTTGSVFKAK AGTEYEFSGS PTEKAILSWA VEELEMGMEK VIEEHDVVHV
EGFNSEKKRS GVLMKKKGVN TENNVVHWKG AAEKILAMCS TFCDGSGVVR EMKEDDKIQF
EKIIQSMAAK SLRCIAFAYS EDNEDNKKLK EEKLSLLGII GIKDPCRPGV KKAVEDCQFA
GVNIKMITGD NIFTARAIAV ECGILTPEDE MNSEAVLEGE KFRNYTQEER LEKVERIKVM
ARSSPFDKLL MVKCLKELGH VVAVTGDGTN DAPALKEADI GLSMGIQGTE VAKESSDIVI
LDDNFASVAT VLKWGRCVYN NIQKFIQFQL TVNVAALVIN FVAAVSAGDV PLTAVQLLWV
NLIMDTLGAL ALATEKPTND LMKKKPIGRV APLITNIMWR NLLAQAFYQI SVLLVLQFRG
RSIFNVTEKV KNTLIFNTFV LCQVFNEFNA RSLEKKNVFK GLHKNRLFIG IIVVTVVLQV
VMVEFLKRFA DTERLNLGQW GVCIAIAAAS WPIGWLVKSV PVPERHFFSY LKWKKRS
