ACA9_ARATH
ID ACA9_ARATH Reviewed; 1086 AA.
AC Q9LU41; Q0WUD3;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Calcium-transporting ATPase 9, plasma membrane-type;
DE EC=7.2.2.10;
DE AltName: Full=Ca(2+)-ATPase isoform 9;
GN Name=ACA9; OrderedLocusNames=At3g21180; ORFNames=MXL8.3;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB01709.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB023045; BAB01709.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002686; AEE76473.1; -; Genomic_DNA.
DR EMBL; AK227228; BAE99265.1; -; mRNA.
DR RefSeq; NP_188755.2; NM_113013.5.
DR AlphaFoldDB; Q9LU41; -.
DR SMR; Q9LU41; -.
DR STRING; 3702.AT3G21180.1; -.
DR TCDB; 3.A.3.2.14; the p-type atpase (p-atpase) superfamily.
DR iPTMnet; Q9LU41; -.
DR PaxDb; Q9LU41; -.
DR PRIDE; Q9LU41; -.
DR ProteomicsDB; 244562; -.
DR EnsemblPlants; AT3G21180.1; AT3G21180.1; AT3G21180.
DR GeneID; 821671; -.
DR Gramene; AT3G21180.1; AT3G21180.1; AT3G21180.
DR KEGG; ath:AT3G21180; -.
DR Araport; AT3G21180; -.
DR TAIR; locus:2094726; AT3G21180.
DR eggNOG; KOG0204; Eukaryota.
DR HOGENOM; CLU_002360_3_0_1; -.
DR InParanoid; Q9LU41; -.
DR OMA; HENHAHA; -.
DR OrthoDB; 115892at2759; -.
DR PhylomeDB; Q9LU41; -.
DR BioCyc; ARA:AT3G21180-MON; -.
DR PRO; PR:Q9LU41; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LU41; baseline and differential.
DR Genevisible; Q9LU41; 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:0016020; C:membrane; HDA:TAIR.
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; 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:0009567; P:double fertilization forming a zygote and endosperm; IMP: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 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 2: Evidence at transcript 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..1086
FT /note="Calcium-transporting ATPase 9, plasma membrane-type"
FT /id="PRO_0000046415"
FT TOPO_DOM 1..194
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..233
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..382
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 383..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 403..439
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 440..457
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 458..857
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 858..876
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 877..887
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 888..908
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 909..928
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 929..951
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 952..963
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 964..988
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 989..1006
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1007..1028
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1029..1038
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1039..1060
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1061..1086
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..68
FT /note="Interaction with calmodulin"
FT /evidence="ECO:0000250"
FT COMPBIAS 20..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 495
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 802
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 806
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1086 AA; 118768 MW; EC317264EE1C3098 CRC64;
MSTSSSNGLL LTSMSGRHDD MEAGSAKTEE HSDHEELQHD PDDPFDIDNT KNASVESLRR
WRQAALVLNA SRRFRYTLDL NKEEHYDNRR RMIRAHAQVI RAALLFKLAG EQQIAFGSST
PAASTGNFDI DLEKLVSMTR NQNMSNLQQY GGVKGVAEKL KSNMEQGINE DEKEVIDRKN
AFGSNTYPKK KGKNFFMFLW EAWQDLTLII LIIAAVTSLA LGIKTEGLKE GWLDGGSIAF
AVLLVIVVTA VSDYRQSLQF QNLNDEKRNI QLEVMRGGRT VKISIYDVVV GDVIPLRIGD
QVPADGVLIS GHSLAIDESS MTGESKIVHK DQKSPFLMSG CKVADGVGNM LVTGVGINTE
WGLLMASISE DTGEETPLQV RLNGLATFIG IVGLSVALVV LVALLVRYFT GTTQDTNGAT
QFIKGTTSIS DIVDDCVKIF TIAVTIVVVA VPEGLPLAVT LTLAYSMRKM MADKALVRRL
SACETMGSAT TICSDKTGTL TLNQMTVVET YAGGSKMDVA DNPSGLHPKL VALISEGVAQ
NTTGNIFHPK DGGEVEISGS PTEKAILSWA YKLGMKFDTI RSESAIIHAF PFNSEKKRGG
VAVLRGDSEV FIHWKGAAEI VLACCTQYMD SNGTLQSIES QKEFFRVAID SMAKNSLRCV
AIACRTQELN QVPKEQEDLD KWALPEDELI LLAIVGIKDP CRPGVREAVR ICTSAGVKVR
MVTGDNLQTA KAIALECGIL SSDTEAVEPT IIEGKVFREL SEKEREQVAK KITVMGRSSP
NDKLLLVQAL RKNGDVVAVT GDGTNDAPAL HEADIGLSMG ISGTEVAKES SDIIILDDNF
ASVVKVVRWG RSVYANIQKF IQFQLTVNVA ALIINVVAAM SSGDVPLKAV QLLWVNLIMD
TLGALALATE PPTDHLMHRT PVGRREPLIT NIMWRNLLVQ SFYQVAVLLV LNFAGLSILG
LNHENHAHAV EVKNTMIFNA FVMCQIFNEF NARKPDEMNV FRGVNKNPLF VAIVGVTFIL
QIIIVTFLGK FAHTVRLGWQ LWLASIIIGL VSWPLAIVGK LIPVPKTPMS VYFKKPFRKY
KASRNA
