AATP1_ARATH
ID AATP1_ARATH Reviewed; 475 AA.
AC Q9LP11; Q7FLL4;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=AAA-ATPase At1g43910;
DE EC=3.6.1.- {ECO:0000250|UniProtKB:Q9FLD5};
GN OrderedLocusNames=At1g43910 {ECO:0000312|EMBL:AEE32007.1};
GN ORFNames=F9C16.7 {ECO:0000312|EMBL:AAF79688.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP INDUCTION BY POTASSIUM STARVATION.
RC STRAIN=cv. Wassilewskija-2;
RX PubMed=15489280; DOI=10.1104/pp.104.046672;
RA Hampton C.R., Bowen H.C., Broadley M.R., Hammond J.P., Mead A., Payne K.A.,
RA Pritchard J., White P.J.;
RT "Cesium toxicity in Arabidopsis.";
RL Plant Physiol. 136:3824-3837(2004).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=16648215; DOI=10.1104/pp.106.081240;
RA Che P., Lall S., Nettleton D., Howell S.H.;
RT "Gene expression programs during shoot, root, and callus development in
RT Arabidopsis tissue culture.";
RL Plant Physiol. 141:620-637(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-85, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q9FLD5};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9FLD5};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in developing shoots.
CC {ECO:0000269|PubMed:16648215}.
CC -!- INDUCTION: Accumulates in shoots and roots upon potassium-starvation.
CC {ECO:0000269|PubMed:15489280}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. BCS1 subfamily.
CC {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; AC022314; AAF79688.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32007.1; -; Genomic_DNA.
DR EMBL; AK118165; BAC42789.2; -; mRNA.
DR PIR; C96503; C96503.
DR RefSeq; NP_175058.1; NM_103518.4.
DR AlphaFoldDB; Q9LP11; -.
DR STRING; 3702.AT1G43910.1; -.
DR TCDB; 3.A.28.1.4; the aaa-atpase, bcs1 (bcs1) family.
DR iPTMnet; Q9LP11; -.
DR PaxDb; Q9LP11; -.
DR PRIDE; Q9LP11; -.
DR ProteomicsDB; 243274; -.
DR EnsemblPlants; AT1G43910.1; AT1G43910.1; AT1G43910.
DR GeneID; 840990; -.
DR Gramene; AT1G43910.1; AT1G43910.1; AT1G43910.
DR KEGG; ath:AT1G43910; -.
DR Araport; AT1G43910; -.
DR TAIR; locus:2037186; AT1G43910.
DR eggNOG; KOG0743; Eukaryota.
DR HOGENOM; CLU_010189_0_1_1; -.
DR InParanoid; Q9LP11; -.
DR OMA; IDEFEGM; -.
DR OrthoDB; 532729at2759; -.
DR PRO; PR:Q9LP11; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LP11; baseline and differential.
DR Genevisible; Q9LP11; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009506; C:plasmodesma; 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:0051365; P:cellular response to potassium ion starvation; IEP:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR025753; AAA_N_dom.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF14363; AAA_assoc; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Hydrolase; Magnesium; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..475
FT /note="AAA-ATPase At1g43910"
FT /id="PRO_0000434703"
FT TRANSMEM 11..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 306..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..475
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 246..253
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 85
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT CONFLICT 416
FT /note="L -> I (in Ref. 3; BAC42789)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 475 AA; 54238 MW; 57A6F607874A9B91 CRC64;
MATLYSQVPS VSAVFSLYTS FSAITMLFRT ILNEIVPKRI REYIAMKAVD FFSSYFQSDF
TFVIEQRWEF VENQTFRAAE VYLPTCLAGL STGKLLVGSS NLKNPAAEPK LGIPVNTKII
DNFEGIHLEW TLHSVETKKY LPEKRYFHLT CKKEFREKIM TDYFTYLAKS AEKIMSHREN
LKIYTYNQDR SKWESAIFEH HTTFETLAVE PDLKKTLIDD LDAFSKGKDF FKSVGRAWKR
GYLLYGPPGT GKSSMVAAIA NHMKYHIYDL QIQSVRDDGE LREILTSTKN RSILLIEDID
CGADASRRRQ SKKKEEDGGE DDGEPQKRKK KFEVGISLSG LLNFVDGLWS SCGEEKIIIF
TTNHKEKLDP ALLRPGRMDV HILMDNCTPF VFKKLVALYL KTDEHVLFDP IEKLILEVSS
TPAEVTQQLM ASKNADIALK GLAEFLENKK LKKGEDSSVE EEGEIEDAET KEAET
