ID ASD_ARATH Reviewed; 514 AA.
AC Q9FLD5;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 145.
DE RecName: Full=AAA-ATPase ASD, mitochondrial;
DE EC=3.6.1.- {ECO:0000269|PubMed:21359673};
DE AltName: Full=AAA-ATPase 1;
DE AltName: Full=Protein ATPASE-IN-SEED-DEVELOPMENT {ECO:0000303|PubMed:21359673};
GN Name=AATP1; Synonyms=ASD {ECO:0000303|PubMed:21359673};
GN OrderedLocusNames=At5g40010 {ECO:0000312|EMBL:AED94501.1};
GN ORFNames=MYH19.21 {ECO:0000312|EMBL:BAB10225.1};
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=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
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 FUNCTION, MUTAGENESIS OF LYS-256, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP INDUCTION BY ABIOTIC STRESSES, SUBCELLULAR LOCATION, AND COFACTOR.
RC STRAIN=cv. Columbia;
RX PubMed=21359673; DOI=10.1007/s10059-011-0048-0;
RA Baek K., Seo P.J., Park C.-M.;
RT "Activation of a mitochondrial ATPase gene induces abnormal seed
RT development in Arabidopsis.";
RL Mol. Cells 31:361-369(2011).
CC -!- FUNCTION: Required to regulate morphology and anatomy during seed
CC maturation. {ECO:0000269|PubMed:21359673}.
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:0000269|PubMed:21359673};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:21359673};
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000269|PubMed:21359673}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in seeds, specifically in the embryo.
CC {ECO:0000269|PubMed:21359673}.
CC -!- DEVELOPMENTAL STAGE: Accumulates gradually in the embryo during the
CC seed development to reach high levels in mature seeds, but repressed
CC rapidly in germinating seeds. {ECO:0000269|PubMed:21359673}.
CC -!- INDUCTION: Induced by abscisic acid (ABA) and abiotic stresses, such as
CC drought, cold, and salt stresses, in an abscisic acid (ABA)- dependent
CC manner. {ECO:0000269|PubMed:21359673}.
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; AB010077; BAB10225.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94501.1; -; Genomic_DNA.
DR RefSeq; NP_198817.1; NM_123364.2.
DR AlphaFoldDB; Q9FLD5; -.
DR STRING; 3702.Q9FLD5; -.
DR TCDB; 3.A.28.1.3; the aaa-atpase, bcs1 (bcs1) family.
DR iPTMnet; Q9FLD5; -.
DR PaxDb; 3702-AT5G40010-1; -.
DR ProteomicsDB; 246945; -.
DR EnsemblPlants; AT5G40010.1; AT5G40010.1; AT5G40010.
DR GeneID; 833998; -.
DR Gramene; AT5G40010.1; AT5G40010.1; AT5G40010.
DR KEGG; ath:AT5G40010; -.
DR Araport; AT5G40010; -.
DR TAIR; AT5G40010; AATP1.
DR eggNOG; KOG0743; Eukaryota.
DR HOGENOM; CLU_010189_0_1_1; -.
DR InParanoid; Q9FLD5; -.
DR OMA; MVQRHVP; -.
DR OrthoDB; 819832at2759; -.
DR PhylomeDB; Q9FLD5; -.
DR PRO; PR:Q9FLD5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FLD5; baseline and differential.
DR Genevisible; Q9FLD5; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:TAIR.
DR GO; GO:0010154; P:fruit development; IMP:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR GO; GO:0009409; P:response to cold; IEP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IEP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
DR GO; GO:0010431; P:seed maturation; IMP:TAIR.
DR CDD; cd19510; RecA-like_BCS1; 1.
DR Gene3D; 6.10.280.40; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR025753; AAA_N_dom.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23070:SF128; AAA-ATPASE ASD, MITOCHONDRIAL; 1.
DR PANTHER; PTHR23070; BCS1 AAA-TYPE ATPASE; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF14363; AAA_assoc; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Hydrolase; Magnesium; Membrane; Mitochondrion;
KW Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..514
FT /note="AAA-ATPase ASD, mitochondrial"
FT /id="PRO_0000434701"
FT TRANSMEM 7..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 311..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..341
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 250..257
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 256
FT /note="K->A,R: Impaired ATPase activity."
FT /evidence="ECO:0000269|PubMed:21359673"
SQ SEQUENCE 514 AA; 60348 MW; FF9E0C8D5E11BDBD CRC64;
MVKMGEVWTN TGSALASLVF IYTIFERFFP YRLREHFEPL AQSLIGFIYP YIQITFHEYS
GERFKRSDVY DAIQSYLSKD SSSRAKKLTA NTIKGNKSII LSMDDHEEIT DEFQGVKVWW
QSKKHQSESR AISFYPKADE SRFYMLKFHR RDREVITKKY LNHVISEGKT IEVKNRERKL
YSNNPSQNWS GYKQTKWSHV TFEHPATFDT LAMEYKKKEE IKNDLIKFSN SKDYYKKIGK
AWKRGYLLFG PPGTGKSTMI AAMANLLEYD VYDLELTTVK DNTELRRLLI ETSGKSIIVI
EDIDCSLDLT GQRKQKKDEE EDEDETSPIE KQMKKDQGEN KGSKVTLSGL LNFIDGLWSA
CGGERIIVFT TNFIDKLDPA LIRKGRMDKH IEMSYCGFEA FKVLANNYLD AKEEDDNELF
DEIKRLLEVE EIKMTPADVG ENLLKKSEVE TKEICLKRLI EALKEEKEEA KRRIEDEEKK
KKEEEEIKRK KREEKKIKKE EKEEKEENET TMKD
//
