ATAD3_CAEEL
ID ATAD3_CAEEL Reviewed; 595 AA.
AC Q20748;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=ATPase family AAA domain-containing protein 3;
GN Name=atad-3 {ECO:0000312|WormBase:F54B3.3};
GN ORFNames=F54B3.3 {ECO:0000312|WormBase:F54B3.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=19888333; DOI=10.1371/journal.pone.0007644;
RA Hoffmann M., Bellance N., Rossignol R., Koopman W.J., Willems P.H.,
RA Mayatepek E., Bossinger O., Distelmaier F.;
RT "C. elegans ATAD-3 is essential for mitochondrial activity and
RT development.";
RL PLoS ONE 4:E7644-E7644(2009).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 592-GLU--VAL-595.
RX PubMed=22245785; DOI=10.1016/j.exger.2011.12.011;
RA Hoffmann M., Honnen S., Mayatepek E., Waetjen W., Koopman W.J.,
RA Bossinger O., Distelmaier F.;
RT "MICS-1 interacts with mitochondrial ATAD-3 and modulates lifespan in C.
RT elegans.";
RL Exp. Gerontol. 47:270-275(2012).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26427876; DOI=10.1016/j.bbrc.2015.09.143;
RA van den Ecker D., Hoffmann M., Mueting G., Maglioni S., Herebian D.,
RA Mayatepek E., Ventura N., Distelmaier F.;
RT "Caenorhabditis elegans ATAD-3 modulates mitochondrial iron and heme
RT homeostasis.";
RL Biochem. Biophys. Res. Commun. 467:389-394(2015).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF 592-GLU--VAL-595.
RX PubMed=27506200; DOI=10.1186/s12915-016-0286-x;
RA Waaijers S., Munoz J., Berends C., Ramalho J.J., Goerdayal S.S., Low T.Y.,
RA Zoumaro-Djayoon A.D., Hoffmann M., Koorman T., Tas R.P., Harterink M.,
RA Seelk S., Kerver J., Hoogenraad C.C., Bossinger O., Tursun B.,
RA van den Heuvel S., Heck A.J., Boxem M.;
RT "A tissue-specific protein purification approach in Caenorhabditis elegans
RT identifies novel interaction partners of DLG-1/Discs large.";
RL BMC Biol. 14:66-66(2016).
CC -!- FUNCTION: Essential for mitochondrial network organization,
CC mitochondrial metabolism and cell growth at organism and cellular level
CC (PubMed:19888333). Important during development for the up-regulation
CC of mitochondrial activity during the transition to higher larval stages
CC (PubMed:19888333). Regulates mitochondrial iron homeostasis
CC (PubMed:26427876). May play an important role in mitochondrial protein
CC synthesis (By similarity). May also participate in mitochondrial DNA
CC replication (By similarity). May bind to mitochondrial DNA D-loops and
CC contribute to nucleoid stability (By similarity). Plays a role in
CC regulating the production of reactive oxygen species in response to
CC heat stress (PubMed:22245785). {ECO:0000250|UniProtKB:Q9NVI7,
CC ECO:0000269|PubMed:19888333, ECO:0000269|PubMed:22245785,
CC ECO:0000269|PubMed:26427876}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:19888333}; Single-pass membrane protein
CC {ECO:0000269|PubMed:19888333}. Mitochondrion matrix, mitochondrion
CC nucleoid {ECO:0000250|UniProtKB:Q9NVI7}. Note=In the mitochondrial
CC inner membrane, enriched in sites with the potential to form contacts
CC with the outer membrane. The N-terminal domain interacts with the inner
CC surface of the mitochondrial outer membrane and the C-terminal domain
CC localizes in a specific matrix compartment, where it is associated with
CC nucleoids. {ECO:0000250|UniProtKB:Q9NVI7}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in an increased
CC adult lifespan (PubMed:22245785). RNAi-mediated knockdown at the L1
CC stage of larval development results in arrest in the majority of
CC animals at this larval stage (PubMed:19888333). Some surviving animals
CC arrest during the subsequent larval stages (PubMed:19888333). RNAi-
CC mediated knockdown in young adults results in a gradual decrease in the
CC reproduction rate over time whereby initially fewer embryos are
CC produced as compared to wild-type animals, and eventually adults fail
CC to reproduce (PubMed:19888333). The few embryos that are produced by
CC the young adults are viable, but animals arrest at the L1 larval stage
CC (PubMed:19888333). RNAi-mediated knockdown results in sufficient
CC mitochondrial function at the L1 larval stage, and no obvious changes
CC in mitochondrial mass (PubMed:19888333). However, RNAi-mediated
CC knockdown results in defects in mitochondrial activity and structure
CC characterized by reduced mitochondrial NADH-ubiquinone oxidoreductase
CC and citrate synthase activity compared to wild-type animals at later
CC stages of development, and a disorganized mitochondrial network with
CC thinner mitochondria (PubMed:19888333). RNAi-mediated knockdown results
CC in increased levels of reactive oxygen species as compared to wild-type
CC animals at 37 degrees Celsius (PubMed:22245785). RNAi-mediated
CC knockdown during early developmental stages and at the L3 larval stage
CC results in increased levels of iron and heme (PubMed:26427876). RNAi-
CC mediated knockdown in a mics-1 mutant background results in an enhanced
CC increase in adult lifespan as compared to the single mutants and wild-
CC type animals (PubMed:22245785). {ECO:0000269|PubMed:19888333,
CC ECO:0000269|PubMed:22245785, ECO:0000269|PubMed:26427876}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
CC -!- CAUTION: Has been shown to interact (via C-terminus) with mics-1 (via
CC PDZ domain) (PubMed:22245785). The physiological significance of this
CC interaction is uncertain; the mics-1 PDZ domain is expected to be in
CC the cytoplasm. {ECO:0000269|PubMed:22245785, ECO:0000305}.
CC -!- CAUTION: Has been shown to interact (via C-terminus) with dlg-1 (via
CC PDZ domain) (PubMed:22245785). The physiological significance of this
CC interaction is uncertain; the dlg-1 PDZ domain is expected to be in the
CC cytoplasm. {ECO:0000269|PubMed:27506200, ECO:0000305}.
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DR EMBL; Z48583; CAA88471.2; -; Genomic_DNA.
DR PIR; T22612; T22612.
DR RefSeq; NP_496210.2; NM_063809.6.
DR AlphaFoldDB; Q20748; -.
DR SMR; Q20748; -.
DR BioGRID; 39909; 8.
DR IntAct; Q20748; 2.
DR STRING; 6239.F54B3.3; -.
DR EPD; Q20748; -.
DR PaxDb; Q20748; -.
DR PeptideAtlas; Q20748; -.
DR EnsemblMetazoa; F54B3.3.1; F54B3.3.1; WBGene00010015.
DR GeneID; 174590; -.
DR KEGG; cel:CELE_F54B3.3; -.
DR UCSC; F54B3.3.1; c. elegans.
DR CTD; 174590; -.
DR WormBase; F54B3.3; CE35878; WBGene00010015; atad-3.
DR eggNOG; KOG0742; Eukaryota.
DR HOGENOM; CLU_011488_2_0_1; -.
DR InParanoid; Q20748; -.
DR OMA; KTCSKMA; -.
DR OrthoDB; 357201at2759; -.
DR PhylomeDB; Q20748; -.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR PRO; PR:Q20748; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00010015; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042645; C:mitochondrial nucleoid; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0007005; P:mitochondrion organization; IMP:WormBase.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR039188; ATAD3.
DR InterPro; IPR021911; ATAD3_N.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23075; PTHR23075; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF12037; DUF3523; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Mitochondrion nucleoid; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..595
FT /note="ATPase family AAA domain-containing protein 3"
FT /id="PRO_0000419288"
FT TOPO_DOM 1..243
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..595
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 80..107
FT /evidence="ECO:0000255"
FT COILED 140..175
FT /evidence="ECO:0000255"
FT MOTIF 592..595
FT /note="PDZ-binding"
FT /evidence="ECO:0000269|PubMed:22245785,
FT ECO:0000269|PubMed:27506200"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 349..356
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 592..595
FT /note="Missing: Increased incidence of embryonic lethality
FT and reduced fertility as compared to wild-type."
FT /evidence="ECO:0000269|PubMed:22245785,
FT ECO:0000269|PubMed:27506200"
SQ SEQUENCE 595 AA; 67147 MW; 5A7A2B44F46C4D23 CRC64;
MSWLFGVQKN ATPQIPDDFQ AGAAPGGPQQ PGQGQRQEGN SKMAYSFDST ALERAAKAAR
DLEKFPNAKE ALELSRMQEV TRQKEVENET KKIEAQLANM KSEHIRVAEE ERRKTLGEET
KHAHSRAEYQ DQLARKRAEE ELAMKARMQE ESLRKQEESV KKQEQLRKQT IEHELALKHK
YELEKIDAET RARAKAARDN RDVNLEQMKL HEEENRKTVI EKIKTSGELI GSGLNQFLND
KTKIAAAVGG LTALAVGWYT AKRGTGVTAR YIESRLGKPS LVRETSRITP LEVLKHPIKS
VQMMTRQKKD PLNGVVLPPA LERRLRDIAI TTSNTKRNNG LFRNVMFYGP PGTGKTLFAK
SLAQHSGLDY AVLTGGDIAP LGRDGVSAIH KVFDWASKSR KGLIVFIDEA DAFLQKRSKN
GMSEDTRAAL NAFLFRTGEQ SRKFMLVVAS NQPEQFDWAV NDRFDQLVEF TLPGMEERER
ILLQYFNEHI VTPATSGSRS QRLKLDNFDW VAKCNEVAKK TSGMSGRELS KLVIGWQASA
YASETGVLTE AIVDRNTADA MVQHEHKMEW LEKEQLKARN QEVKFGTTLK RETAV
