ATAD3_MOUSE
ID ATAD3_MOUSE Reviewed; 591 AA.
AC Q925I1; A2AD89; Q3TA78; Q3UE74; Q69ZM7; Q8C6C6;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=ATPase family AAA domain-containing protein 3;
DE AltName: Full=AAA-ATPase TOB3;
GN Name=Atad3; Synonyms=Atad3a, Kiaa1273;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ;
RA Parng C., Piepenhagen P.A., Casanova J., Pillai S.;
RT "TOB3 is a novel AAA-ATPase involved in protein secretion.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Embryonic tail;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Bone marrow, Embryonic tail, Lung, Spleen, and Sympathetic ganglion;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, Colon, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 302-311 AND 478-485, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=12865426; DOI=10.1074/jbc.m304940200;
RA Da Cruz S., Xenarios I., Langridge J., Vilbois F., Parone P.A.,
RA Martinou J.-C.;
RT "Proteomic analysis of the mouse liver mitochondrial inner membrane.";
RL J. Biol. Chem. 278:41566-41571(2003).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=20332122; DOI=10.1242/jcs.062034;
RA Fang H.Y., Chang C.L., Hsu S.H., Huang C.Y., Chiang S.F., Chiou S.H.,
RA Huang C.H., Hsiao Y.T., Lin T.Y., Chiang I.P., Hsu W.H., Sugano S.,
RA Chen C.Y., Lin C.Y., Ko W.J., Chow K.C.;
RT "ATPase family AAA domain-containing 3A is a novel anti-apoptotic factor in
RT lung adenocarcinoma cells.";
RL J. Cell Sci. 123:1171-1180(2010).
RN [11]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-490, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-490; LYS-494 AND LYS-512, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Essential for mitochondrial network organization,
CC mitochondrial metabolism and cell growth at organism and cellular
CC level. May play an important role in mitochondrial protein synthesis.
CC May also participate in mitochondrial DNA replication. May bind to
CC mitochondrial DNA D-loops and contribute to nucleoid stability.
CC Required for enhanced channeling of cholesterol for hormone-dependent
CC steroidogenesis. Involved in mitochondrial-mediated antiviral innate
CC immunity. {ECO:0000250|UniProtKB:Q9NVI7}.
CC -!- SUBUNIT: Can form homooligomers. Homodimer formation at the N-terminus
CC may be regulated by ATP and is required for the interaction with the
CC inner surface of the mitochondrial outer membrane and correct
CC mitochondrial homeostasis. Interacts with components of the
CC mitochondrial ribosome and with other proteins involved in
CC mitochondrial RNA metabolism. May also interact with protein involved
CC in lipid metabolism, including STARD9. May interact with FAM210A.
CC Interacts with GADD45GIP1. Interacts with S100B in a Ca(+2)- and
CC Zn(+2)-dependent manner; this interaction probably occurs in the
CC cytosol prior to mitochondrial targeting. S100B could assist ATAD3A
CC cytoplasmic processing, preventing aggregation and favoring
CC mitochondrial localization. Interacts with HSP60/HSPD1. Forms
CC heterooligomers with ATAD3B; this interaction may affect ATAD3A
CC activity. Interacts with CLPB. {ECO:0000250|UniProtKB:Q9NVI7}.
CC -!- INTERACTION:
CC Q925I1; Q8K1M6: Dnm1l; NbExp=13; IntAct=EBI-772703, EBI-2365792;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}. Mitochondrion matrix,
CC mitochondrion nucleoid {ECO:0000250}. Note=In the mitochondrial inner
CC membrane, enriched in sites with the potential to form contacts with
CC 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 (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q925I1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q925I1-2; Sequence=VSP_015643;
CC -!- TISSUE SPECIFICITY: Expressed in heart, spleen, kidney, liver and at
CC smaller levels, in lung and muscle (at protein level).
CC {ECO:0000269|PubMed:20332122}.
CC -!- DOMAIN: The transmembrane domain and a C-terminal adjacent region
CC contain all information necessary for mitochondrial targeting.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; AF343079; AAK38648.1; -; mRNA.
DR EMBL; AK075921; BAC36055.1; -; mRNA.
DR EMBL; AK148974; BAE28707.1; -; mRNA.
DR EMBL; AK149702; BAE29037.1; -; mRNA.
DR EMBL; AK150037; BAE29259.1; -; mRNA.
DR EMBL; AK166099; BAE38570.1; -; mRNA.
DR EMBL; AK172038; BAE42791.1; -; mRNA.
DR EMBL; AK173141; BAD32419.1; -; Unassigned_RNA.
DR EMBL; AL670236; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466594; EDL15028.1; -; Genomic_DNA.
DR EMBL; BC023301; AAH23301.1; -; mRNA.
DR EMBL; BC058373; AAH58373.1; -; mRNA.
DR EMBL; BC060036; AAH60036.1; -; mRNA.
DR CCDS; CCDS19037.1; -. [Q925I1-1]
DR RefSeq; NP_849534.2; NM_179203.3. [Q925I1-1]
DR AlphaFoldDB; Q925I1; -.
DR SMR; Q925I1; -.
DR BioGRID; 224456; 19.
DR DIP; DIP-32373N; -.
DR IntAct; Q925I1; 8.
DR MINT; Q925I1; -.
DR STRING; 10090.ENSMUSP00000030903; -.
DR iPTMnet; Q925I1; -.
DR PhosphoSitePlus; Q925I1; -.
DR SwissPalm; Q925I1; -.
DR EPD; Q925I1; -.
DR jPOST; Q925I1; -.
DR MaxQB; Q925I1; -.
DR PaxDb; Q925I1; -.
DR PeptideAtlas; Q925I1; -.
DR PRIDE; Q925I1; -.
DR ProteomicsDB; 265139; -. [Q925I1-1]
DR ProteomicsDB; 265140; -. [Q925I1-2]
DR Antibodypedia; 26400; 165 antibodies from 24 providers.
DR Ensembl; ENSMUST00000030903; ENSMUSP00000030903; ENSMUSG00000029036. [Q925I1-1]
DR GeneID; 108888; -.
DR KEGG; mmu:108888; -.
DR UCSC; uc008wen.2; mouse. [Q925I1-1]
DR CTD; 55210; -.
DR MGI; MGI:1919214; Atad3a.
DR VEuPathDB; HostDB:ENSMUSG00000029036; -.
DR eggNOG; KOG0742; Eukaryota.
DR GeneTree; ENSGT00730000111059; -.
DR HOGENOM; CLU_011488_2_0_1; -.
DR InParanoid; Q925I1; -.
DR OMA; KTCSKMA; -.
DR OrthoDB; 357201at2759; -.
DR PhylomeDB; Q925I1; -.
DR TreeFam; TF313922; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 108888; 29 hits in 75 CRISPR screens.
DR ChiTaRS; Atad3a; mouse.
DR PRO; PR:Q925I1; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q925I1; protein.
DR Bgee; ENSMUSG00000029036; Expressed in metanephric renal vesicle and 249 other tissues.
DR ExpressionAtlas; Q925I1; baseline and differential.
DR Genevisible; Q925I1; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0042645; C:mitochondrial nucleoid; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0140374; P:antiviral innate immune response; ISS:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0001558; P:regulation of cell growth; IEA:Ensembl.
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; 2.
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 Acetylation; Alternative splicing; ATP-binding; Coiled coil;
KW Direct protein sequencing; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Mitochondrion nucleoid; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q5T9A4"
FT CHAIN 2..591
FT /note="ATPase family AAA domain-containing protein 3"
FT /id="PRO_0000084801"
FT TOPO_DOM 2..245
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..586
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..49
FT /note="Required for interaction with the inner surface of
FT the mitochondrial outer membrane"
FT /evidence="ECO:0000250"
FT REGION 289..304
FT /note="S100B-binding"
FT /evidence="ECO:0000250"
FT REGION 572..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 55..216
FT /evidence="ECO:0000255"
FT BINDING 351..358
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T9A4"
FT MOD_RES 490
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 490
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 494
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 512
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT VAR_SEQ 422..501
FT /note="EKISEDLRATLNAFLHRTGQHSSKFMLVLASNQPEQFDWAINDRIDEMVCFA
FT LPQREERERLVRMYFDKYVLKPATEGKQ -> R (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15368895"
FT /id="VSP_015643"
FT CONFLICT 376
FT /note="T -> K (in Ref. 2; BAC36055)"
FT /evidence="ECO:0000305"
FT CONFLICT 447
FT /note="M -> I (in Ref. 3; BAE42791)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 591 AA; 66742 MW; 66B599114B94620E CRC64;
MSWLFGIKGP KGEGTGPPLP LPPAQPGAEG GGDRGAGDRP SPKDKWSNFD PTGLERAAKA
ARELEHSRHA KEALSLAQMQ EQTLQLEQQS KLKEYEAAVE QLKSEQIRVQ AEERRKTLTE
ETRQHQARAQ YQDKLARQRY EDQLKQQQLL NEENLRKQEE SVQKQEAIRR ATVEREMELR
HKNEMLRVEA EARARAKADR ENADIIREQI RLKAAEHRQT ILESIRTAGT LLGEGFRAFV
TDWDKVTATV AGLTLLAVGV YSAKNATSVA GRYIEARLGK PSLVRETSRI SVLEALRHPI
QVSRRLVSRP QDALEGVILS PSLEARVRDI AIATRNTKKN KSLYRNVLMY GPPGTGKTLF
AKKLALHSGM DYAIMTGGDV APMGREGVTA MHKVFDWAST SRRGLLLFVD EADAFLRKRA
TEKISEDLRA TLNAFLHRTG QHSSKFMLVL ASNQPEQFDW AINDRIDEMV CFALPQREER
ERLVRMYFDK YVLKPATEGK QRLKVAQFDY GKKCSEVAQL TEGMSGREIA QLAVAWQAMA
YSSEDGVLTE AMMDARVQDA VQQHQQKMQW LKVERPDSQT NKPPHPSLLS C
