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Protein

ATPase family AAA domain-containing protein 3

Gene

Atad3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organism and cellular level. May play an important in mitochondrial protein synthesis. May also participate in mitochondrial DNA replication. May bind to mitochondrial DNA D-loops and contribute to nucleoid stability. Required for enhanced channeling of cholesterol for hormone-dependent steroidogenesis (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi351 – 3588ATPSequence analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ATPase family AAA domain-containing protein 3
Alternative name(s):
AAA-ATPase TOB3
Gene namesi
Name:Atad3
Synonyms:Atad3a, Kiaa1273
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1919214. Atad3a.

Subcellular locationi

  • Mitochondrion inner membrane By similarity; Single-pass membrane protein By similarity
  • Mitochondrion matrixmitochondrion nucleoid By similarity

  • Note: In the mitochondrial inner membrane, enriched in sites with the potential to form contacts with the outer membrane. The N-terminal domain interacts with the inner surface of the mitochondrial outer membrane and the C-terminal domain localizes in a specific matrix compartment, where it is associated with nucleoids (By similarity).By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 245245Mitochondrial intermembraneSequence analysisAdd
BLAST
Transmembranei246 – 26318HelicalSequence analysisAdd
BLAST
Topological domaini264 – 586323Mitochondrial matrixSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • mitochondrial inner membrane Source: MGI
  • mitochondrial nucleoid Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane, Mitochondrion nucleoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 591591ATPase family AAA domain-containing protein 3PRO_0000084801Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei490 – 4901N6-acetyllysine; alternateCombined sources
Modified residuei490 – 4901N6-succinyllysine; alternateCombined sources
Modified residuei494 – 4941N6-acetyllysineCombined sources
Modified residuei512 – 5121N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ925I1.
MaxQBiQ925I1.
PaxDbiQ925I1.
PRIDEiQ925I1.

PTM databases

iPTMnetiQ925I1.
PhosphoSiteiQ925I1.
SwissPalmiQ925I1.

Expressioni

Tissue specificityi

Expressed in heart, spleen, kidney, liver and at smaller levels, in lung and muscle (at protein level).1 Publication

Gene expression databases

BgeeiQ925I1.
CleanExiMM_ATAD3A.
ExpressionAtlasiQ925I1. baseline and differential.
GenevisibleiQ925I1. MM.

Interactioni

Subunit structurei

Can form homooligomers. Homodimer formation at the N-terminus may be regulated by ATP and is required for the interaction with the inner surface of the mitochondrial outer membrane and correct mitochondrial homeostasis. Interacts with components of the mitochondrial ribosome and with other proteins involved in mitochondrial RNA metabolism. May also interact with protein involved in lipid metabolism, including STARD9. May interact with FAM210A. Interacts with GADD45GIP1. Interacts with S100B in a Ca(+2)- and Zn(+2)-dependent manner; this interaction probably occurs in the cytosol prior to mitochondrial targeting. S100B could assist ATAD3A cytoplasmic processing, preventing aggregation and favoring mitochondrial localization. Interacts with HSP60/HSPD1. Forms heterooligomers with ATAD3B; this interaction may affect ATAD3A activity (By similarity).By similarity

Protein-protein interaction databases

BioGridi224456. 5 interactions.
DIPiDIP-32373N.
IntActiQ925I1. 4 interactions.
MINTiMINT-4123180.
STRINGi10090.ENSMUSP00000030903.

Structurei

3D structure databases

ProteinModelPortaliQ925I1.
SMRiQ925I1. Positions 319-570.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 4949Required for interaction with the inner surface of the mitochondrial outer membraneBy similarityAdd
BLAST
Regioni289 – 30416S100B-bindingBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili55 – 216162Sequence analysisAdd
BLAST

Domaini

The transmembrane domain and a C-terminal adjacent region contain all information necessary for mitochondrial targeting.By similarity

Sequence similaritiesi

Belongs to the AAA ATPase family.Curated

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0742. Eukaryota.
COG1223. LUCA.
GeneTreeiENSGT00730000111059.
HOGENOMiHOG000231291.
HOVERGENiHBG058506.
InParanoidiQ925I1.
KOiK17681.
OMAiQQHRQKM.
OrthoDBiEOG7J9VP8.
PhylomeDBiQ925I1.
TreeFamiTF313922.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR021911. DUF3523.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
PF12037. DUF3523. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q925I1-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSWLFGIKGP KGEGTGPPLP LPPAQPGAEG GGDRGAGDRP SPKDKWSNFD
60 70 80 90 100
PTGLERAAKA ARELEHSRHA KEALSLAQMQ EQTLQLEQQS KLKEYEAAVE
110 120 130 140 150
QLKSEQIRVQ AEERRKTLTE ETRQHQARAQ YQDKLARQRY EDQLKQQQLL
160 170 180 190 200
NEENLRKQEE SVQKQEAIRR ATVEREMELR HKNEMLRVEA EARARAKADR
210 220 230 240 250
ENADIIREQI RLKAAEHRQT ILESIRTAGT LLGEGFRAFV TDWDKVTATV
260 270 280 290 300
AGLTLLAVGV YSAKNATSVA GRYIEARLGK PSLVRETSRI SVLEALRHPI
310 320 330 340 350
QVSRRLVSRP QDALEGVILS PSLEARVRDI AIATRNTKKN KSLYRNVLMY
360 370 380 390 400
GPPGTGKTLF AKKLALHSGM DYAIMTGGDV APMGREGVTA MHKVFDWAST
410 420 430 440 450
SRRGLLLFVD EADAFLRKRA TEKISEDLRA TLNAFLHRTG QHSSKFMLVL
460 470 480 490 500
ASNQPEQFDW AINDRIDEMV CFALPQREER ERLVRMYFDK YVLKPATEGK
510 520 530 540 550
QRLKVAQFDY GKKCSEVAQL TEGMSGREIA QLAVAWQAMA YSSEDGVLTE
560 570 580 590
AMMDARVQDA VQQHQQKMQW LKVERPDSQT NKPPHPSLLS C
Length:591
Mass (Da):66,742
Last modified:December 1, 2001 - v1
Checksum:i66B599114B94620E
GO
Isoform 2 (identifier: Q925I1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     422-501: EKISEDLRAT...VLKPATEGKQ → R

Note: No experimental confirmation available.
Show »
Length:512
Mass (Da):57,428
Checksum:i8A2573513F8051BF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti376 – 3761T → K in BAC36055 (PubMed:15368895).Curated
Sequence conflicti447 – 4471M → I in BAE42791 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei422 – 50180EKISE…TEGKQ → R in isoform 2. 1 PublicationVSP_015643Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF343079 mRNA. Translation: AAK38648.1.
AK075921 mRNA. Translation: BAC36055.1.
AK148974 mRNA. Translation: BAE28707.1.
AK149702 mRNA. Translation: BAE29037.1.
AK150037 mRNA. Translation: BAE29259.1.
AK166099 mRNA. Translation: BAE38570.1.
AK172038 mRNA. Translation: BAE42791.1.
AK173141 Unassigned RNA. Translation: BAD32419.1.
AL670236 Genomic DNA. Translation: CAM18382.1.
CH466594 Genomic DNA. Translation: EDL15028.1.
BC023301 mRNA. Translation: AAH23301.1.
BC058373 mRNA. Translation: AAH58373.1.
BC060036 mRNA. Translation: AAH60036.1.
CCDSiCCDS19037.1. [Q925I1-1]
RefSeqiNP_849534.2. NM_179203.3. [Q925I1-1]
UniGeneiMm.241152.

Genome annotation databases

EnsembliENSMUST00000030903; ENSMUSP00000030903; ENSMUSG00000029036. [Q925I1-1]
GeneIDi108888.
KEGGimmu:108888.
UCSCiuc008wen.2. mouse. [Q925I1-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF343079 mRNA. Translation: AAK38648.1.
AK075921 mRNA. Translation: BAC36055.1.
AK148974 mRNA. Translation: BAE28707.1.
AK149702 mRNA. Translation: BAE29037.1.
AK150037 mRNA. Translation: BAE29259.1.
AK166099 mRNA. Translation: BAE38570.1.
AK172038 mRNA. Translation: BAE42791.1.
AK173141 Unassigned RNA. Translation: BAD32419.1.
AL670236 Genomic DNA. Translation: CAM18382.1.
CH466594 Genomic DNA. Translation: EDL15028.1.
BC023301 mRNA. Translation: AAH23301.1.
BC058373 mRNA. Translation: AAH58373.1.
BC060036 mRNA. Translation: AAH60036.1.
CCDSiCCDS19037.1. [Q925I1-1]
RefSeqiNP_849534.2. NM_179203.3. [Q925I1-1]
UniGeneiMm.241152.

3D structure databases

ProteinModelPortaliQ925I1.
SMRiQ925I1. Positions 319-570.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi224456. 5 interactions.
DIPiDIP-32373N.
IntActiQ925I1. 4 interactions.
MINTiMINT-4123180.
STRINGi10090.ENSMUSP00000030903.

PTM databases

iPTMnetiQ925I1.
PhosphoSiteiQ925I1.
SwissPalmiQ925I1.

Proteomic databases

EPDiQ925I1.
MaxQBiQ925I1.
PaxDbiQ925I1.
PRIDEiQ925I1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030903; ENSMUSP00000030903; ENSMUSG00000029036. [Q925I1-1]
GeneIDi108888.
KEGGimmu:108888.
UCSCiuc008wen.2. mouse. [Q925I1-1]

Organism-specific databases

CTDi55210.
MGIiMGI:1919214. Atad3a.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG0742. Eukaryota.
COG1223. LUCA.
GeneTreeiENSGT00730000111059.
HOGENOMiHOG000231291.
HOVERGENiHBG058506.
InParanoidiQ925I1.
KOiK17681.
OMAiQQHRQKM.
OrthoDBiEOG7J9VP8.
PhylomeDBiQ925I1.
TreeFamiTF313922.

Miscellaneous databases

PROiQ925I1.
SOURCEiSearch...

Gene expression databases

BgeeiQ925I1.
CleanExiMM_ATAD3A.
ExpressionAtlasiQ925I1. baseline and differential.
GenevisibleiQ925I1. MM.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR021911. DUF3523.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
PF12037. DUF3523. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "TOB3 is a novel AAA-ATPase involved in protein secretion."
    Parng C., Piepenhagen P.A., Casanova J., Pillai S.
    Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: BALB/cJ.
  2. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
    DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Embryonic tail.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J and NOD.
    Tissue: Bone marrow, Embryonic tail, Lung, Spleen and Sympathetic ganglion.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J and FVB/N.
    Tissue: Brain, Colon and Mammary tumor.
  7. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 302-311 AND 478-485, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain.
  8. "Proteomic analysis of the mouse liver mitochondrial inner membrane."
    Da Cruz S., Xenarios I., Langridge J., Vilbois F., Parone P.A., Martinou J.-C.
    J. Biol. Chem. 278:41566-41571(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Pancreas, Spleen and Testis.
  10. "ATPase family AAA domain-containing 3A is a novel anti-apoptotic factor in lung adenocarcinoma cells."
    Fang H.Y., Chang C.L., Hsu S.H., Huang C.Y., Chiang S.F., Chiou S.H., Huang C.H., Hsiao Y.T., Lin T.Y., Chiang I.P., Hsu W.H., Sugano S., Chen C.Y., Lin C.Y., Ko W.J., Chow K.C.
    J. Cell Sci. 123:1171-1180(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  11. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-490, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-490; LYS-494 AND LYS-512, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiATAD3_MOUSE
AccessioniPrimary (citable) accession number: Q925I1
Secondary accession number(s): A2AD89
, Q3TA78, Q3UE74, Q69ZM7, Q8C6C6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: December 1, 2001
Last modified: June 8, 2016
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.