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Q9D5T0 (ATAD1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATPase family AAA domain-containing protein 1

EC=3.6.1.3
Alternative name(s):
Thorase
Gene names
Name:Atad1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length361 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

ATPase that plays a critical role in regulating the surface expression of AMPA receptors (AMPAR), thereby regulating synaptic plasticity and learning and memory. Required for NMDA-stimulated AMPAR internalization and inhibition of GRIA1 and GRIA2 recycling back to the plasma membrane; these activities are ATPase-dependent. Ref.5

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

Interacts with GRIA2 and GRIP1 in an ATP-dependent manner. ATAD1-catalyzed ATP hydrolysis disrupts not only its binding to GRIA2 and GRIP1, but also interaction between GRIP1 and GRIA2, leading to AMPAR complex disassembly. Ref.5

Subcellular location

Peroxisome. Cell junctionsynapsepostsynaptic cell membrane Ref.3 Ref.5.

Tissue specificity

Widely expressed with the highest expression in the brain and testis. In the brain, relatively high expression in hippocampal CA1 pyramidal cells (at protein level). Ref.5

Disruption phenotype

About 80% of the mutant mice die of a seizure-like syndrome between postnatal days 19 and 25; the remaining 20% survive up to 8 weeks of age. No gross abnormalities in tissues analyzed, including heart, lung, spleen, kidney, thymus, liver, intestine, testis, eyes, and muscle. In the CA1 region of the hippocampus, no substantial difference in the dendritic complexity or in the number or size of dendritic spines and normal density of synapses in mutant animals compared to wild-type. Ref.5

Sequence similarities

Belongs to the AAA ATPase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 361361ATPase family AAA domain-containing protein 1
PRO_0000084792

Regions

Nucleotide binding133 – 1408ATP Potential

Amino acid modifications

Cross-link46Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Experimental info

Sequence conflict1231L → M in BAB26274. Ref.1
Sequence conflict2061H → L in BAB26274. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9D5T0 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 2FAE88BA7E7140BC

FASTA36140,744
        10         20         30         40         50         60 
MVHAEAFSRP LSRNEVVGLI FRLTIFGAVT YFTIKWMVDA IDPTRKQKVE AQKQAEKLMK 

        70         80         90        100        110        120 
QIGVKNVKLS EYEMSIAAHL VDPLNMHVTW SDIAGLDDVI TDLKDTVILP IKKKHLFENS 

       130        140        150        160        170        180 
RLLQPPKGVL LYGPPGCGKT LIAKATAKEA GCRFINLQPS TLTDKWYGES QKLAAAVFSL 

       190        200        210        220        230        240 
AIKLQPSIIF IDEIDSFLRN RSSSDHEATA MMKAQFMSLW DGLDTDHSCQ VIVMGATNRP 

       250        260        270        280        290        300 
QDLDSAIMRR MPTRFHINQP ALKQREAILK LILKNENVDR HVDLLEVAQE TDGFSGSDLK 

       310        320        330        340        350        360 
EMCRDAALLC VREYVNSTSE ESHDEDEIRP VQQQDLHRAI EKMKKSKDAA FQNVLTHVCL 


D 

« Hide

References

« Hide 'large scale' references
[1]"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. expand/collapse author list , 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].
Strain: C57BL/6J.
Tissue: Bone marrow, Cecum, Embryo, Lung, Testis and Tongue.
[2]"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].
Strain: C57BL/6 and FVB/N.
Tissue: Brain and Mammary tumor.
[3]"Proteomics characterization of mouse kidney peroxisomes by tandem mass spectrometry and protein correlation profiling."
Wiese S., Gronemeyer T., Ofman R., Kunze M., Grou C.P., Almeida J.A., Eisenacher M., Stephan C., Hayen H., Schollenberger L., Korosec T., Waterham H.R., Schliebs W., Erdmann R., Berger J., Meyer H.E., Just W., Azevedo J.E., Wanders R.J., Warscheid B.
Mol. Cell. Proteomics 6:2045-2057(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
Tissue: Kidney.
[4]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[5]"The AAA+ ATPase Thorase regulates AMPA receptor-dependent synaptic plasticity and behavior."
Zhang J., Wang Y., Chi Z., Keuss M.J., Pai Y.M., Kang H.C., Shin J.H., Bugayenko A., Wang H., Xiong Y., Pletnikov M.V., Mattson M.P., Dawson T.M., Dawson V.L.
Cell 145:284-299(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH GRIA2 AND GRIP1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK009419 mRNA. Translation: BAB26274.1.
AK014967 mRNA. Translation: BAB29643.1.
AK030719 mRNA. Translation: BAC27097.1.
AK033639 mRNA. Translation: BAC28402.1.
AK150469 mRNA. Translation: BAE29586.1.
AK152059 mRNA. Translation: BAE30915.1.
AK165953 mRNA. Translation: BAE38481.1.
BC029085 mRNA. Translation: AAH29085.1.
BC043051 mRNA. Translation: AAH43051.1.
CCDSCCDS29752.1.
RefSeqNP_080763.2. NM_026487.3.
XP_006527376.1. XM_006527313.1.
UniGeneMm.27123.

3D structure databases

ProteinModelPortalQ9D5T0.
SMRQ9D5T0. Positions 54-348.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid212578. 1 interaction.
IntActQ9D5T0. 4 interactions.
MINTMINT-4127126.

PTM databases

PhosphoSiteQ9D5T0.

Proteomic databases

MaxQBQ9D5T0.
PaxDbQ9D5T0.
PRIDEQ9D5T0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000070210; ENSMUSP00000069962; ENSMUSG00000013662.
GeneID67979.
KEGGmmu:67979.
UCSCuc008hfo.1. mouse.

Organism-specific databases

CTD84896.
MGIMGI:1915229. Atad1.

Phylogenomic databases

eggNOGCOG0464.
GeneTreeENSGT00550000074823.
HOGENOMHOG000225141.
HOVERGENHBG057074.
InParanoidQ9D5T0.
OMAYNCQVIV.
OrthoDBEOG7SR4MJ.
PhylomeDBQ9D5T0.
TreeFamTF105016.

Gene expression databases

ArrayExpressQ9D5T0.
BgeeQ9D5T0.
CleanExMM_ATAD1.
GenevestigatorQ9D5T0.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00004. AAA. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS00674. AAA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSATAD1. mouse.
NextBio326122.
PROQ9D5T0.
SOURCESearch...

Entry information

Entry nameATAD1_MOUSE
AccessionPrimary (citable) accession number: Q9D5T0
Secondary accession number(s): Q3U8V2, Q9D7A4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot