Q9D5T0 (ATAD1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATPase family AAA domain-containing protein 1
EC=3.6.1.3

Alternative name(s):
Thorase

Gene names

Name:

Atad1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	361 AA.
Sequence status	Complete.
Protein existence	Evidence 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.6
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.6
Subcellular location	Peroxisome. Cell junction › synapse › postsynaptic cell membrane Ref.4 Ref.6.
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.6
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.6
Sequence similarities	Belongs to the AAA ATPase family.

Ontologies

Keywords
Cellular component	Cell junction Cell membrane Membrane Peroxisome Postsynaptic cell membrane Synapse
Ligand	ATP-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	learning Inferred from mutant phenotype Ref.6. Source: UniProtKB memory Inferred from mutant phenotype Ref.6. Source: UniProtKB negative regulation of synaptic transmission, glutamatergic Inferred from mutant phenotype Ref.6. Source: UniProtKB positive regulation of receptor internalization Inferred from mutant phenotype Ref.6. Source: UniProtKB
Cellular_component	cell junction Inferred from electronic annotation. Source: UniProtKB-KW mitochondrion Inferred from direct assay PubMed 18614015. Source: MGI peroxisomal membrane Inferred from electronic annotation. Source: Compara plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW postsynaptic membrane Inferred from direct assay Ref.6. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity Inferred from direct assay Ref.6. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 361	361	ATPase family AAA domain-containing protein 1		PRO_0000084792
Regions
	Nucleotide binding	133 – 140	8	ATP Potential
Amino acid modifications
	Modified residue	322	1	Phosphoserine Ref.3 Ref.5
	Cross-link	46		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Experimental info
	Sequence conflict	123	1	L → M in BAB26274. Ref.1
	Sequence conflict	206	1	H → L in BAB26274. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9D5T0 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 2FAE88BA7E7140BC	FASTA	361	40,744
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"Mitochondrial phosphoproteome revealed by an improved IMAC method and MS/MS/MS." Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y. Mol. Cell. Proteomics 6:669-676(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-322, MASS SPECTROMETRY. Tissue: Liver.
[4]	"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.
[5]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-322, MASS SPECTROMETRY. Tissue: Liver.
[6]	"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.
IPI	IPI00108410.
RefSeq	NP_080763.2. NM_026487.3.
UniGene	Mm.27123.
3D structure databases
ProteinModelPortal	Q9D5T0.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9D5T0. 1 interaction.
PTM databases
PhosphoSite	Q9D5T0.
Proteomic databases
PaxDb	Q9D5T0.
PRIDE	Q9D5T0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000070210; ENSMUSP00000069962; ENSMUSG00000013662.
GeneID	67979.
KEGG	mmu:67979.
UCSC	uc008hfo.1. mouse.
Organism-specific databases
CTD	84896.
MGI	MGI:1915229. Atad1.
Phylogenomic databases
eggNOG	COG0464.
GeneTree	ENSGT00550000074823.
HOGENOM	HOG000225141.
HOVERGEN	HBG057074.
InParanoid	Q9D5T0.
OMA	KNENXDR.
OrthoDB	EOG412M5T.
Gene expression databases
ArrayExpress	Q9D5T0.
Bgee	Q9D5T0.
CleanEx	MM_ATAD1.
Genevestigator	Q9D5T0.
GermOnline	ENSMUSG00000013662. Mus musculus.
Family and domain databases
InterPro	IPR003593. AAA+_ATPase. IPR003959. ATPase_AAA_core. IPR003960. ATPase_AAA_CS. [Graphical view]
Pfam	PF00004. AAA. 1 hit. [Graphical view]
SMART	SM00382. AAA. 1 hit. [Graphical view]
PROSITE	PS00674. AAA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ATAD1. mouse.
NextBio	326122.
SOURCE	Search...

Entry information

Entry name

ATAD1_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program