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Protein

ATPase family AAA domain-containing protein 1

Gene

Atad1

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

Functioni

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.1 Publication

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi133 – 1408ATPSequence Analysis

GO - Molecular functioni

  1. ATPase activity Source: UniProtKB
  2. ATP binding Source: UniProtKB-KW
  3. microtubule-severing ATPase activity Source: GO_Central

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. cytoplasmic microtubule organization Source: GO_Central
  3. learning Source: UniProtKB
  4. memory Source: UniProtKB
  5. negative regulation of synaptic transmission, glutamatergic Source: UniProtKB
  6. positive regulation of receptor internalization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ATPase family AAA domain-containing protein 1 (EC:3.6.1.3)
Alternative name(s):
Thorase
Gene namesi
Name:Atad1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 19

Organism-specific databases

MGIiMGI:1915229. Atad1.

Subcellular locationi

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. membrane Source: MGI
  3. mitochondrion Source: MGI
  4. nucleus Source: GO_Central
  5. peroxisomal membrane Source: MGI
  6. postsynaptic membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Peroxisome, Postsynaptic cell membrane, Synapse

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 361361ATPase family AAA domain-containing protein 1PRO_0000084792Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki46 – 46Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiQ9D5T0.
PaxDbiQ9D5T0.
PRIDEiQ9D5T0.

PTM databases

PhosphoSiteiQ9D5T0.

Expressioni

Tissue specificityi

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).1 Publication

Gene expression databases

BgeeiQ9D5T0.
CleanExiMM_ATAD1.
ExpressionAtlasiQ9D5T0. baseline and differential.
GenevestigatoriQ9D5T0.

Interactioni

Subunit structurei

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.1 Publication

Protein-protein interaction databases

BioGridi212578. 1 interaction.
IntActiQ9D5T0. 4 interactions.
MINTiMINT-4127126.

Structurei

3D structure databases

ProteinModelPortaliQ9D5T0.
SMRiQ9D5T0. Positions 54-348.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AAA ATPase family.Curated

Phylogenomic databases

eggNOGiCOG0464.
GeneTreeiENSGT00550000074823.
HOGENOMiHOG000225141.
HOVERGENiHBG057074.
InParanoidiQ9D5T0.
OMAiDYELMIA.
OrthoDBiEOG7SR4MJ.
PhylomeDBiQ9D5T0.
TreeFamiTF105016.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00674. AAA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9D5T0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVHAEAFSRP LSRNEVVGLI FRLTIFGAVT YFTIKWMVDA IDPTRKQKVE
60 70 80 90 100
AQKQAEKLMK QIGVKNVKLS EYEMSIAAHL VDPLNMHVTW SDIAGLDDVI
110 120 130 140 150
TDLKDTVILP IKKKHLFENS RLLQPPKGVL LYGPPGCGKT LIAKATAKEA
160 170 180 190 200
GCRFINLQPS TLTDKWYGES QKLAAAVFSL AIKLQPSIIF IDEIDSFLRN
210 220 230 240 250
RSSSDHEATA MMKAQFMSLW DGLDTDHSCQ VIVMGATNRP QDLDSAIMRR
260 270 280 290 300
MPTRFHINQP ALKQREAILK LILKNENVDR HVDLLEVAQE TDGFSGSDLK
310 320 330 340 350
EMCRDAALLC VREYVNSTSE ESHDEDEIRP VQQQDLHRAI EKMKKSKDAA
360
FQNVLTHVCL D
Length:361
Mass (Da):40,744
Last modified:June 1, 2001 - v1
Checksum:i2FAE88BA7E7140BC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti123 – 1231L → M in BAB26274. (PubMed:16141072)Curated
Sequence conflicti206 – 2061H → L in BAB26274. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS29752.1.
RefSeqiNP_080763.2. NM_026487.3.
XP_006527376.1. XM_006527313.1.
UniGeneiMm.27123.

Genome annotation databases

EnsembliENSMUST00000070210; ENSMUSP00000069962; ENSMUSG00000013662.
GeneIDi67979.
KEGGimmu:67979.
UCSCiuc008hfo.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS29752.1.
RefSeqiNP_080763.2. NM_026487.3.
XP_006527376.1. XM_006527313.1.
UniGeneiMm.27123.

3D structure databases

ProteinModelPortaliQ9D5T0.
SMRiQ9D5T0. Positions 54-348.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212578. 1 interaction.
IntActiQ9D5T0. 4 interactions.
MINTiMINT-4127126.

PTM databases

PhosphoSiteiQ9D5T0.

Proteomic databases

MaxQBiQ9D5T0.
PaxDbiQ9D5T0.
PRIDEiQ9D5T0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000070210; ENSMUSP00000069962; ENSMUSG00000013662.
GeneIDi67979.
KEGGimmu:67979.
UCSCiuc008hfo.1. mouse.

Organism-specific databases

CTDi84896.
MGIiMGI:1915229. Atad1.

Phylogenomic databases

eggNOGiCOG0464.
GeneTreeiENSGT00550000074823.
HOGENOMiHOG000225141.
HOVERGENiHBG057074.
InParanoidiQ9D5T0.
OMAiDYELMIA.
OrthoDBiEOG7SR4MJ.
PhylomeDBiQ9D5T0.
TreeFamiTF105016.

Miscellaneous databases

ChiTaRSiAtad1. mouse.
NextBioi326122.
PROiQ9D5T0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D5T0.
CleanExiMM_ATAD1.
ExpressionAtlasiQ9D5T0. baseline and differential.
GenevestigatoriQ9D5T0.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00674. AAA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: SUBCELLULAR LOCATION.
    Tissue: Kidney.
  4. 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.

Entry informationi

Entry nameiATAD1_MOUSE
AccessioniPrimary (citable) accession number: Q9D5T0
Secondary accession number(s): Q3U8V2, Q9D7A4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: June 1, 2001
Last modified: February 4, 2015
This is version 111 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, 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

External Data

Dasty 3

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 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.