ATPase family AAA domain-containing protein 1

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Q505J9 (ATAD1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 58. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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
Synonyms:	Npg6

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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.3
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.3
Subcellular location	Peroxisome By similarity. Cell junction › synapse › postsynaptic cell membrane By similarity.
Sequence similarities	Belongs to the AAA ATPase family.
Biophysicochemical properties	Kinetic parameters: K_M=43.4 mM for ATP Ref.3 V_max=11.0 nM/min/mg enzyme
Sequence caution	The sequence ABX10437.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

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 sequence or structural similarity. Source: UniProtKB memory Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of synaptic transmission, glutamatergic Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of receptor internalization Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cell junction Inferred from electronic annotation. Source: UniProtKB-KW mitochondrion Inferred from electronic annotation. Source: Compara peroxisomal membrane Inferred from electronic annotation. Source: Compara plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW postsynaptic membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Gria2	P19491	3	EBI-4280289,EBI-77718

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_0000084793

Regions

Nucleotide binding

133 – 140

ATP Potential

Amino acid modifications

Modified residue

322

Phosphoserine By similarity

Cross-link

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

Experimental info

Mutagenesis

139

K → T: ATPase activity reduced by 60%-70%. ATPase activity reduced by 92%; when associated with Q-193. Ref.3

Mutagenesis

193

E → Q: ATPase activity reduced by 60%-70%. ATPase activity reduced by 92%; when associated with T-139. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

Q505J9 [UniParc].

Last modified June 7, 2005. Version 1.
Checksum: 358788BA7E7140BC
Show »

FASTA

361

40,717

        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 FQSVLTHVCL 


D

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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]. Tissue: Ovary.
[2]	"Functional identification of neuroprotective molecules." Dai C., Liang D., Li H., Sasaki M., Dawson T.M., Dawson V.L. PLoS ONE 5:E15008-E15008(2010) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 49-361.
[3]	"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, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH GRIA2 AND GRIP1, MUTAGENESIS OF LYS-139 AND GLU-193.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC094514 mRNA. Translation: AAH94514.1. EF688601 mRNA. Translation: ABX10437.1. Different initiation.
IPI	IPI00566676.
RefSeq	NP_001030174.1. NM_001035002.1.
UniGene	Rn.54918.
3D structure databases
ProteinModelPortal	Q505J9.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q505J9. 1 interaction.
STRING	10116.ENSRNOP00000041122.
PTM databases
PhosphoSite	Q505J9.
Proteomic databases
PaxDb	Q505J9.
PRIDE	Q505J9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000014684; ENSRNOP00000014684; ENSRNOG00000010861.
GeneID	309532.
KEGG	rno:309532.
UCSC	RGD:1308570. rat.
Organism-specific databases
CTD	84896.
RGD	1308570. Atad1.
Phylogenomic databases
eggNOG	COG0464.
GeneTree	ENSGT00550000074823.
HOGENOM	HOG000225141.
HOVERGEN	HBG057074.
OMA	KNENXDR.
Gene expression databases
ArrayExpress	Q505J9.
Genevestigator	Q505J9.
GermOnline	ENSRNOG00000010861. Rattus norvegicus.
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
NextBio	660942.

Entry information

Entry name

ATAD1_RAT

Accession

Primary (citable) accession number: Q505J9
Secondary accession number(s): B3STU2

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2005
Last sequence update:	June 7, 2005
Last modified:	April 3, 2013
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents