ATAD1_RAT
ID ATAD1_RAT Reviewed; 361 AA.
AC Q505J9; B3STU2;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Outer mitochondrial transmembrane helix translocase {ECO:0000305};
DE EC=7.4.2.- {ECO:0000250|UniProtKB:P28737, ECO:0000250|UniProtKB:Q8NBU5};
DE AltName: Full=ATPase family AAA domain-containing protein 1 {ECO:0000305};
DE AltName: Full=Neuroprotective protein 6 {ECO:0000303|PubMed:21124846};
DE AltName: Full=Thorase {ECO:0000303|PubMed:21496646};
GN Name=Atad1 {ECO:0000250|UniProtKB:Q8NBU5};
GN Synonyms=Npg6 {ECO:0000303|PubMed:21124846};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 49-361.
RX PubMed=21124846; DOI=10.1371/journal.pone.0015008;
RA Dai C., Liang D., Li H., Sasaki M., Dawson T.M., Dawson V.L.;
RT "Functional identification of neuroprotective molecules.";
RL PLoS ONE 5:E15008-E15008(2010).
RN [3]
RP FUNCTION, ATPASE ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH
RP GRIA2 AND GRIP1, AND MUTAGENESIS OF LYS-139 AND GLU-193.
RX PubMed=21496646; DOI=10.1016/j.cell.2011.03.016;
RA Zhang J., Wang Y., Chi Z., Keuss M.J., Pai Y.M., Kang H.C., Shin J.H.,
RA Bugayenko A., Wang H., Xiong Y., Pletnikov M.V., Mattson M.P., Dawson T.M.,
RA Dawson V.L.;
RT "The AAA+ ATPase Thorase regulates AMPA receptor-dependent synaptic
RT plasticity and behavior.";
RL Cell 145:284-299(2011).
CC -!- FUNCTION: Outer mitochondrial translocase required to remove
CC mislocalized tail-anchored transmembrane proteins on mitochondria (By
CC similarity). Specifically recognizes and binds tail-anchored
CC transmembrane proteins: acts as a dislocase that mediates the ATP-
CC dependent extraction of mistargeted tail-anchored transmembrane
CC proteins from the mitochondrion outer membrane (By similarity). Also
CC plays a critical role in regulating the surface expression of AMPA
CC receptors (AMPAR), thereby regulating synaptic plasticity and learning
CC and memory (PubMed:21496646). Required for NMDA-stimulated AMPAR
CC internalization and inhibition of GRIA1 and GRIA2 recycling back to the
CC plasma membrane; these activities are ATPase-dependent
CC (PubMed:21496646). {ECO:0000250|UniProtKB:P28737,
CC ECO:0000250|UniProtKB:Q8NBU5, ECO:0000269|PubMed:21496646}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-with a C-terminal TM segment(out) + ATP + H2O =
CC [protein]-with a C-terminal TM segment(in) + ADP + H(+) + phosphate;
CC Xref=Rhea:RHEA:66168, Rhea:RHEA-COMP:16963, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:90782, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P28737,
CC ECO:0000250|UniProtKB:Q8NBU5};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=43.4 mM for ATP {ECO:0000269|PubMed:21496646};
CC Vmax=11.0 nM/min/mg enzyme {ECO:0000269|PubMed:21496646};
CC -!- SUBUNIT: Interacts with GRIA2 and GRIP1 in an ATP-dependent manner
CC (PubMed:21496646). ATAD1-catalyzed ATP hydrolysis disrupts not only its
CC binding to GRIA2 and GRIP1, but also interaction between GRIP1 and
CC GRIA2, leading to AMPAR complex disassembly (PubMed:21496646).
CC {ECO:0000269|PubMed:21496646}.
CC -!- INTERACTION:
CC Q505J9; P19491: Gria2; NbExp=3; IntAct=EBI-4280289, EBI-77718;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q8NBU5}; Single-pass membrane protein
CC {ECO:0000255}. Peroxisome membrane {ECO:0000250|UniProtKB:Q8NBU5};
CC Single-pass membrane protein {ECO:0000255}. Postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:Q9D5T0}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. MSP1 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABX10437.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC094514; AAH94514.1; -; mRNA.
DR EMBL; EF688601; ABX10437.1; ALT_INIT; mRNA.
DR RefSeq; NP_001030174.1; NM_001035002.1.
DR AlphaFoldDB; Q505J9; -.
DR SMR; Q505J9; -.
DR IntAct; Q505J9; 1.
DR STRING; 10116.ENSRNOP00000014684; -.
DR iPTMnet; Q505J9; -.
DR PhosphoSitePlus; Q505J9; -.
DR jPOST; Q505J9; -.
DR PaxDb; Q505J9; -.
DR PRIDE; Q505J9; -.
DR ABCD; Q505J9; 1 sequenced antibody.
DR GeneID; 309532; -.
DR KEGG; rno:309532; -.
DR UCSC; RGD:1308570; rat.
DR CTD; 84896; -.
DR RGD; 1308570; Atad1.
DR eggNOG; KOG0737; Eukaryota.
DR HOGENOM; CLU_000688_21_14_1; -.
DR InParanoid; Q505J9; -.
DR OrthoDB; 1430018at2759; -.
DR Reactome; R-RNO-9603798; Class I peroxisomal membrane protein import.
DR SABIO-RK; Q505J9; -.
DR PRO; PR:Q505J9; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; Q505J9; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005778; C:peroxisomal membrane; ISS:UniProtKB.
DR GO; GO:0098794; C:postsynapse; ISO:RGD.
DR GO; GO:0045211; C:postsynaptic membrane; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0140567; F:transmembrane protein dislocase activity; IEA:RHEA.
DR GO; GO:0140570; P:extraction of mislocalized protein from mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0007612; P:learning; ISS:UniProtKB.
DR GO; GO:0007613; P:memory; ISS:UniProtKB.
DR GO; GO:0051967; P:negative regulation of synaptic transmission, glutamatergic; ISS:UniProtKB.
DR GO; GO:0002092; P:positive regulation of receptor internalization; ISS:UniProtKB.
DR GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; ISO:RGD.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Nucleotide-binding; Peroxisome;
KW Phosphoprotein; Postsynaptic cell membrane; Reference proteome; Synapse;
KW Translocase; Transmembrane; Transmembrane helix.
FT CHAIN 1..361
FT /note="Outer mitochondrial transmembrane helix translocase"
FT /id="PRO_0000084793"
FT TOPO_DOM 1..15
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 16..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..361
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT BINDING 133..140
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D5T0"
FT MUTAGEN 139
FT /note="K->T: ATPase activity reduced by 60%-70%. ATPase
FT activity reduced by 92%; when associated with Q-193."
FT /evidence="ECO:0000269|PubMed:21496646"
FT MUTAGEN 193
FT /note="E->Q: ATPase activity reduced by 60%-70%. ATPase
FT activity reduced by 92%; when associated with T-139."
FT /evidence="ECO:0000269|PubMed:21496646"
SQ SEQUENCE 361 AA; 40717 MW; 358788BA7E7140BC CRC64;
MVHAEAFSRP LSRNEVVGLI FRLTIFGAVT YFTIKWMVDA IDPTRKQKVE AQKQAEKLMK
QIGVKNVKLS EYEMSIAAHL VDPLNMHVTW SDIAGLDDVI TDLKDTVILP IKKKHLFENS
RLLQPPKGVL LYGPPGCGKT LIAKATAKEA GCRFINLQPS TLTDKWYGES QKLAAAVFSL
AIKLQPSIIF IDEIDSFLRN RSSSDHEATA MMKAQFMSLW DGLDTDHSCQ VIVMGATNRP
QDLDSAIMRR MPTRFHINQP ALKQREAILK LILKNENVDR HVDLLEVAQE TDGFSGSDLK
EMCRDAALLC VREYVNSTSE ESHDEDEIRP VQQQDLHRAI EKMKKSKDAA FQSVLTHVCL
D
