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 24-JAN-2024, entry version 117. 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 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.ENSRNOP00000072875; -. DR iPTMnet; Q505J9; -. DR PhosphoSitePlus; Q505J9; -. DR SwissPalm; Q505J9; -. DR jPOST; Q505J9; -. DR PaxDb; 10116-ENSRNOP00000014684; -. DR ABCD; Q505J9; 1 sequenced antibody. DR GeneID; 309532; -. DR KEGG; rno:309532; -. DR UCSC; RGD:1308570; rat. DR AGR; RGD:1308570; -. DR CTD; 84896; -. DR RGD; 1308570; Atad1. DR eggNOG; KOG0737; Eukaryota. DR HOGENOM; CLU_000688_21_14_1; -. DR InParanoid; Q505J9; -. DR OrthoDB; 102713at2759; -. DR Reactome; R-RNO-9603798; Class I peroxisomal membrane protein import. DR SABIO-RK; Q505J9; -. DR PRO; PR:Q505J9; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD. 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:membrane 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 CDD; cd19520; RecA-like_ATAD1; 1. DR Gene3D; 1.10.8.60; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 PANTHER; PTHR45644; AAA ATPASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G12920)-RELATED-RELATED; 1. DR PANTHER; PTHR45644:SF2; OUTER MITOCHONDRIAL TRANSMEMBRANE HELIX TRANSLOCASE; 1. DR Pfam; PF00004; AAA; 1. DR Pfam; PF17862; AAA_lid_3; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00674; AAA; 1. DR Genevisible; Q505J9; RN. 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 //