ATAD1_MOUSE
ID ATAD1_MOUSE Reviewed; 361 AA.
AC Q9D5T0; Q3U8V2; Q9D7A4;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 157.
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=Thorase {ECO:0000303|PubMed:21496646};
GN Name=Atad1 {ECO:0000312|MGI:MGI:1915229};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Bone marrow, Cecum, Embryo, Lung, Testis, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary tumor;
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 [3]
RP SUBCELLULAR LOCATION.
RC TISSUE=Kidney;
RX PubMed=17768142; DOI=10.1074/mcp.m700169-mcp200;
RA Wiese S., Gronemeyer T., Ofman R., Kunze M., Grou C.P., Almeida J.A.,
RA Eisenacher M., Stephan C., Hayen H., Schollenberger L., Korosec T.,
RA Waterham H.R., Schliebs W., Erdmann R., Berger J., Meyer H.E., Just W.,
RA Azevedo J.E., Wanders R.J., Warscheid B.;
RT "Proteomics characterization of mouse kidney peroxisomes by tandem mass
RT spectrometry and protein correlation profiling.";
RL Mol. Cell. Proteomics 6:2045-2057(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-322, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17208939; DOI=10.1074/mcp.m600218-mcp200;
RA Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT MS/MS/MS.";
RL Mol. Cell. Proteomics 6:669-676(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP FUNCTION, INTERACTION WITH GRIA2 AND GRIP1, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
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 -!- 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 -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q8NBU5}; Single-pass membrane protein
CC {ECO:0000255}. Peroxisome membrane {ECO:0000269|PubMed:17768142};
CC Single-pass membrane protein {ECO:0000255}. Postsynaptic cell membrane
CC {ECO:0000269|PubMed:21496646}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Widely expressed with the highest expression in the
CC brain and testis. In the brain, relatively high expression in
CC hippocampal CA1 pyramidal cells (at protein level).
CC {ECO:0000269|PubMed:21496646}.
CC -!- DISRUPTION PHENOTYPE: About 80% of the mutant mice die of a seizure-
CC like syndrome between postnatal days 19 and 25; the remaining 20%
CC survive up to 8 weeks of age. No gross abnormalities in tissues
CC analyzed, including heart, lung, spleen, kidney, thymus, liver,
CC intestine, testis, eyes, and muscle. In the CA1 region of the
CC hippocampus, no substantial difference in the dendritic complexity or
CC in the number or size of dendritic spines and normal density of
CC synapses in mutant animals compared to wild-type.
CC {ECO:0000269|PubMed:21496646}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. MSP1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AK009419; BAB26274.1; -; mRNA.
DR EMBL; AK014967; BAB29643.1; -; mRNA.
DR EMBL; AK030719; BAC27097.1; -; mRNA.
DR EMBL; AK033639; BAC28402.1; -; mRNA.
DR EMBL; AK150469; BAE29586.1; -; mRNA.
DR EMBL; AK152059; BAE30915.1; -; mRNA.
DR EMBL; AK165953; BAE38481.1; -; mRNA.
DR EMBL; BC029085; AAH29085.1; -; mRNA.
DR EMBL; BC043051; AAH43051.1; -; mRNA.
DR CCDS; CCDS29752.1; -.
DR RefSeq; NP_080763.2; NM_026487.3.
DR RefSeq; XP_006527376.1; XM_006527313.2.
DR AlphaFoldDB; Q9D5T0; -.
DR SMR; Q9D5T0; -.
DR BioGRID; 212578; 14.
DR IntAct; Q9D5T0; 1.
DR STRING; 10090.ENSMUSP00000069962; -.
DR GlyConnect; 2138; 2 N-Linked glycans (1 site).
DR GlyGen; Q9D5T0; 1 site, 2 N-linked glycans (1 site).
DR iPTMnet; Q9D5T0; -.
DR PhosphoSitePlus; Q9D5T0; -.
DR SwissPalm; Q9D5T0; -.
DR EPD; Q9D5T0; -.
DR jPOST; Q9D5T0; -.
DR MaxQB; Q9D5T0; -.
DR PaxDb; Q9D5T0; -.
DR PeptideAtlas; Q9D5T0; -.
DR PRIDE; Q9D5T0; -.
DR ProteomicsDB; 265136; -.
DR ABCD; Q9D5T0; 1 sequenced antibody.
DR Antibodypedia; 49559; 177 antibodies from 26 providers.
DR DNASU; 67979; -.
DR Ensembl; ENSMUST00000070210; ENSMUSP00000069962; ENSMUSG00000013662.
DR Ensembl; ENSMUST00000235412; ENSMUSP00000157842; ENSMUSG00000013662.
DR Ensembl; ENSMUST00000236011; ENSMUSP00000157772; ENSMUSG00000013662.
DR Ensembl; ENSMUST00000236985; ENSMUSP00000158237; ENSMUSG00000013662.
DR GeneID; 67979; -.
DR KEGG; mmu:67979; -.
DR UCSC; uc008hfo.1; mouse.
DR CTD; 84896; -.
DR MGI; MGI:1915229; Atad1.
DR VEuPathDB; HostDB:ENSMUSG00000013662; -.
DR eggNOG; KOG0737; Eukaryota.
DR GeneTree; ENSGT00550000074823; -.
DR HOGENOM; CLU_000688_21_14_1; -.
DR InParanoid; Q9D5T0; -.
DR OMA; GPRWQQF; -.
DR OrthoDB; 1430018at2759; -.
DR PhylomeDB; Q9D5T0; -.
DR TreeFam; TF105016; -.
DR Reactome; R-MMU-9603798; Class I peroxisomal membrane protein import.
DR BioGRID-ORCS; 67979; 7 hits in 73 CRISPR screens.
DR ChiTaRS; Atad1; mouse.
DR PRO; PR:Q9D5T0; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9D5T0; protein.
DR Bgee; ENSMUSG00000013662; Expressed in animal zygote and 276 other tissues.
DR ExpressionAtlas; Q9D5T0; baseline and differential.
DR Genevisible; Q9D5T0; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
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:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005778; C:peroxisomal membrane; ISS:UniProtKB.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA: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; IMP:UniProtKB.
DR GO; GO:0007613; P:memory; IMP:UniProtKB.
DR GO; GO:0051967; P:negative regulation of synaptic transmission, glutamatergic; IMP:UniProtKB.
DR GO; GO:0002092; P:positive regulation of receptor internalization; IMP:UniProtKB.
DR GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; IDA:SynGO.
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_0000084792"
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:0007744|PubMed:17208939"
FT CONFLICT 123
FT /note="L -> M (in Ref. 1; BAB26274)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="H -> L (in Ref. 1; BAB26274)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 361 AA; 40744 MW; 2FAE88BA7E7140BC 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 FQNVLTHVCL
D
