ID ATAD1_HUMAN Reviewed; 361 AA. AC Q8NBU5; D3DR26; Q6DKG1; Q6P4B9; Q8N3G1; Q8WYR9; Q969Y3; DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 27-NOV-2024, entry version 177. DE RecName: Full=Outer mitochondrial transmembrane helix translocase {ECO:0000305}; DE EC=7.4.2.- {ECO:0000305|PubMed:24843043}; DE AltName: Full=ATPase family AAA domain-containing protein 1 {ECO:0000305}; DE Short=hATAD1 {ECO:0000303|PubMed:24843043}; DE AltName: Full=Thorase {ECO:0000250|UniProtKB:Q9D5T0}; GN Name=ATAD1 {ECO:0000303|PubMed:24843043, ECO:0000312|HGNC:HGNC:25903}; GN ORFNames=FNP001 {ECO:0000303|Ref.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Pituitary; RA Liu F., Xu X.R., Qian B.Z., Xiao H., Chen Z., Han Z.; RT "A novel gene expressed in fetal normal pituitary."; RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Placenta; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 32-361 (ISOFORM 1). RC TISSUE=Bone, Lung, and PNS; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 47-361 (ISOFORM 1). RC TISSUE=Melanoma; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [11] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=24843043; DOI=10.15252/embj.201487943; RA Chen Y.C., Umanah G.K., Dephoure N., Andrabi S.A., Gygi S.P., Dawson T.M., RA Dawson V.L., Rutter J.; RT "Msp1/ATAD1 maintains mitochondrial function by facilitating the RT degradation of mislocalized tail-anchored proteins."; RL EMBO J. 33:1548-1564(2014). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [14] RP INVOLVEMENT IN HKPX4, VARIANT HKPX4 276-GLU--ASP-361 DEL, AND RP CHARACTERIZATION OF VARIANT HKPX4 276-GLU--ASP-361 DEL. RX PubMed=28180185; DOI=10.1212/nxg.0000000000000130; RA Ahrens-Nicklas R.C., Umanah G.K., Sondheimer N., Deardorff M.A., RA Wilkens A.B., Conlin L.K., Santani A.B., Nesbitt A., Juulsola J., Ma E., RA Dawson T.M., Dawson V.L., Marsh E.D.; RT "Precision therapy for a new disorder of AMPA receptor recycling due to RT mutations in ATAD1."; RL Neurol. Genet. 3:E130-E130(2017). RN [15] RP INVOLVEMENT IN HKPX4, AND VARIANT HKPX4 HIS-54. RX PubMed=29659736; DOI=10.1093/brain/awy095; RA Wolf N.I., Zschocke J., Jakobs C., Rating D., Hoffmann G.F.; RT "ATAD1 encephalopathy and stiff baby syndrome: a recognizable clinical RT presentation."; RL Brain 141:E49-E49(2018). RN [16] RP INVOLVEMENT IN HKPX4. RX PubMed=29390050; DOI=10.1093/brain/awx377; RA Piard J., Umanah G.K.E., Harms F.L., Abalde-Atristain L., Amram D., RA Chang M., Chen R., Alawi M., Salpietro V., Rees M.I., Chung S.K., RA Houlden H., Verloes A., Dawson T.M., Dawson V.L., Van Maldergem L., RA Kutsche K.; RT "A homozygous ATAD1 mutation impairs postsynaptic AMPA receptor trafficking RT and causes a lethal encephalopathy."; RL Brain 141:651-661(2018). RN [17] RP VARIANT [LARGE SCALE ANALYSIS] ILE-107. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Outer mitochondrial translocase required to remove CC mislocalized tail-anchored transmembrane proteins on mitochondria CC (PubMed:24843043). 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 (By similarity). 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 (By similarity). CC {ECO:0000250|UniProtKB:P28737, ECO:0000250|UniProtKB:Q9D5T0, CC ECO:0000269|PubMed:24843043}. 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 + phosphate + H(+); 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:0000305|PubMed:24843043}; CC -!- SUBUNIT: Interacts with GRIA2 and GRIP1 in an ATP-dependent manner (By CC similarity). 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 (By similarity). CC {ECO:0000250|UniProtKB:Q9D5T0}. CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane CC {ECO:0000269|PubMed:24843043}; Single-pass membrane protein CC {ECO:0000255}. Peroxisome membrane {ECO:0000269|PubMed:24843043}; CC Single-pass membrane protein {ECO:0000255}. Postsynaptic cell membrane CC {ECO:0000250|UniProtKB:Q9D5T0}; Single-pass membrane protein CC {ECO:0000255}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8NBU5-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8NBU5-2; Sequence=VSP_037304; CC -!- DISEASE: Hyperekplexia 4 (HKPX4) [MIM:618011]: An autosomal recessive CC severe neurologic disorder apparent from birth. HKPX4 is characterized CC by little if any development, hypertonia, early-onset refractory CC seizures in some patients, and respiratory failure resulting in early CC death, mostly in the first months of life. CC {ECO:0000269|PubMed:28180185, ECO:0000269|PubMed:29390050, CC ECO:0000269|PubMed:29659736}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the AAA ATPase family. MSP1 subfamily. CC {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; AF361493; AAL57218.1; -; mRNA. DR EMBL; AK027506; BAB55161.1; -; mRNA. DR EMBL; AK075223; BAC11482.1; -; mRNA. DR EMBL; AC022016; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL133327; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471066; EAW50180.1; -; Genomic_DNA. DR EMBL; CH471066; EAW50177.1; -; Genomic_DNA. DR EMBL; CH471066; EAW50179.1; -; Genomic_DNA. DR EMBL; BC010868; AAH10868.1; -; mRNA. DR EMBL; BC063530; AAH63530.1; -; mRNA. DR EMBL; BC073998; AAH73998.1; -; mRNA. DR EMBL; AL834370; CAD39033.1; -; mRNA. DR CCDS; CCDS7386.1; -. [Q8NBU5-1] DR RefSeq; NP_001308896.1; NM_001321967.1. [Q8NBU5-1] DR RefSeq; NP_116199.2; NM_032810.3. [Q8NBU5-1] DR RefSeq; XP_005270309.1; XM_005270252.4. [Q8NBU5-1] DR RefSeq; XP_016872336.1; XM_017016847.1. [Q8NBU5-1] DR PDB; 7UPR; EM; 3.20 A; A/B/C/D/E/F=42-361. DR PDB; 7UPT; EM; 3.50 A; A/B/C/D/E/F=42-361. DR PDBsum; 7UPR; -. DR PDBsum; 7UPT; -. DR AlphaFoldDB; Q8NBU5; -. DR EMDB; EMD-26674; -. DR EMDB; EMD-26675; -. DR SMR; Q8NBU5; -. DR BioGRID; 124336; 94. DR IntAct; Q8NBU5; 43. DR MINT; Q8NBU5; -. DR STRING; 9606.ENSP00000339017; -. DR GlyGen; Q8NBU5; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q8NBU5; -. DR PhosphoSitePlus; Q8NBU5; -. DR SwissPalm; Q8NBU5; -. DR BioMuta; ATAD1; -. DR DMDM; 74762551; -. DR jPOST; Q8NBU5; -. DR MassIVE; Q8NBU5; -. DR PaxDb; 9606-ENSP00000339017; -. DR PeptideAtlas; Q8NBU5; -. DR ProteomicsDB; 72823; -. [Q8NBU5-1] DR ProteomicsDB; 72824; -. [Q8NBU5-2] DR Pumba; Q8NBU5; -. DR ABCD; Q8NBU5; 1 sequenced antibody. DR Antibodypedia; 49559; 174 antibodies from 25 providers. DR DNASU; 84896; -. DR Ensembl; ENST00000308448.11; ENSP00000339017.4; ENSG00000138138.14. [Q8NBU5-1] DR Ensembl; ENST00000328142.3; ENSP00000339016.2; ENSG00000138138.14. [Q8NBU5-1] DR Ensembl; ENST00000680024.1; ENSP00000506333.1; ENSG00000138138.14. [Q8NBU5-1] DR GeneID; 84896; -. DR KEGG; hsa:84896; -. DR MANE-Select; ENST00000680024.1; ENSP00000506333.1; NM_001321967.2; NP_001308896.1. DR UCSC; uc001key.2; human. [Q8NBU5-1] DR AGR; HGNC:25903; -. DR CTD; 84896; -. DR DisGeNET; 84896; -. DR GeneCards; ATAD1; -. DR HGNC; HGNC:25903; ATAD1. DR HPA; ENSG00000138138; Low tissue specificity. DR MalaCards; ATAD1; -. DR MIM; 614452; gene. DR MIM; 618011; phenotype. DR neXtProt; NX_Q8NBU5; -. DR OpenTargets; ENSG00000138138; -. DR Orphanet; 3197; Hereditary hyperekplexia. DR PharmGKB; PA134914940; -. DR VEuPathDB; HostDB:ENSG00000138138; -. DR eggNOG; KOG0737; Eukaryota. DR GeneTree; ENSGT00550000074823; -. DR HOGENOM; CLU_000688_21_14_1; -. DR InParanoid; Q8NBU5; -. DR OMA; CRNAAMR; -. DR OrthoDB; 102713at2759; -. DR PhylomeDB; Q8NBU5; -. DR TreeFam; TF105016; -. DR PathwayCommons; Q8NBU5; -. DR Reactome; R-HSA-9603798; Class I peroxisomal membrane protein import. DR SignaLink; Q8NBU5; -. DR BioGRID-ORCS; 84896; 46 hits in 1154 CRISPR screens. DR ChiTaRS; ATAD1; human. DR GenomeRNAi; 84896; -. DR Pharos; Q8NBU5; Tbio. DR PRO; PR:Q8NBU5; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; Q8NBU5; protein. DR Bgee; ENSG00000138138; Expressed in right testis and 181 other cell types or tissues. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; HTP:FlyBase. DR GO; GO:0005778; C:peroxisomal membrane; IDA:UniProtKB. 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; IDA: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; IEA:Ensembl. DR CDD; cd19520; RecA-like_ATAD1; 1. DR FunFam; 1.10.8.60:FF:000044; ATPase family AAA domain-containing protein 1; 1. DR FunFam; 3.40.50.300:FF:000538; ATPase family AAA domain-containing protein 1; 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; IPR051701; Mito_OM_Translocase_MSP1. 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. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Cell membrane; KW Disease variant; Membrane; Mitochondrion; Mitochondrion outer membrane; KW Nucleotide-binding; Peroxisome; Phosphoprotein; Postsynaptic cell membrane; KW Proteomics identification; Reference proteome; Synapse; Translocase; KW Transmembrane; Transmembrane helix. FT CHAIN 1..361 FT /note="Outer mitochondrial transmembrane helix translocase" FT /id="PRO_0000084791" 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 VAR_SEQ 278..361 FT /note="VDRHVDLLEVAQETDGFSGSDLKEMCRDAALLCVREYVNSTSEESHDEDEIR FT PVQQQDLHRAIEKMKKSKDAAFQNVLTHVCLD -> LRKLKPREVL (in isoform FT 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_037304" FT VARIANT 54 FT /note="Q -> H (in HKPX4; uncertain significance; likely FT affects splicing due to removal of the splice donor site of FT intron 2; dbSNP:rs1554884979)" FT /evidence="ECO:0000269|PubMed:29659736" FT /id="VAR_080830" FT VARIANT 107 FT /note="V -> I (in a colorectal cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035903" FT VARIANT 276..361 FT /note="Missing (in HKPX4; severely decreased ATAD1 mRNA FT expression in lymphoblastoid cells derived from the patient FT compared to an unaffected control)" FT /evidence="ECO:0000269|PubMed:28180185" FT /id="VAR_080831" FT CONFLICT 160 FT /note="S -> R (in Ref. 1; AAL57218)" FT /evidence="ECO:0000305" FT HELIX 48..52 FT /evidence="ECO:0007829|PDB:7UPR" FT STRAND 53..56 FT /evidence="ECO:0007829|PDB:7UPR" FT HELIX 57..60 FT /evidence="ECO:0007829|PDB:7UPR" FT HELIX 71..77 FT /evidence="ECO:0007829|PDB:7UPR" FT HELIX 83..85 FT /evidence="ECO:0007829|PDB:7UPR" FT HELIX 90..92 FT /evidence="ECO:0007829|PDB:7UPR" FT HELIX 98..106 FT /evidence="ECO:0007829|PDB:7UPR" FT HELIX 108..111 FT /evidence="ECO:0007829|PDB:7UPR" FT HELIX 114..117 FT /evidence="ECO:0007829|PDB:7UPR" FT STRAND 129..138 FT /evidence="ECO:0007829|PDB:7UPR" FT HELIX 139..148 FT /evidence="ECO:0007829|PDB:7UPR" FT STRAND 152..156 FT /evidence="ECO:0007829|PDB:7UPR" FT TURN 159..162 FT /evidence="ECO:0007829|PDB:7UPR" FT HELIX 170..183 FT /evidence="ECO:0007829|PDB:7UPR" FT STRAND 184..190 FT /evidence="ECO:0007829|PDB:7UPR" FT TURN 192..197 FT /evidence="ECO:0007829|PDB:7UPR" FT STRAND 203..205 FT /evidence="ECO:0007829|PDB:7UPR" FT HELIX 207..220 FT /evidence="ECO:0007829|PDB:7UPR" FT STRAND 221..224 FT /evidence="ECO:0007829|PDB:7UPR" FT STRAND 226..228 FT /evidence="ECO:0007829|PDB:7UPR" FT STRAND 231..236 FT /evidence="ECO:0007829|PDB:7UPR" FT HELIX 240..242 FT /evidence="ECO:0007829|PDB:7UPR" FT HELIX 246..250 FT /evidence="ECO:0007829|PDB:7UPR" FT STRAND 253..256 FT /evidence="ECO:0007829|PDB:7UPR" FT HELIX 262..272 FT /evidence="ECO:0007829|PDB:7UPR" FT HELIX 284..291 FT /evidence="ECO:0007829|PDB:7UPR" FT HELIX 298..315 FT /evidence="ECO:0007829|PDB:7UPR" FT HELIX 334..346 FT /evidence="ECO:0007829|PDB:7UPR" FT HELIX 347..349 FT /evidence="ECO:0007829|PDB:7UPR" 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 //