ATAD1_HUMAN
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 03-AUG-2022, entry version 164.
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 + 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: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}.
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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 AlphaFoldDB; Q8NBU5; -.
DR SMR; Q8NBU5; -.
DR BioGRID; 124336; 73.
DR IntAct; Q8NBU5; 25.
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 EPD; Q8NBU5; -.
DR jPOST; Q8NBU5; -.
DR MassIVE; Q8NBU5; -.
DR MaxQB; Q8NBU5; -.
DR PaxDb; Q8NBU5; -.
DR PeptideAtlas; Q8NBU5; -.
DR PRIDE; Q8NBU5; -.
DR ProteomicsDB; 72823; -. [Q8NBU5-1]
DR ProteomicsDB; 72824; -. [Q8NBU5-2]
DR ABCD; Q8NBU5; 1 sequenced antibody.
DR Antibodypedia; 49559; 177 antibodies from 26 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; ENST00000634773.1; ENSP00000489353.1; ENSG00000283024.1. [Q8NBU5-1]
DR Ensembl; ENST00000634970.1; ENSP00000489455.1; ENSG00000283024.1. [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 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; GPRWQQF; -.
DR OrthoDB; 1430018at2759; -.
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 1078 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 179 other tissues.
DR Genevisible; Q8NBU5; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
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:transmembrane 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 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 Alternative splicing; ATP-binding; Cell membrane; Disease variant;
KW Membrane; Mitochondrion; Mitochondrion outer membrane; Nucleotide-binding;
KW Peroxisome; Phosphoprotein; Postsynaptic cell membrane; Reference proteome;
KW Synapse; Translocase; 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; unknown pathological significance;
FT likely affects splicing due to removal of the splice donor
FT site of 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"
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
