ID   ATD1A_DANRE             Reviewed;         380 AA.
AC   Q7ZZ25; Q66IE9;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 2.
DT   27-MAR-2024, entry version 124.
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-A {ECO:0000305};
GN   Name=atad1a {ECO:0000250|UniProtKB:Q8NBU5};
GN   ORFNames=si:zc156n3.1 {ECO:0000303|PubMed:23594743}, zgc:101570
GN   {ECO:0000303|Ref.2};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Embryo;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250|UniProtKB:P28737,
CC       ECO:0000250|UniProtKB:Q8NBU5, ECO:0000250|UniProtKB:Q9D5T0}.
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   -!- 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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q7ZZ25-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7ZZ25-2; Sequence=VSP_015632;
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. MSP1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AL772163; CAD60864.1; -; Genomic_DNA.
DR   EMBL; BC081379; AAH81379.1; -; mRNA.
DR   RefSeq; NP_001004640.1; NM_001004640.3. [Q7ZZ25-1]
DR   AlphaFoldDB; Q7ZZ25; -.
DR   SMR; Q7ZZ25; -.
DR   STRING; 7955.ENSDARP00000035974; -.
DR   PaxDb; 7955-ENSDARP00000035974; -.
DR   GeneID; 368672; -.
DR   KEGG; dre:368672; -.
DR   AGR; ZFIN:ZDB-GENE-030616-593; -.
DR   CTD; 368672; -.
DR   ZFIN; ZDB-GENE-030616-593; atad1a.
DR   eggNOG; KOG0737; Eukaryota.
DR   HOGENOM; CLU_000688_21_14_1; -.
DR   InParanoid; Q7ZZ25; -.
DR   OrthoDB; 102713at2759; -.
DR   PhylomeDB; Q7ZZ25; -.
DR   TreeFam; TF105016; -.
DR   PRO; PR:Q7ZZ25; -.
DR   Proteomes; UP000000437; Chromosome 5.
DR   Bgee; ENSDARG00000023267; Expressed in blastula and 21 other cell types or tissues.
DR   ExpressionAtlas; Q7ZZ25; baseline and differential.
DR   GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR   GO; GO:0005778; C:peroxisomal membrane; ISS:UniProtKB.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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   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:SF8; 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   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Cell membrane; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; Nucleotide-binding; Peroxisome;
KW   Postsynaptic cell membrane; Reference proteome; Synapse; Translocase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..380
FT                   /note="Outer mitochondrial transmembrane helix translocase"
FT                   /id="PRO_0000084794"
FT   TOPO_DOM        1..18
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        19..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        38..380
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   BINDING         136..143
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         330..337
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_015632"
SQ   SEQUENCE   380 AA;  42580 MW;  ECF39E64F9A6CF52 CRC64;
     MLSDIPRDAL LRPLTRNEVV GMLVRLTVFG AATYYSIKWV VDALDPTQKQ KSQAKKRAEQ
     LMKQIGVEGV SLTEYEMNIA TLLVDPRSIK VTWRDVAGLD EIISEMQDTV ILPFQKRHLF
     SGSKLLQPPK GVLLYGPPGC GKTLIAKATA KASGCRFINL QASTLTDKWY GESQKLTAAV
     FSLAVKIQPC IIFLDEIDSF LRNRSSMDHE ATAMMKAQFM SLWDGLDTGE NSQVMVMGAT
     NRPQDVDAAI LRRMPTAFHV GLPNAAQREE ILRLILSGEN LSNAINLKEI ASQSEGYSGS
     DLKELCRDAA MYRVRDYVRK QQMKQIAQQF QLDEEEEHVD SRQLRPVTQL DLLFGLDKMR
     ESKQATATTD PANLREVPLD
//