ID   ATAD1_BOVIN             Reviewed;         361 AA.
AC   F6QV99; A7MB55;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2012, sequence version 2.
DT   03-AUG-2022, entry version 63.
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;
DE   AltName: Full=Thorase {ECO:0000250|UniProtKB:Q9D5T0};
GN   Name=ATAD1 {ECO:0000250|UniProtKB:Q8NBU5};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford;
RX   PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA   Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA   Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA   Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT   "A whole-genome assembly of the domestic cow, Bos taurus.";
RL   Genome Biol. 10:R42.01-R42.10(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) 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. Required for NMDA-stimulated AMPAR internalization and
CC       inhibition of GRIA1 and GRIA2 recycling back to the plasma membrane;
CC       these activities are ATPase-dependent (By similarity).
CC       {ECO:0000250|UniProtKB:P28737, ECO:0000250|UniProtKB:Q8NBU5,
CC       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   -!- SUBUNIT: Interacts with GRIA2 and GRIP1 in an ATP-dependent manner.
CC       ATAD1-catalyzed ATP hydrolysis disrupts not only its binding to GRIA2
CC       and GRIP1, but also interaction between GRIP1 and GRIA2, leading to
CC       AMPAR complex disassembly. {ECO:0000250|UniProtKB:Q9D5T0}.
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=AAI51347.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; DAAA02058710; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC151346; AAI51347.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001192510.1; NM_001205581.1.
DR   AlphaFoldDB; F6QV99; -.
DR   SMR; F6QV99; -.
DR   STRING; 9913.ENSBTAP00000001066; -.
DR   PaxDb; F6QV99; -.
DR   PRIDE; F6QV99; -.
DR   Ensembl; ENSBTAT00000001066; ENSBTAP00000001066; ENSBTAG00000000806.
DR   GeneID; 506045; -.
DR   KEGG; bta:506045; -.
DR   CTD; 84896; -.
DR   VEuPathDB; HostDB:ENSBTAG00000000806; -.
DR   VGNC; VGNC:26232; ATAD1.
DR   eggNOG; KOG0737; Eukaryota.
DR   GeneTree; ENSGT00550000074823; -.
DR   HOGENOM; CLU_000688_21_14_1; -.
DR   InParanoid; F6QV99; -.
DR   OMA; GPRWQQF; -.
DR   OrthoDB; 1430018at2759; -.
DR   Proteomes; UP000009136; Chromosome 26.
DR   Bgee; ENSBTAG00000000806; Expressed in semen and 105 other tissues.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
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:0005778; C:peroxisomal membrane; ISS: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; 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; 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   2: Evidence at transcript 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                   /evidence="ECO:0000255"
FT                   /id="PRO_0000416486"
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   MOD_RES         322
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D5T0"
SQ   SEQUENCE   361 AA;  40774 MW;  841A99A87FA74DDB CRC64;
     MVHAETFSRP 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