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ATAD1_XENTR
ID   ATAD1_XENTR             Reviewed;         360 AA.
AC   B4F6J6; F7CNN7;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2012, sequence version 2.
DT   03-AUG-2022, entry version 76.
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};
GN   Name=atad1 {ECO:0000250|UniProtKB:Q8NBU5};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20431018; DOI=10.1126/science.1183670;
RA   Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA   Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA   Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA   Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA   Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA   Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA   Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA   Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA   Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT   "The genome of the Western clawed frog Xenopus tropicalis.";
RL   Science 328:633-636(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2008) 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   -!- SIMILARITY: Belongs to the AAA ATPase family. MSP1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AAMC01046255; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC167903; AAI67903.1; -; mRNA.
DR   RefSeq; NP_001135501.1; NM_001142029.1.
DR   RefSeq; XP_012821650.1; XM_012966196.2.
DR   AlphaFoldDB; B4F6J6; -.
DR   SMR; B4F6J6; -.
DR   PaxDb; B4F6J6; -.
DR   Ensembl; ENSXETT00000020353; ENSXETP00000020353; ENSXETG00000009266.
DR   GeneID; 100216041; -.
DR   KEGG; xtr:100216041; -.
DR   CTD; 84896; -.
DR   Xenbase; XB-GENE-5779938; atad1.
DR   eggNOG; KOG0737; Eukaryota.
DR   HOGENOM; CLU_000688_21_14_1; -.
DR   InParanoid; B4F6J6; -.
DR   OMA; GPRWQQF; -.
DR   OrthoDB; 1430018at2759; -.
DR   PhylomeDB; B4F6J6; -.
DR   Reactome; R-XTR-9603798; Class I peroxisomal membrane protein import.
DR   Proteomes; UP000008143; Chromosome 7.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000009266; Expressed in 4-cell stage embryo and 13 other tissues.
DR   ExpressionAtlas; B4F6J6; baseline and differential.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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; 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:transmembrane protein dislocase activity; IEA:RHEA.
DR   GO; GO:0140570; P:extraction of mislocalized protein from mitochondrial outer membrane; ISS:UniProtKB.
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   Postsynaptic cell membrane; Reference proteome; Synapse; Translocase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..360
FT                   /note="Outer mitochondrial transmembrane helix translocase"
FT                   /id="PRO_0000416487"
FT   TOPO_DOM        1..15
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        16..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        35..360
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   CONFLICT        185
FT                   /note="Q -> H (in Ref. 2; AAI67903)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   360 AA;  40492 MW;  428543C0E8C7A0DE CRC64;
     MVHGEAFSRP LSRNEVVGLI FRLTIFGAVT YFTIKWMVDA IDPTRKQKVE AQKQAEKLMR
     QIGVKNVKLT EYEMSIAAHL VDPLSMLVTW SDIAGLDDVI TDLKDTVILP IRKRYLFENS
     RLLQPPKGVL LYGPPGCGKT MIAKATAKEA GCRFINLQPS TLTDKWYGES QKLAAAVFSL
     AVKLQPSIIF IDEIDSFLRS RSSSDHEATA MMKAQFMSLW DGLDTDFNCQ VIVMGATNRP
     QDLDTAIMRR MPTRFHINQP SLKQREAILD LILRNESVDS HVDLMEIARG SDGFSGSDLK
     EMCRDAALLC VRDSVNNSSE ESPCEEIRPI HQQDLLRAID KMKRSKSATN QNVLMHVSLD
 
 
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