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
