ATD1B_DANRE
ID ATD1B_DANRE Reviewed; 362 AA.
AC Q503W7; Q5SQM1;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 110.
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-B {ECO:0000305};
GN Name=atad1b {ECO:0000250|UniProtKB:Q8NBU5};
GN ORFNames=si:bz1g13.1 {ECO:0000303|Ref.1},
GN zgc:110042 {ECO:0000303|PubMed:23594743};
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 MRNA].
RC TISSUE=Eye;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-281.
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).
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; BC095151; AAH95151.1; -; mRNA.
DR EMBL; AL731788; CAI11460.1; -; Genomic_DNA.
DR RefSeq; NP_001019592.1; NM_001024421.2.
DR RefSeq; XP_017213925.1; XM_017358436.1.
DR AlphaFoldDB; Q503W7; -.
DR SMR; Q503W7; -.
DR STRING; 7955.ENSDARP00000073585; -.
DR PaxDb; Q503W7; -.
DR Ensembl; ENSDART00000079130; ENSDARP00000073585; ENSDARG00000056609.
DR Ensembl; ENSDART00000189257; ENSDARP00000156137; ENSDARG00000056609.
DR GeneID; 368412; -.
DR KEGG; dre:368412; -.
DR CTD; 368412; -.
DR ZFIN; ZDB-GENE-030616-44; atad1b.
DR eggNOG; KOG0737; Eukaryota.
DR GeneTree; ENSGT00550000074823; -.
DR HOGENOM; CLU_000688_21_14_1; -.
DR InParanoid; Q503W7; -.
DR OMA; GPRWQQF; -.
DR OrthoDB; 1430018at2759; -.
DR PhylomeDB; Q503W7; -.
DR TreeFam; TF105016; -.
DR Reactome; R-DRE-9603798; Class I peroxisomal membrane protein import.
DR PRO; PR:Q503W7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 12.
DR Bgee; ENSDARG00000056609; Expressed in testis and 22 other tissues.
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..362
FT /note="Outer mitochondrial transmembrane helix translocase"
FT /id="PRO_0000084795"
FT TOPO_DOM 1..19
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 20..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..362
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT BINDING 137..144
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 95
FT /note="H -> Y (in Ref. 2; AAH95151)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="V -> A (in Ref. 2; AAH95151)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 362 AA; 41094 MW; 70136A5CC5CF05EC CRC64;
MVLKEIPTEN ITRPLGRNEV IGLLFRLTIF GAVTYFTIKW MVDAIDPTRK QKVEAQKQAE
KLMRQIGVQN VKLSEYEMSI AAHLVDPLTM QITWHDIAGL DEVITELKDT VILPIQKRHL
FEGSRLLQPP KGVLLYGPPG CGKTLIAKAT AKEAGFRFIN LQPSTLTDKW YGESQKLAAA
VFSLAIKLQP SIIFIDEIDS FLRNRSSSDH EATAMMKAQF MSLWDGLDTD YNCQVIIMGA
TNRPQDLDSA ILRRMPTRFH INQPNVRQRK DILKLILENE NVESAVELSE IAKQTDGFSG
SDLREMCRDA ALLCVRDFVH QESPEEDFIR PIRQEDLQRA IEKMKKSKSA GVHEAFMQVP
LD
