ID   ATAD3_XENTR             Reviewed;         594 AA.
AC   Q6NVR9;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=ATPase family AAA domain-containing protein 3;
GN   Name=atad3;
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 MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Essential for mitochondrial network organization,
CC       mitochondrial metabolism and cell growth at organism and cellular
CC       level. May play an important role in mitochondrial protein synthesis.
CC       May also participate in mitochondrial DNA replication. May bind to
CC       mitochondrial DNA D-loops and contribute to nucleoid stability.
CC       Required for enhanced channeling of cholesterol for hormone-dependent
CC       steroidogenesis (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Single-pass membrane protein {ECO:0000250}. Mitochondrion matrix,
CC       mitochondrion nucleoid {ECO:0000250}. Note=In the mitochondrial inner
CC       membrane, enriched in sites with the potential to form contacts with
CC       the outer membrane. The N-terminal domain interacts with the inner
CC       surface of the mitochondrial outer membrane and the C-terminal domain
CC       localizes in a specific matrix compartment, where it is associated with
CC       nucleoids (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR   EMBL; BC067935; AAH67935.1; -; mRNA.
DR   RefSeq; NP_998849.1; NM_213684.1.
DR   AlphaFoldDB; Q6NVR9; -.
DR   SMR; Q6NVR9; -.
DR   PaxDb; Q6NVR9; -.
DR   DNASU; 407895; -.
DR   Ensembl; ENSXETT00000028394; ENSXETP00000028394; ENSXETG00000012959.
DR   GeneID; 407895; -.
DR   KEGG; xtr:407895; -.
DR   CTD; 55210; -.
DR   Xenbase; XB-GENE-946129; atad3a.
DR   eggNOG; KOG0742; Eukaryota.
DR   HOGENOM; CLU_011488_2_0_1; -.
DR   InParanoid; Q6NVR9; -.
DR   OMA; RSKLIMT; -.
DR   OrthoDB; 357201at2759; -.
DR   PhylomeDB; Q6NVR9; -.
DR   TreeFam; TF313922; -.
DR   Reactome; R-XTR-6798695; Neutrophil degranulation.
DR   Proteomes; UP000008143; Chromosome 7.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000012959; Expressed in ovary and 14 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042645; C:mitochondrial nucleoid; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR039188; ATAD3.
DR   InterPro; IPR021911; ATAD3_N.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR23075; PTHR23075; 2.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF12037; DUF3523; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Coiled coil; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Mitochondrion nucleoid; Nucleotide-binding;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..594
FT                   /note="ATPase family AAA domain-containing protein 3"
FT                   /id="PRO_0000311984"
FT   TOPO_DOM        1..242
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        243..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        261..594
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          571..594
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          51..213
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        34..50
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         348..355
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   594 AA;  66860 MW;  B7308B72ABD14C6D CRC64;
     MSWLFGLNKG QQGPPSVPGF PEPPSPPGGS GDGGDKNKPK DKWSNFDPTG LERAAKAARE
     LDQSRHAKEA LNLAKVQEET LQLEQQSKIK EYEAAVEQLK NEQIRVQAEE RRKTLNEETK
     QHQARAQYQD KLARQRYEDQ LRQQQLQNEE NLRRQEESVQ KQEAMRKATV EHEMELRHKN
     EMLRIEAEAR ARAKVERENA DIIRENIRLK AAEHRQTVLE SIKTAGTVFG EGFRAFISDW
     DKVTATVAGL SLLAVGIYTA KNATGVAGRY IEARLGKPSL VRDTSRFTVA EAVKHPVKIS
     KRLLSKIQDA LEGVILSPKL EERVRDIAIA TRNTKANKGL YRNILMYGPP GTGKTLFAKK
     LAMHSGMDYA IMTGGDVAPM GREGVTAMHK VFDWAGTSKR GLLLFVDEAD AFLRKRSTEK
     ISEDLRATLN AFLYRTGEQS NKFMLVLASN QPEQFDWAIN DRIDEIVHFD LPGLEERERL
     VRLYFDKYVL QPASEGKQRL KVAQFDYGKK CSDLAQLTEG MSGREISKLG VAWQAAAYAS
     EDGILNEAMI DARVADAIRQ HQQKMEWLKA EGKENAAKES GKNPLQPLLE GTPV