ATAD3_RAT
ID ATAD3_RAT Reviewed; 591 AA.
AC Q3KRE0;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=ATPase family AAA domain-containing protein 3;
GN Name=Atad3; Synonyms=Atad3a;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=17210950; DOI=10.1083/jcb.200609158;
RA He J., Mao C.C., Reyes A., Sembongi H., Di Re M., Granycome C.,
RA Clippingdale A.B., Fearnley I.M., Harbour M., Robinson A.J., Reichelt S.,
RA Spelbrink J.N., Walker J.E., Holt I.J.;
RT "The AAA+ protein ATAD3 has displacement loop binding properties and is
RT involved in mitochondrial nucleoid organization.";
RL J. Cell Biol. 176:141-146(2007).
RN [3]
RP INTERACTION WITH S100B, AND DEVELOPMENTAL STAGE.
RX PubMed=20351179; DOI=10.1128/mcb.01468-09;
RA Gilquin B., Cannon B.R., Hubstenberger A., Moulouel B., Falk E., Merle N.,
RA Assard N., Kieffer S., Rousseau D., Wilder P.T., Weber D.J., Baudier J.;
RT "The calcium-dependent interaction between S100B and the mitochondrial AAA
RT ATPase ATAD3A and the role of this complex in the cytoplasmic processing of
RT ATAD3A.";
RL Mol. Cell. Biol. 30:2724-2736(2010).
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. Involved in mitochondrial-mediated antiviral innate
CC immunity. {ECO:0000250|UniProtKB:Q9NVI7}.
CC -!- SUBUNIT: Can form homooligomers. Homodimer formation at the N-terminus
CC may be regulated by ATP and is required for the interaction with the
CC inner surface of the mitochondrial outer membrane and correct
CC mitochondrial homeostasis. Interacts with components of the
CC mitochondrial ribosome and with other proteins involved in
CC mitochondrial RNA metabolism. May also interact with protein involved
CC in lipid metabolism, including STARD9. May interact with FAM210A.
CC Interacts with GADD45GIP1. Interacts with HSP60/HSPD1. Forms
CC heterooligomers with ATAD3B; this interaction may affect ATAD3A
CC activity (By similarity). Interacts with S100B in a Ca(+2)- and Zn(+2)-
CC dependent manner; this interaction probably occurs in the cytosol prior
CC to mitochondrial targeting. S100B could assist ATAD3A cytoplasmic
CC processing, preventing aggregation and favoring mitochondrial
CC localization (PubMed:20351179). Interacts with CLPB (By similarity).
CC {ECO:0000250|UniProtKB:Q9NVI7, ECO:0000269|PubMed:20351179}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000269|PubMed:17210950}. Mitochondrion inner membrane
CC {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
CC Mitochondrion matrix, mitochondrion nucleoid {ECO:0000250}. Note=Lacks
CC a canonical N-terminal mitochondrial targeting signal. Has been shown
CC to be very tightly associated with mitochondrial inner membrane. The N-
CC terminus being either exposed to the cytosol or located in an
CC accessible intermembrane space. Exposure to the cytosol would imply a
CC second transmembrane that could not be predicted. The C-terminus is
CC facing the matrix. In the matrix, may be associated with nucleoids (By
CC similarity). {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated during oligodendrocyte progenitor
CC cell differentiation. {ECO:0000269|PubMed:20351179}.
CC -!- DOMAIN: The transmembrane domain and a C-terminal adjacent region
CC contain all information necessary for mitochondrial targeting.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; BC105762; AAI05763.1; -; mRNA.
DR RefSeq; NP_001030094.1; NM_001034922.1.
DR AlphaFoldDB; Q3KRE0; -.
DR SMR; Q3KRE0; -.
DR BioGRID; 255984; 1.
DR IntAct; Q3KRE0; 1.
DR STRING; 10116.ENSRNOP00000046842; -.
DR iPTMnet; Q3KRE0; -.
DR PhosphoSitePlus; Q3KRE0; -.
DR jPOST; Q3KRE0; -.
DR PaxDb; Q3KRE0; -.
DR PRIDE; Q3KRE0; -.
DR Ensembl; ENSRNOT00000045053; ENSRNOP00000046842; ENSRNOG00000018118.
DR GeneID; 298682; -.
DR KEGG; rno:298682; -.
DR CTD; 55210; -.
DR RGD; 1305964; Atad3a.
DR eggNOG; KOG0742; Eukaryota.
DR GeneTree; ENSGT00730000111059; -.
DR HOGENOM; CLU_011488_2_0_1; -.
DR InParanoid; Q3KRE0; -.
DR OMA; KTCSKMA; -.
DR OrthoDB; 357201at2759; -.
DR PhylomeDB; Q3KRE0; -.
DR TreeFam; TF313922; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:Q3KRE0; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000018118; Expressed in ovary and 19 other tissues.
DR Genevisible; Q3KRE0; RN.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:RGD.
DR GO; GO:0042645; C:mitochondrial nucleoid; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140374; P:antiviral innate immune response; ISS:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:0001558; P:regulation of cell growth; ISO:RGD.
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 1: Evidence at protein level;
KW Acetylation; ATP-binding; Coiled coil; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Mitochondrion nucleoid; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q5T9A4"
FT CHAIN 2..591
FT /note="ATPase family AAA domain-containing protein 3"
FT /id="PRO_0000311981"
FT TOPO_DOM 2..245
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..591
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..49
FT /note="Required for interaction with the inner surface of
FT the mitochondrial outer membrane"
FT /evidence="ECO:0000250"
FT REGION 289..304
FT /note="S100B-binding"
FT /evidence="ECO:0000250"
FT COILED 55..216
FT /evidence="ECO:0000255"
FT BINDING 351..358
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T9A4"
FT MOD_RES 490
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q925I1"
FT MOD_RES 490
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q925I1"
FT MOD_RES 494
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q925I1"
FT MOD_RES 512
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q925I1"
SQ SEQUENCE 591 AA; 66759 MW; B436447F34E949DE CRC64;
MSWLFGIKGP KGEGTGPPLP LPPAQPGAES GGDRGAGDRP SPKDKWSNFD PTGLERAAKA
ARELEHSRHA KEALNLAQMQ EQTLQLEQQS KLKEYEAAVE QLKSEQIRVQ AEERRKTLNE
ETRQHQARAQ YQDKLARQRY EDQLKQQQLL NEENLRKQEE SVQKQEAIRR ATVEREMELR
HKNEMLRVEA EARARAKADR ENADIIREQI RLKAAEHRQT ILESIRTAGT LFGEGFRAFV
TDWDKVTATV AGLTLLAVGV YSAKNATSVA GRYIEARLGK PSLVRETSRI SVLEALRHPI
QVSRRLVSRP QDALEGVILS PSLEARVRDI AIATRNTKKN KSLYRNVLMY GPPGTGKTLF
AKKLALHSGM DYAIMTGGDV APMGREGVTA MHKVFDWAST SRRGLLLFVD EADAFLRKRA
TEKISEDLRA TLNAFLHRTG QHSNKFMLVL ASNQPEQFDW AINDRIDEMV CFALPQREER
ERLVRMYFDK YVLKPATEGK QRLKVAQFDY GKKCSEVAQL TAGMSGREIA QLAVAWQAMA
YSSEDGVLTE AMMDARVQDA VQQHQQKMQW LKVERPDSEA SKPPHPSLLS C
