ATAD3_BOVIN
ID ATAD3_BOVIN Reviewed; 586 AA.
AC A7YWC4;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=ATPase family AAA domain-containing protein 3;
GN Name=ATAD3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP INDUCTION.
RX PubMed=20154147; DOI=10.1128/mcb.00007-10;
RA Gilquin B., Taillebourg E., Cherradi N., Hubstenberger A., Gay O.,
RA Merle N., Assard N., Fauvarque M.O., Tomohiro S., Kuge O., Baudier J.;
RT "The AAA+ ATPase ATAD3A controls mitochondrial dynamics at the interface of
RT the inner and outer membranes.";
RL Mol. Cell. Biol. 30:1984-1996(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 S100B in a Ca(+2)- and
CC Zn(+2)-dependent manner; this interaction probably occurs in the
CC cytosol prior to mitochondrial targeting. S100B could assist ATAD3A
CC cytoplasmic processing, preventing aggregation and favoring
CC mitochondrial localization. Interacts with HSP60/HSPD1. Forms
CC heterooligomers with ATAD3B; this interaction may affect ATAD3A
CC activity. Interacts with CLPB. {ECO:0000250|UniProtKB:Q9NVI7}.
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 -!- INDUCTION: Up-regulated by Angiotensin/AGT.
CC {ECO:0000269|PubMed:20154147}.
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; BC134487; AAI34488.1; -; mRNA.
DR RefSeq; NP_001098932.1; NM_001105462.1.
DR AlphaFoldDB; A7YWC4; -.
DR SMR; A7YWC4; -.
DR STRING; 9913.ENSBTAP00000012676; -.
DR PaxDb; A7YWC4; -.
DR PRIDE; A7YWC4; -.
DR Ensembl; ENSBTAT00000012676; ENSBTAP00000012676; ENSBTAG00000002219.
DR GeneID; 784353; -.
DR KEGG; bta:784353; -.
DR CTD; 55210; -.
DR VEuPathDB; HostDB:ENSBTAG00000002219; -.
DR eggNOG; KOG0742; Eukaryota.
DR GeneTree; ENSGT00730000111059; -.
DR HOGENOM; CLU_011488_2_0_1; -.
DR InParanoid; A7YWC4; -.
DR OMA; KTCSKMA; -.
DR OrthoDB; 357201at2759; -.
DR TreeFam; TF313922; -.
DR Reactome; R-BTA-6798695; Neutrophil degranulation.
DR Proteomes; UP000009136; Chromosome 16.
DR Bgee; ENSBTAG00000002219; Expressed in digestive system secreted substance and 104 other tissues.
DR ExpressionAtlas; A7YWC4; baseline and differential.
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:0140374; P:antiviral innate immune response; IEA:Ensembl.
DR GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0001558; P:regulation of cell growth; IEA:Ensembl.
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 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..586
FT /note="ATPase family AAA domain-containing protein 3"
FT /id="PRO_0000311980"
FT TOPO_DOM 2..245
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..586
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..218
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 586 AA; 66107 MW; ED989EB4FECEDE46 CRC64;
MSWLFGIKGS KGEGTGPPLP LPPVQPGGEG SGDGGAGDRP GPKDKWSNFD PTGLERAAKA
ARELEHSRHA KEALSLAQMQ EQTLQLEHQA KLKEYEAAVE QLKGDQIRVQ AEERRKTLSE
ETRQHQARAQ YQDKLARQRY EDQLKQQQLL NEENLRKQEE SVQKQEALRR ATVEREMELR
HKNEMLRVEA EARARAKAER ENADIIREQI RLKAAEHRQT ILESIRTAGT LFGEGFRAFV
TDWDKVTATV AGLTLLAVGI YSAKNATSVA GRYIEARLGK PSLVRETSRI TVLEALRHPI
QVSRRLLSKP QDALEGVVLS PSLEARVRDI AIATRNTKKN KSLYRNVLMY GPPGTGKTLF
AKKLALHSGM DYAIMTGGDV APMGRDGVTA MHKVFDWAST SRRGLLLFVD EADAFLRKRA
TEKISEDLRA TLNAFLHRTG QHSSKFMLVL ASNQPEQFDW AINDRIDEMV SFELPQREER
ERLVRMYFDK YVLKPATEGK QRLKLAQFDY GKKCSEIAQL TEGMSGREIS QLAVAWQAMA
YASEDGVLTE AMMDARVQDA IQQHRQKMQW LKAEGSQPPT LRTQAE
