ATD3A_DROME
ID ATD3A_DROME Reviewed; 604 AA.
AC Q9VEX6;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=ATPase family AAA domain-containing protein 3A homolog {ECO:0000250|UniProtKB:Q9NVI7};
DE AltName: Full=Belphegor protein {ECO:0000303|Ref.3};
GN Name=bor {ECO:0000303|Ref.3, ECO:0000312|FlyBase:FBgn0287225};
GN ORFNames=CG6815, Dmel_CG6815;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA Calgaro S.T., Boube M., Cribbs D.L., Bourbon H.M.;
RT "The Drosophila belphegor (bor) gene encodes a novel member of the AAA
RT family.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND MUTAGENESIS OF ARG-534.
RX PubMed=27640307; DOI=10.1016/j.ajhg.2016.08.007;
RG Baylor-Hopkins Center for Mendelian Genomics;
RG University of Washington Center for Mendelian Genomics;
RA Harel T., Yoon W.H., Garone C., Gu S., Coban-Akdemir Z., Eldomery M.K.,
RA Posey J.E., Jhangiani S.N., Rosenfeld J.A., Cho M.T., Fox S., Withers M.,
RA Brooks S.M., Chiang T., Duraine L., Erdin S., Yuan B., Shao Y.,
RA Moussallem E., Lamperti C., Donati M.A., Smith J.D., McLaughlin H.M.,
RA Eng C.M., Walkiewicz M., Xia F., Pippucci T., Magini P., Seri M.,
RA Zeviani M., Hirano M., Hunter J.V., Srour M., Zanigni S., Lewis R.A.,
RA Muzny D.M., Lotze T.E., Boerwinkle E., Gibbs R.A., Hickey S.E.,
RA Graham B.H., Yang Y., Buhas D., Martin D.M., Potocki L., Graziano C.,
RA Bellen H.J., Lupski J.R.;
RT "Recurrent de novo and biallelic variation of ATAD3A, encoding a
RT mitochondrial membrane protein, Results in distinct neurological
RT syndromes.";
RL Am. J. Hum. Genet. 99:831-845(2016).
CC -!- FUNCTION: Required to maintain the proper number of mitochondria in
CC neurons and muscles. {ECO:0000269|PubMed:27640307}.
CC -!- SUBUNIT: Can form homooligomers. {ECO:0000250|UniProtKB:Q9NVI7}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q9NVI7}. Mitochondrion matrix, mitochondrion
CC nucleoid {ECO:0000250|UniProtKB:Q9NVI7}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF227210; AAF43016.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF55289.2; -; Genomic_DNA.
DR EMBL; AE014297; AFH06453.1; -; Genomic_DNA.
DR EMBL; AF227209; AAF43014.1; -; mRNA.
DR RefSeq; NP_001247135.1; NM_001260206.1.
DR RefSeq; NP_524996.1; NM_080257.4.
DR AlphaFoldDB; Q9VEX6; -.
DR SMR; Q9VEX6; -.
DR IntAct; Q9VEX6; 14.
DR MINT; Q9VEX6; -.
DR STRING; 7227.FBpp0297140; -.
DR PaxDb; Q9VEX6; -.
DR PRIDE; Q9VEX6; -.
DR EnsemblMetazoa; FBtr0083276; FBpp0082728; FBgn0287225.
DR EnsemblMetazoa; FBtr0305998; FBpp0297140; FBgn0287225.
DR GeneID; 53565; -.
DR KEGG; dme:Dmel_CG6815; -.
DR UCSC; CG6815-RA; d. melanogaster.
DR CTD; 53565; -.
DR FlyBase; FBgn0287225; bor.
DR VEuPathDB; VectorBase:FBgn0287225; -.
DR eggNOG; KOG0742; Eukaryota.
DR GeneTree; ENSGT00730000111059; -.
DR HOGENOM; CLU_011488_2_0_1; -.
DR InParanoid; Q9VEX6; -.
DR OMA; KTCSKMA; -.
DR OrthoDB; 357201at2759; -.
DR PhylomeDB; Q9VEX6; -.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR SignaLink; Q9VEX6; -.
DR BioGRID-ORCS; 53565; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 53565; -.
DR PRO; PR:Q9VEX6; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR ExpressionAtlas; Q9VEX6; baseline and differential.
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; HDA:FlyBase.
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; IMP:UniProtKB.
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; 1.
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 ATP-binding; Coiled coil; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Mitochondrion nucleoid; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..604
FT /note="ATPase family AAA domain-containing protein 3A
FT homolog"
FT /id="PRO_0000439797"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 62..221
FT /evidence="ECO:0000255"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 358..365
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 534
FT /note="R->W: Decreases the number of mitochondria in motor
FT neurons or in body wall muscles."
FT /evidence="ECO:0000269|PubMed:27640307"
SQ SEQUENCE 604 AA; 68361 MW; 5DED4EFE025EFBD9 CRC64;
MSWLLGRNRQ QPQPDQTAGF SEGGGAADPE GRTAGEKSGD SQLSRAERKA MEAYRFDSSA
LERAADAAKT LERSKHAREA LELSKMQEAT RQTEYNTKVK EYEAHIEQAK VEQKRIDHEE
RRKTLIEETK QQQQRAQYQD QLSRKRYEDQ LLQQQRVQEE NLRKQEESVQ RQEAMRRQTI
EHEIEMKEKN RLKLLEHELR AKARVDRENR DINLEKIRLK AQEHRTTVLE GIKTAGTVIG
AGAEAMLTDW DKVLTAAGGL SLLALGVYTA KGATGVVSRY VEARIGKPTL VGETSRFAFL
DALKNPLHYL KRLRAKPTDA LQGVVLNPKL EERLRDIAIA TKNTRINKGM YRNVLMHGPP
GTGKTMFAKK LAEHSGMDFA IMTGGDVAPM GKEGVTAIHK VFDWSHTSRR GLLLFVDEAD
AFLRKRSSEK ISEDLRAALN AFLYRTSEQN PKFMLVLASN TPEQFDYAIN DRLDEMVEFT
LPGLEERERL LRLYFDKYVL QPAAAGAKRF KLDTFDYGKT CSKMAALCEG MSGREISKLG
VSWQAAVYAS EDGLLTEKMV LDRCYSAAQQ HKQKMAWLSD QERADHKSIT GTAAPPLTLT
AKKL
