DAXX_DROME
ID DAXX_DROME Reviewed; 1659 AA.
AC Q9VMD0; Q6NNF9;
DT 31-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 3.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Daxx-like protein {ECO:0000303|PubMed:28320872};
DE Short=DLP {ECO:0000303|PubMed:28320872};
GN Name=Daxx {ECO:0000312|FlyBase:FBgn0031820};
GN ORFNames=CG9537 {ECO:0000312|FlyBase:FBgn0031820};
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 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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] {ECO:0000312|EMBL:AAR96121.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAR96121.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAR96121.1};
RA Stapleton M., Carlson J., Chavez C., Frise E., George R., Pacleb J.,
RA Park S., Wan K., Yu C., Rubin G.M., Celniker S.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH P53, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17933869; DOI=10.1074/jbc.m705547200;
RA Bodai L., Pardi N., Ujfaludi Z., Bereczki O., Komonyi O., Balint E.,
RA Boros I.M.;
RT "Daxx-like protein of Drosophila interacts with Dmp53 and affects longevity
RT and Ark mRNA level.";
RL J. Biol. Chem. 282:36386-36393(2007).
RN [5] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=23593018; DOI=10.1371/journal.pgen.1003412;
RA Hwang S., Song S., Hong Y.K., Choi G., Suh Y.S., Han S.Y., Lee M.,
RA Park S.H., Lee J.H., Lee S., Bang S.M., Jeong Y., Chung W.J., Lee I.S.,
RA Jeong G., Chung J., Cho K.S.;
RT "Drosophila DJ-1 decreases neural sensitivity to stress by negatively
RT regulating Daxx-like protein through dFOXO.";
RL PLoS Genet. 9:E1003412-E1003412(2013).
RN [6] {ECO:0000305}
RP FUNCTION, INTERACTION WITH HIS3.3A; HIS3.3B AND ASF1, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RX PubMed=28320872; DOI=10.1128/mcb.00597-16;
RA Fromental-Ramain C., Ramain P., Hamiche A.;
RT "The Drosophila DAXX-Like Protein (DLP) Cooperates with ASF1 for H3.3
RT Deposition and Heterochromatin Formation.";
RL Mol. Cell. Biol. 37:0-0(2017).
CC -!- FUNCTION: Transcription regulator (PubMed:23593018, PubMed:17933869).
CC Acts as a histone chaperone that facilitates deposition of histone H3.3
CC (PubMed:28320872). Has a role in chromatin remodeling together with
CC asf1 and XNP (PubMed:28320872). Has role in the transcriptional
CC apoptotic response to oxidative and UV stress (PubMed:17933869,
CC PubMed:23593018). {ECO:0000269|PubMed:17933869,
CC ECO:0000269|PubMed:23593018, ECO:0000269|PubMed:28320872}.
CC -!- SUBUNIT: Interacts with p53 (via C-terminus) (PubMed:17933869).
CC Interacts (via C-terminus) with His3.3A and His3.3B (PubMed:28320872).
CC Interacts with asf1 (PubMed:28320872). {ECO:0000269|PubMed:17933869,
CC ECO:0000269|PubMed:28320872}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:23593018}.
CC Nucleus {ECO:0000269|PubMed:23593018}. Chromosome
CC {ECO:0000269|PubMed:28320872}. Note=Localization to the nucleus is
CC regulated by dj-1beta and oxidative stress (PubMed:23593018). Localizes
CC to pericentric heterochromatin associated with chromosomes X and 4
CC (PubMed:28320872). {ECO:0000269|PubMed:23593018,
CC ECO:0000269|PubMed:28320872}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with higher levels in the
CC head (at protein level) (PubMed:23593018). Expressed in the germ line,
CC with prominent expression in primary spermatocytes and meiotic
CC spermatocytes (at protein level) (PubMed:28320872). In ovaries,
CC expressed in nurse cells and in the germinal vesicle of the ovarian
CC follicle at stage 10 (at protein level) (PubMed:28320872).
CC {ECO:0000269|PubMed:23593018, ECO:0000269|PubMed:28320872}.
CC -!- DEVELOPMENTAL STAGE: Expressed in all developmental stages
CC (PubMed:17933869). Higher level of expression detected at the end of
CC the third larval stage, in adult females and in early embryos
CC containing maternally deposited transcripts (PubMed:17933869). At later
CC stages of development, specific expression can be detected in tissues
CC containing mitotic cells such as in the brain hemispheres and imaginal
CC disks (PubMed:17933869). {ECO:0000269|PubMed:17933869}.
CC -!- DISRUPTION PHENOTYPE: Reduces longevity and female fertility, but
CC increases resistance to oxidative stress and UV irradiation-induced
CC pupal lethality (PubMed:23593018). Double knockouts for DJ-1beta and
CC Daxx restore normal number of dopaminergic neurons, locomotor activity
CC and sensitivity to oxidative stress and UV-induced damage
CC (PubMed:23593018). RNAi-mediated knockdown results in increased
CC resistance to oxidative stress (PubMed:23593018).
CC {ECO:0000269|PubMed:23593018}.
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DR EMBL; AE014134; AAF52390.3; -; Genomic_DNA.
DR EMBL; AE014134; AHN54190.1; -; Genomic_DNA.
DR EMBL; BT011329; AAR96121.1; -; mRNA.
DR RefSeq; NP_001285675.1; NM_001298746.1.
DR RefSeq; NP_609035.2; NM_135191.3.
DR AlphaFoldDB; Q9VMD0; -.
DR SMR; Q9VMD0; -.
DR IntAct; Q9VMD0; 3.
DR STRING; 7227.FBpp0078890; -.
DR PaxDb; Q9VMD0; -.
DR EnsemblMetazoa; FBtr0079260; FBpp0078890; FBgn0031820.
DR EnsemblMetazoa; FBtr0344764; FBpp0311092; FBgn0031820.
DR GeneID; 33906; -.
DR KEGG; dme:Dmel_CG9537; -.
DR UCSC; CG9537-RA; d. melanogaster.
DR CTD; 1616; -.
DR FlyBase; FBgn0031820; Daxx.
DR VEuPathDB; VectorBase:FBgn0031820; -.
DR eggNOG; ENOG502QRS6; Eukaryota.
DR GeneTree; ENSGT00390000009448; -.
DR HOGENOM; CLU_004145_0_0_1; -.
DR InParanoid; Q9VMD0; -.
DR OMA; LNANFVH; -.
DR OrthoDB; 447891at2759; -.
DR PhylomeDB; Q9VMD0; -.
DR Reactome; R-DME-9670095; Inhibition of DNA recombination at telomere.
DR BioGRID-ORCS; 33906; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Daxx; fly.
DR GenomeRNAi; 33906; -.
DR PRO; PR:Q9VMD0; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0031820; Expressed in egg cell and 25 other tissues.
DR ExpressionAtlas; Q9VMD0; baseline and differential.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016605; C:PML body; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0006334; P:nucleosome assembly; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:FlyBase.
DR GO; GO:0042981; P:regulation of apoptotic process; IGI:FlyBase.
DR GO; GO:0006979; P:response to oxidative stress; IMP:FlyBase.
DR CDD; cd13150; DAXX_histone_binding; 1.
DR Gene3D; 1.10.8.810; -; 1.
DR Gene3D; 1.20.58.2170; -; 1.
DR InterPro; IPR046378; DAXX_histone_binding.
DR InterPro; IPR046426; DAXX_histone_binding_sf.
DR InterPro; IPR038298; Daxx_N_sf.
PE 1: Evidence at protein level;
KW Apoptosis; Chaperone; Chromosome; Coiled coil; Cytoplasm; Nucleus;
KW Reference proteome.
FT CHAIN 1..1659
FT /note="Daxx-like protein"
FT /id="PRO_0000447643"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 870..1659
FT /note="Necessary for interaction with His3.3A and His3.3B"
FT /evidence="ECO:0000269|PubMed:28320872"
FT REGION 872..894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 924..952
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1023..1060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1536..1555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 438..469
FT /evidence="ECO:0000255"
FT COMPBIAS 265..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..333
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 596
FT /note="T -> K (in Ref. 3; AAR96121)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1659 AA; 183875 MW; 781552C81CDFAB83 CRC64;
MSASVICVDL SSESDEESPA KRRRLEDPLR LLTPSGRQSF PAKLLNIPKA SLGSAMVVPV
AETGPARETP VIVDPLRSMH IPSGITITKH QKNVLATNGN MNLSLAESNN NNNTTSLNKN
VTPKQINVGT GQKVAWSVSS KAPSPNAVIT TVPSHQVRVT PFNPIRLAPG SKIIPASNAM
PAKIQPILGM GQPQQQAQAQ QPKAIIVGFP KPNTAVAQMA QHQKPLTLQI HQKLIAGQQQ
HIASISQLQQ VSLQQQQPLR PVSIQLQQQQ NQRNGSLPGK QQKPLECPVP AQQEKLPRGP
LPTKPAEPLS GPLPTEPDEP LGGPLPTRPK PPVRSLQQPV NKNTAIGVQI QQSQEPLGGT
LPTRQKPLGG QLLTQQKPPV GSIQQSVKQN TGIGVQIQQI PKVVVGQQPQ KVYLNKLQQE
QQKIFLGHLQ QQQQKTFLGQ LQQEQQKILG QLQQQKQQQQ QQQKKILGQS QQQKVPLGQP
QPQQKLPQQL NNSLVQLQQQ HQQRTSVGQL QQQQPHQSQQ KNSMVHVKQQ PQQQKKISVG
QFQQQPQQQQ KTSVAQLQQQ PQQQQKISVG QLQQQSQQQQ KPSVGQLQQQ SQQQQTPLVG
QLQRQTQQQQ KTSAGQFQQQ PQQQQKISAG QLQEHSQQQQ KTLAGQLQQQ AQQQLNTSAG
QLQQQQKPPK ASLAQQAAAQ KQGAGLGQQQ QFQSQPQQRT SAGLLQQQQM PQKKIVMQPQ
LPKTSVVLPR PQQLPKNPLL VAQQQSPKTP LVNSVMGPQF PSQQPSLPVV NQITHKSMTI
QRLPMLQTVQ KILPKQIAPQ QTPPPAHIVQ KQTMPNAAMQ NPPFAHRPPI VRPMTVAKIS
PVPTNNKVCI PMKPQMASYV SPTDPTMTAA RTLPFRSSQR KTSEAPMTST HVQGFTASAT
PPQRLLATPP HCAAALNEPL LLNLPPTTSI TPQLTPTTTP PPAGPSAAVQ QQQLAKAAAI
KLNSLPEASI SPVNRSPTAS AKRIQPITVL KKSDEEWQRH LEQQQQKKHV QLQSSSMTTI
VLVESPPTTP PTDKPEPERG PMTVEKSSIK PMATDKQSRA IKRPAVMIST KKSGLVVTEI
VDLDEIPDIP PEKRGKECFP PIKNAAKAAP SVNAPFTTEY AALLRLCREV DKSTHMERLV
KGELTQYYYS APESFVMSCG FRNLVTMAMA RIRSESYLVY VHLKYVLDEL ASRRLTKMFP
TVRAIPPASQ FPLPPASQFP LPPTLTTPKQ PAIVKAPGQQ TVMAGREQDD EVEEVTLVNV
GTVSCEERRR DERIRHFYRT LHAITKRIKM LEEAEVDLND EDSSYLQLER FKKRACQIYE
KICDLKGESK SVRRQLKKPI HFKDSDYPHF NNSLSAFVNR MQDFPDYHDV LQILEKCNKE
KELGLAKYEM KRIAYDAFNK VGRMLQSRRK NDLYETVTHY TANGKDPASS DPELLAKLKE
NNKKQTKISD ILEKYALEQD LNAEERQEAR LKEKKLKQVK ADEEAAKLAA LAEDDDKPCT
SAQAAAKAAA LAALKRGPAA RGNVIRKKRA ANGRIFKIAD DGDDSEEESD SEDDDVEEFV
NNFQANSDVS DADSEVEAVT SPKRDALPLA EEEDVIDITR DETGKKNDEG TPNGRLKIMS
VSSLNANFVH GQDLHRKPNP MPSAKPVIAD QIIISDEES
