ATRX_DROME
ID ATRX_DROME Reviewed; 1311 AA.
AC Q9GQN5; A4V3E4; Q9VBQ8;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2001, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Transcriptional regulator ATRX homolog;
DE EC=3.6.4.12;
DE AltName: Full=ATP-dependent helicase XNP;
DE AltName: Full=X-linked nuclear protein;
DE AltName: Full=d-xnp;
DE AltName: Full=dXNP;
GN Name=XNP; ORFNames=CG4548;
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 [MRNA].
RA Cardoso C., Usseglio F., Villard L., Manfruelli P., Rothbacher U.,
RA Aragnol D., Pradel J., Fontes M.;
RT "d-xnp: Drosophila melanogaster xnp/atr-x gene.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126; SER-127; SER-267;
RP SER-268; SER-270; SER-336; SER-338; SER-342; SER-343; SER-857 AND SER-859,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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: Global transcriptional regulator. Modifies gene expression by
CC affecting chromatin. {ECO:0000269|PubMed:28320872}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28320872}. Chromosome
CC {ECO:0000269|PubMed:28320872}. Note=Localizes to pericentric
CC heterochromatin associated with the X chromosome.
CC {ECO:0000269|PubMed:28320872}.
CC -!- DISRUPTION PHENOTYPE: Deregulates heterochromatin silencing.
CC {ECO:0000269|PubMed:28320872}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; AF217802; AAG40586.1; -; mRNA.
DR EMBL; AE014297; AAF56471.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN14055.1; -; Genomic_DNA.
DR EMBL; AY058592; AAL13821.1; -; mRNA.
DR RefSeq; NP_651398.1; NM_143141.4.
DR RefSeq; NP_733107.1; NM_170228.3.
DR AlphaFoldDB; Q9GQN5; -.
DR SMR; Q9GQN5; -.
DR BioGRID; 67994; 11.
DR IntAct; Q9GQN5; 1.
DR STRING; 7227.FBpp0084212; -.
DR iPTMnet; Q9GQN5; -.
DR PaxDb; Q9GQN5; -.
DR PRIDE; Q9GQN5; -.
DR DNASU; 43080; -.
DR EnsemblMetazoa; FBtr0084837; FBpp0084212; FBgn0039338.
DR EnsemblMetazoa; FBtr0084838; FBpp0084213; FBgn0039338.
DR GeneID; 43080; -.
DR KEGG; dme:Dmel_CG4548; -.
DR UCSC; CG4548-RA; d. melanogaster.
DR CTD; 43080; -.
DR FlyBase; FBgn0039338; XNP.
DR VEuPathDB; VectorBase:FBgn0039338; -.
DR eggNOG; KOG1015; Eukaryota.
DR GeneTree; ENSGT00940000155902; -.
DR InParanoid; Q9GQN5; -.
DR OrthoDB; 815681at2759; -.
DR PhylomeDB; Q9GQN5; -.
DR SignaLink; Q9GQN5; -.
DR BioGRID-ORCS; 43080; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 43080; -.
DR PRO; PR:Q9GQN5; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0039338; Expressed in wing disc and 43 other tissues.
DR ExpressionAtlas; Q9GQN5; baseline and differential.
DR Genevisible; Q9GQN5; DM.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0042585; C:germinal vesicle; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:FlyBase.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0015616; F:DNA translocase activity; IDA:FlyBase.
DR GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:0051276; P:chromosome organization; IMP:FlyBase.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006336; P:DNA replication-independent chromatin assembly; IMP:FlyBase.
DR GO; GO:0008347; P:glial cell migration; IMP:FlyBase.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; IMP:FlyBase.
DR GO; GO:0007399; P:nervous system development; IMP:FlyBase.
DR GO; GO:0031508; P:pericentric heterochromatin assembly; IMP:FlyBase.
DR GO; GO:0046328; P:regulation of JNK cascade; IGI:FlyBase.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR044574; ARIP4-like.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45797; PTHR45797; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chromosome; DNA damage; DNA repair; DNA-binding; Helicase;
KW Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..1311
FT /note="Transcriptional regulator ATRX homolog"
FT /id="PRO_0000074309"
FT DOMAIN 476..664
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 905..1085
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1285..1311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 615..618
FT /note="DEGH box"
FT COMPBIAS 11..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..311
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 489..496
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 857
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 859
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 785
FT /note="N -> T (in Ref. 1; AAG40586)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1311 AA; 148220 MW; 71B78942468D4A6B CRC64;
MGKKNPNARH TDAATPLTTD DSNSSSVSRR ESATESKSAS ESESSPPRSN TKQSRTHKNV
KASGKATVSS SSDSDQAVAN SSANDEEKEP VCKIRIVPLE KLLASPKTKE RPSRGSQQKN
VTINDSSDEE PLKGSKLVLP ARKSRNKNAS IIELSDSEEV DEEEESLLVA IPLPKEAQQT
KPEKNSSKAS KESIEKRQKA QKEATTSSAR AIRSVNGTRR GSLSSERSSR ASSSRAESPP
RPKRCVVRLK RVSLPKTKPA QKPKKMSSDS EEAATTSKKS RQRRSKSESE ADSDYEAPAA
EEEEEEERKS SGDEEEAANS SDSEVMPQRK RRRKKSESDK GSSDFEPEEK QKKKGRKRIK
KTSSGESDGD GDDDKQKNKR KHIRKIIKTK DLDLTTKEAA KEEDDRRKRI EDRQKLYNRI
FVKSESVEIN ELVLDFDEES KKALLQVDKG LLKKLKPHQV AGVKFMWDAC FETLKESQEK
PGSGCILAHC MGLGKTLQVV TLSHTLLVNT RRTGVDRVLI ISPLSTVNNW AREFTSWMKF
ANRNDIEVYD ISRYKDKPTR IFKLNEWFNE GGVCILGYDM YRILANEKAK GLRKKQREQL
MQALVDPGPD LVVCDEGHLL KNEKTSISKA VTRMRTKRRI VLTGTPLQNN LREYYCMIQF
VKPNLLGTYK EYMNRFVNPI TNGQYTDSTE RDLRLMKHRS HILHKLLEGC IQRRDYSVLA
PYLPPKHEYV VYTTLSELQQ KLYGYYMTTH REQSGGDVVG KGARLFQDFQ DLRRIWTHPM
NLRVNSDNVI AKRLLSNDDS DMEGFICDET DEDEAASNSS DSCETFKSDA SMSGLAASSG
KVKKRKTRNG NAGGGDSDSD LEMLGGLGGG SSVQKDDPSE WWKPFVEERE LNNVHHSPKL
LILLRLLQQC EAIGDKLLVF SQSLQSLDVI EHFLSLVDSN TKNYEFEGDV GDFKGCWTSG
KDYFRLDGSC SVEQREAMCK QFNNITNLRA RLFLISTRAG GLGINLVAAN RVVIFDVSWN
PSHDTQSIFR VYRFGQIKPC YIYRLIAMGT MEQKVYERQV AKQATAKRVI DEQQISRHYN
QTDLMELYSY ELKPSTEREM PILPKDRLFA EILTEHEKLI FKYHEHDSLL EQEEHENLTE
EERKSAWAEY EAEKTRTVQA SQYMSYDRNA FGNQVMGQFG NASGSVTSNK IFGFRSDILL
QLLNMKISKD HQELNQNQVI QLVPTYLQQL YNEMNNGDPT MYKDLLNLHS NIVHPSGMYM
NPLLYANQNP NAAGYNQGTG GVPPMAGGSV AHGPPAAPAP GFEPDKVYEI D
