GLYR1_DROME
ID GLYR1_DROME Reviewed; 602 AA.
AC Q8T079; Q9VL51;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Cytokine-like nuclear factor N-PAC;
DE Short=NPAC;
DE AltName: Full=Glyoxylate reductase 1 homolog;
DE AltName: Full=Nuclear protein NP60 homolog;
DE AltName: Full=Nucleosome-destabilizing factor {ECO:0000312|FlyBase:FBgn0043456};
DE AltName: Full=Putative oxidoreductase GLYR1 homolog;
GN Name=Ndf {ECO:0000312|FlyBase:FBgn0043456};
GN ORFNames=CG4747 {ECO:0000312|FlyBase:FBgn0043456};
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 [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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-10; SER-224; SER-228
RP AND SER-243, 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 [5]
RP FUNCTION, INTERACTION WITH MSL COMPLEX, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=23295261; DOI=10.1038/nsmb.2477;
RA Wang C.I., Alekseyenko A.A., LeRoy G., Elia A.E., Gorchakov A.A.,
RA Britton L.M., Elledge S.J., Kharchenko P.V., Garcia B.A., Kuroda M.I.;
RT "Chromatin proteins captured by ChIP-mass spectrometry are linked to dosage
RT compensation in Drosophila.";
RL Nat. Struct. Mol. Biol. 20:202-209(2013).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH
RP NUCLEOSOMES, AND SUBCELLULAR LOCATION.
RX PubMed=29759984; DOI=10.1101/gad.313973.118;
RA Fei J., Ishii H., Hoeksema M.A., Meitinger F., Kassavetis G.A., Glass C.K.,
RA Ren B., Kadonaga J.T.;
RT "NDF, a nucleosome-destabilizing factor that facilitates transcription
RT through nucleosomes.";
RL Genes Dev. 32:682-694(2018).
CC -!- FUNCTION: Nucleosome-destabilizing factor that is recruited to genes
CC during transcriptional activation and colocalizes with a subset of
CC trimethylated 'Lys-36' histone H3 (H3K36me3)-enriched regions
CC (PubMed:23295261, PubMed:29759984). Binds DNA (in vitro)
CC (PubMed:29759984). Facilitates Pol II transcription through nucleosomes
CC (PubMed:29759984). Facilitates male-specific lethal (MSL) histone
CC acetyltransferase complex targeting to active genes on the X chromosome
CC (PubMed:23295261). Stimulates the acetylation of 'Lys-56' of
CC nucleosomal histone H3 (H3K56ac) by nej (PubMed:29759984). May have
CC oxidoreductase activity (By similarity). {ECO:0000250|UniProtKB:Q49A26,
CC ECO:0000269|PubMed:23295261, ECO:0000269|PubMed:29759984}.
CC -!- SUBUNIT: Binds to mononucleosomes (PubMed:29759984). Interacts with
CC male-specific lethal (MSL) histone acetyltransferase complex at least
CC composed of mof, msl-1, msl-2 and msl-3 (PubMed:23295261).
CC {ECO:0000269|PubMed:23295261, ECO:0000269|PubMed:29759984}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:23295261,
CC ECO:0000269|PubMed:29759984}. Note=Localization to open chromatin
CC depends on H3K36 trimethylation by Set2. {ECO:0000269|PubMed:23295261}.
CC -!- DOMAIN: The PWWP domain is a H3 reader and strongly binds DNA.
CC {ECO:0000250|UniProtKB:Q49A26}.
CC -!- DOMAIN: In the dehydrogenase domain, the conserved NAD(P)H-binding
CC sites and sequence similarity to plant dehydrogenases suggest that this
CC protein may have oxidoreductase activity. However, since the active
CC site is not conserved, the dehydrogenase domain seems to serve as a
CC catalytically inert oligomerization module.
CC {ECO:0000250|UniProtKB:Q49A26}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in ectopic MSL-
CC binding sites on autosomes of male larvae.
CC {ECO:0000269|PubMed:23295261}.
CC -!- SIMILARITY: Belongs to the HIBADH-related family. NP60 subfamily.
CC {ECO:0000305}.
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DR EMBL; AE014134; AAF52846.3; -; Genomic_DNA.
DR EMBL; AY069497; AAL39642.1; -; mRNA.
DR RefSeq; NP_001285791.1; NM_001298862.1.
DR RefSeq; NP_609336.3; NM_135492.5.
DR AlphaFoldDB; Q8T079; -.
DR SMR; Q8T079; -.
DR BioGRID; 72969; 7.
DR IntAct; Q8T079; 10.
DR STRING; 7227.FBpp0292905; -.
DR iPTMnet; Q8T079; -.
DR PaxDb; Q8T079; -.
DR DNASU; 192507; -.
DR EnsemblMetazoa; FBtr0079930; FBpp0079520; FBgn0043456.
DR EnsemblMetazoa; FBtr0343740; FBpp0310306; FBgn0043456.
DR GeneID; 192507; -.
DR KEGG; dme:Dmel_CG4747; -.
DR UCSC; CG4747-RA; d. melanogaster.
DR CTD; 192507; -.
DR FlyBase; FBgn0043456; Ndf.
DR VEuPathDB; VectorBase:FBgn0043456; -.
DR eggNOG; KOG0409; Eukaryota.
DR HOGENOM; CLU_018075_0_0_1; -.
DR InParanoid; Q8T079; -.
DR OMA; DNIMSKN; -.
DR PhylomeDB; Q8T079; -.
DR SignaLink; Q8T079; -.
DR BioGRID-ORCS; 192507; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 192507; -.
DR PRO; PR:Q8T079; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0043456; Expressed in egg cell and 27 other tissues.
DR ExpressionAtlas; Q8T079; baseline and differential.
DR Genevisible; Q8T079; DM.
DR GO; GO:0005705; C:polytene chromosome interband; IDA:FlyBase.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0031491; F:nucleosome binding; IDA:UniProtKB.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR GO; GO:0007549; P:dosage compensation; IMP:UniProtKB.
DR GO; GO:0035066; P:positive regulation of histone acetylation; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR CDD; cd05836; N_Pac_NP60; 1.
DR Gene3D; 1.10.1040.10; -; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR006115; 6PGDH_NADP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR029154; NADP-bd.
DR InterPro; IPR035501; NP60_PWWP.
DR InterPro; IPR000313; PWWP_dom.
DR Pfam; PF14833; NAD_binding_11; 1.
DR Pfam; PF03446; NAD_binding_2; 1.
DR Pfam; PF00855; PWWP; 1.
DR SMART; SM00293; PWWP; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS50812; PWWP; 1.
PE 1: Evidence at protein level;
KW Chromosome; Phosphoprotein; Reference proteome.
FT CHAIN 1..602
FT /note="Cytokine-like nuclear factor N-PAC"
FT /id="PRO_0000312130"
FT DOMAIN 22..81
FT /note="PWWP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT REGION 162..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..602
FT /note="Dehydrogenase domain"
FT /evidence="ECO:0000250|UniProtKB:Q49A26"
FT COMPBIAS 177..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 319..333
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q49A26"
FT BINDING 411
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q49A26"
FT BINDING 554
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q49A26"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
SQ SEQUENCE 602 AA; 65252 MW; E004EEC610C23625 CRC64;
MSKNKKLSLS GGDTTEKFIY KPKDLIWAKM KGFTPWPGMI VDPPLDLLSQ QRRANTKCVF
FFGSRNFAWI EENNIKPFEG PWKEELAKVS KPAAFRHAMT DIEKYIDDPA EVDEQVNKSC
GAPNHATEAD FDKIRDGLDS EEIVGEEATA DGNNGVVAHV VGSPDEGDGL DVEINADSSA
SPVTSPAVTT KAAGKRTPKA KSVAATSVKS TKGSAKSAQK RRTSAQQSPS GPSNAKRGKR
DVSGEALQDA DEASSTPTGR RRVETDALLA SIAAKRAPNA IALLDRPVVT RPEAQVIDMS
SRSNTLADRD IVPSEQTFGF LGLGMMGSTI VKDLIYTGHK VVVWNRTIDK CQPFAEAGAE
VKDTPMDVVE AADVIFCCVS DPKGAKDLVF GNCGVLQLKD LNNKAYVEMS TIDPDTSLDI
GEGIKQCNGR YLEAQIHGSR QEAAEGMLII LAGGDRSVFE ECHSCFKTIA KNTFFLGNIG
NACKVNLILQ TILGVSLVGL AEALALADRF SISLNDIIDI FDLTSMKSPM LLAKGKEMAK
GDFNPQQPLS HMQRDLRLVL NMAENLDQSM PVTSITNEVF KHTKRLGYSE HDSSAVFVRS
RF
