RTF1_DROME
ID RTF1_DROME Reviewed; 775 AA.
AC Q9W261;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=RNA polymerase-associated protein Rtf1;
DE Short=dRtf1;
GN Name=Rtf1; ORFNames=CG10955;
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 FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=16882721; DOI=10.1073/pnas.0603620103;
RA Tenney K., Gerber M., Ilvarsonn A., Schneider J., Gause M., Dorsett D.,
RA Eissenberg J.C., Shilatifard A.;
RT "Drosophila Rtf1 functions in histone methylation, gene expression, and
RT Notch signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11970-11974(2006).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=16354696; DOI=10.1128/mcb.26.1.250-260.2006;
RA Adelman K., Wei W., Ardehali M.B., Werner J., Zhu B., Reinberg D.,
RA Lis J.T.;
RT "Drosophila Paf1 modulates chromatin structure at actively transcribed
RT genes.";
RL Mol. Cell. Biol. 26:250-260(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-51; SER-53; SER-269;
RP SER-271; TYR-384; SER-385; SER-388; SER-390; SER-391; SER-412; SER-413 AND
RP SER-415, 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).
CC -!- FUNCTION: Plays a role in transcription-coupled histone modification.
CC Required for methylation of 'Lys-4' of histone H3. Plays a role in
CC regulation of transcription. Required for maximal induction of heat-
CC shock genes. Plays a role in Notch signaling in the wing margins.
CC {ECO:0000269|PubMed:16354696, ECO:0000269|PubMed:16882721}.
CC -!- SUBUNIT: Interacts with the RNA polymerase II complex. May interact
CC with the PAF1 complex. {ECO:0000269|PubMed:16354696}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:16354696}. Chromosome
CC {ECO:0000269|PubMed:16354696}. Note=Co-localizes with Paf1 and RNA
CC polymerase II on transcriptionally active sites on chromosomes.
CC -!- DEVELOPMENTAL STAGE: Detected in embryo. Expression is very low in
CC larvae, pupae or adults. {ECO:0000269|PubMed:16882721}.
CC -!- DISRUPTION PHENOTYPE: Death at pupal stage. Weaker mutants that live to
CC adulthood exhibit reduced wing width. {ECO:0000269|PubMed:16882721}.
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DR EMBL; AE013599; AAF46837.1; -; Genomic_DNA.
DR RefSeq; NP_001286717.1; NM_001299788.1.
DR RefSeq; NP_611665.1; NM_137821.3.
DR AlphaFoldDB; Q9W261; -.
DR SMR; Q9W261; -.
DR BioGRID; 63170; 10.
DR IntAct; Q9W261; 4.
DR STRING; 7227.FBpp0071731; -.
DR iPTMnet; Q9W261; -.
DR PaxDb; Q9W261; -.
DR DNASU; 37554; -.
DR EnsemblMetazoa; FBtr0071820; FBpp0071731; FBgn0034722.
DR EnsemblMetazoa; FBtr0342988; FBpp0309752; FBgn0034722.
DR GeneID; 37554; -.
DR KEGG; dme:Dmel_CG10955; -.
DR UCSC; CG10955-RA; d. melanogaster.
DR CTD; 23168; -.
DR FlyBase; FBgn0034722; Rtf1.
DR VEuPathDB; VectorBase:FBgn0034722; -.
DR eggNOG; KOG2402; Eukaryota.
DR GeneTree; ENSGT00940000168478; -.
DR HOGENOM; CLU_018644_0_0_1; -.
DR InParanoid; Q9W261; -.
DR OMA; SGCKSAV; -.
DR OrthoDB; 523922at2759; -.
DR PhylomeDB; Q9W261; -.
DR Reactome; R-DME-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-DME-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-DME-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-DME-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR BioGRID-ORCS; 37554; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Rtf1; fly.
DR GenomeRNAi; 37554; -.
DR PRO; PR:Q9W261; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0034722; Expressed in egg cell and 27 other tissues.
DR ExpressionAtlas; Q9W261; baseline and differential.
DR Genevisible; Q9W261; DM.
DR GO; GO:0016593; C:Cdc73/Paf1 complex; IBA:GO_Central.
DR GO; GO:0000785; C:chromatin; IMP:UniProtKB.
DR GO; GO:0000791; C:euchromatin; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:1990269; F:RNA polymerase II C-terminal domain phosphoserine binding; IBA:GO_Central.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IMP:FlyBase.
DR GO; GO:1905437; P:positive regulation of histone H3-K4 trimethylation; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:FlyBase.
DR Gene3D; 3.90.70.200; -; 1.
DR InterPro; IPR004343; Plus-3_dom.
DR InterPro; IPR036128; Plus3-like_sf.
DR Pfam; PF03126; Plus-3; 1.
DR SMART; SM00719; Plus3; 1.
DR SUPFAM; SSF159042; SSF159042; 1.
DR PROSITE; PS51360; PLUS3; 1.
PE 1: Evidence at protein level;
KW Activator; Chromosome; Coiled coil; Notch signaling pathway; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..775
FT /note="RNA polymerase-associated protein Rtf1"
FT /id="PRO_0000255935"
FT DOMAIN 428..559
FT /note="Plus3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00693"
FT REGION 1..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 738..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 604..665
FT /evidence="ECO:0000255"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..426
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..775
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 384
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
SQ SEQUENCE 775 AA; 87552 MW; FF9EEC3F2AD8FC88 CRC64;
MGKRRTQSLI DSNSSDSDSE SETNLESDLM SLAKKRKKPQ TAAKSSSRSD SDSDWANNKA
GAPSSKKKKR QKPSRDSSSS ESNWDDDSQD ERQPARQSPA QTQQEHKPPE QASQPAQLSE
QEEGEVSDSD SDKSKSNSSS SGSDSSSSSS SSDSEFDDGF DDDLMGDDED RRRLNGLSEK
ERETEIYKRI EQREIMRTRW EIERKLKLAR RGEKNQEKSK NKGERAKKKK EKREKKARKA
REAQAPLPTQ ASTSTLLDVE PKPSNEVRSA SPLSTPALNR DAASTSAAVA SIMPDDAASS
AGVSDYFDHK ERSKERKKNV EANKTDDKRS NAMALLKAKR EGKAKREEEE AKRMAEKDRD
DDKEELDSVS GCKSAVKLKA SEIYSDDSGS SDWDEEEKPA GKRSRSNSSK ASSESEDEEK
APQRPVFITT REDLNKLRLS RYKMERFVNL PIFESTVLNC FVRISIGNNG QKPVYRVAEI
VGVVETGKIY SLGTTRTNRG LRLKHGTQER VFRLEFISNQ EFTENEFNKW NEVCQQSHVQ
MPTIDLIAIK QNDIKKALNY EFKDEDVDKI VEEKNRFRNR PTNYAMKKTC LMKERDAAML
RGDYDIAQDL GQQIDELENR ASELDKRRSH TLNLISYIND RNRKKNVEDA EKAILEEARA
NKGLKISDPF TRRITQPRMG FKGAKKDEDD MQLAPLPPPP PGKKRPNEAG TSSASVRSTD
SKDYSLYSLH DFDIDLDVPL PVNTNSVPKP ASKPAETVSK RSLNLEDYKK KRGLI
