ID RPB4_DROME Reviewed; 139 AA. AC Q9VEA5; Q4V3P8; Q8I0A4; DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot. DT 03-APR-2007, sequence version 5. DT 28-JUN-2023, entry version 158. DE RecName: Full=DNA-directed RNA polymerase II subunit Rpb4 {ECO:0000303|PubMed:19921261}; GN Name=Rpb4 {ECO:0000303|PubMed:19921261, ECO:0000312|FlyBase:FBgn0263757}; GN ORFNames=CG43662 {ECO:0000312|FlyBase:FBgn0263757}; 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] {ECO:0000305, ECO:0000312|EMBL:AAN88031.1} RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION. RX PubMed=12482983; DOI=10.1128/mcb.23.1.306-321.2003; RA Muratoglu S., Georgieva S., Papai G., Scheer E., Enunlu I., Komonyi O., RA Cserpan I., Lebedeva L., Nabirochkina E., Udvardy A., Tora L., Boros I.; RT "Two different Drosophila ADA2 homologues are present in distinct GCN5 RT histone acetyltransferase-containing complexes."; RL Mol. Cell. Biol. 23:306-321(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132}; 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] {ECO:0000305} RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING. 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] {ECO:0000312|EMBL:AAY51562.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Berkeley; RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., RA Park S., Wan K.H., Yu C., Celniker S.E.; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP FUNCTION. RX PubMed=12697829; DOI=10.1128/mcb.23.9.3305-3319.2003; RA Kusch T., Guelman S., Abmayr S.M., Workman J.L.; RT "Two Drosophila Ada2 homologues function in different multiprotein RT complexes."; RL Mol. Cell. Biol. 23:3305-3319(2003). RN [6] RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND INDUCTION BY HEAT SHOCK. RX PubMed=19921261; DOI=10.1007/s00438-009-0499-6; RA Pankotai T., Ujfaludi Z., Vamos E., Suri K., Boros I.M.; RT "The dissociable RPB4 subunit of RNA Pol II has vital functions in RT Drosophila."; RL Mol. Genet. Genomics 283:89-97(2010). CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of CC DNA into RNA using the four ribonucleoside triphosphates as substrates. CC Associates with POLR2G. {ECO:0000269|PubMed:12482983, CC ECO:0000269|PubMed:12697829}. CC -!- SUBUNIT: RNA polymerase II consists of 12 different subunits. CC {ECO:0000250|UniProtKB:O15514}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12482983}. Chromosome CC {ECO:0000269|PubMed:19921261}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=D {ECO:0000269|PubMed:10731132}; CC IsoId=Q9VEA5-1; Sequence=Displayed; CC Name=B; CC IsoId=Q7KSD8-1; Sequence=External; CC Name=A; CC IsoId=Q7KSD8-2; Sequence=External; CC Name=C {ECO:0000269|PubMed:12482983}; Synonyms=ADA2A-SV2 CC {ECO:0000269|PubMed:12482983}; CC IsoId=Q7KSD8-3; Sequence=External; CC Name=E {ECO:0000269|PubMed:12482983}; Synonyms=ADA2A-SV1 CC {ECO:0000269|PubMed:12482983}; CC IsoId=Q7KSD8-4; Sequence=External; CC -!- DEVELOPMENTAL STAGE: During development expression peaks in embryos, CC decreases sharply in L1 larvae and then remains low throughout larval CC development. {ECO:0000269|PubMed:19921261}. CC -!- INDUCTION: Under heat shock conditions, up-regulated in early larvae CC and then expression levels appear to return to normal during the L2/L3 CC and pupal stages. In second instar larvae, down-regulated 1 hr after CC starvation and then remains low until at least 4 hr after nutritional CC starvation. {ECO:0000269|PubMed:19921261}. CC -!- MISCELLANEOUS: This protein is produced by a bicistronic gene which CC also produces the Ada2a protein by alternative splicing CC (PubMed:19921261). Three distinct zinc-containing RNA polymerases are CC found in eukaryotic nuclei: polymerase I for the ribosomal RNA CC precursor, polymerase II for the mRNA precursor, and polymerase III for CC 5S and tRNA genes (Probable). {ECO:0000269|PubMed:19921261, CC ECO:0000305}. CC -!- SIMILARITY: Belongs to the eukaryotic RPB4 RNA polymerase subunit CC family. {ECO:0000255}. 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; AF544019; AAN88031.1; -; mRNA. DR EMBL; AF544020; AAN88032.1; -; mRNA. DR EMBL; AE014297; AAF55522.5; -; Genomic_DNA. DR EMBL; BT022168; AAY51562.1; -; mRNA. DR EMBL; BT023308; AAY55724.1; -; mRNA. DR EMBL; BT023309; AAY55725.1; -; mRNA. DR RefSeq; NP_001014633.2; NM_001014633.3. [Q9VEA5-1] DR AlphaFoldDB; Q9VEA5; -. DR SMR; Q9VEA5; -. DR BioGRID; 2593107; 2. DR IntAct; Q9VEA5; 4. DR STRING; 7227.FBpp0302530; -. DR PaxDb; Q9VEA5; -. DR DNASU; 14462484; -. DR EnsemblMetazoa; FBtr0310379; FBpp0302530; FBgn0263757. [Q9VEA5-1] DR GeneID; 14462484; -. DR KEGG; dme:Dmel_CG43662; -. DR UCSC; CG33520-RA; d. melanogaster. [Q9VEA5-1] DR AGR; FB:FBgn0263757; -. DR CTD; 5433; -. DR FlyBase; FBgn0263757; Rpb4. DR VEuPathDB; VectorBase:FBgn0263757; -. DR eggNOG; KOG2351; Eukaryota. DR GeneTree; ENSGT00390000004912; -. DR HOGENOM; CLU_110332_2_1_1; -. DR InParanoid; Q9VEA5; -. DR OMA; TMRKFQS; -. DR OrthoDB; 5491678at2759; -. DR PhylomeDB; Q9VEA5; -. DR Reactome; R-DME-112382; Formation of RNA Pol II elongation complex. DR Reactome; R-DME-113418; Formation of the Early Elongation Complex. DR Reactome; R-DME-674695; RNA Polymerase II Pre-transcription Events. DR Reactome; R-DME-6781823; Formation of TC-NER Pre-Incision Complex. DR Reactome; R-DME-6782135; Dual incision in TC-NER. DR Reactome; R-DME-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER. DR Reactome; R-DME-6796648; TP53 Regulates Transcription of DNA Repair Genes. DR Reactome; R-DME-6807505; RNA polymerase II transcribes snRNA genes. DR Reactome; R-DME-72086; mRNA Capping. DR Reactome; R-DME-72163; mRNA Splicing - Major Pathway. DR Reactome; R-DME-72165; mRNA Splicing - Minor Pathway. DR Reactome; R-DME-72203; Processing of Capped Intron-Containing Pre-mRNA. DR Reactome; R-DME-73776; RNA Polymerase II Promoter Escape. DR Reactome; R-DME-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening. DR Reactome; R-DME-75953; RNA Polymerase II Transcription Initiation. DR Reactome; R-DME-75955; RNA Polymerase II Transcription Elongation. DR Reactome; R-DME-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance. DR Reactome; R-DME-77075; RNA Pol II CTD phosphorylation and interaction with CE. DR Reactome; R-DME-9018519; Estrogen-dependent gene expression. DR BioGRID-ORCS; 14462484; 1 hit in 1 CRISPR screen. DR GenomeRNAi; 14462484; -. DR Proteomes; UP000000803; Chromosome 3R. DR Bgee; FBgn0263757; Expressed in Malpighian tubule and 15 other tissues. DR Genevisible; Q9VEA5; DM. DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase. DR GO; GO:0005705; C:polytene chromosome interband; IDA:FlyBase. DR GO; GO:0005703; C:polytene chromosome puff; IDA:UniProtKB. DR GO; GO:0005665; C:RNA polymerase II, core complex; IDA:UniProtKB. DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro. DR GO; GO:0031369; F:translation initiation factor binding; IBA:GO_Central. DR GO; GO:0034402; P:recruitment of 3'-end processing factors to RNA polymerase II holoenzyme complex; IBA:GO_Central. DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IBA:GO_Central. DR Gene3D; 1.20.1250.40; -; 1. DR InterPro; IPR010997; HRDC-like_sf. DR InterPro; IPR006590; RNA_pol_Rpb4/RPC9_core. DR InterPro; IPR045222; Rpb4-like. DR InterPro; IPR005574; Rpb4/RPC9. DR InterPro; IPR038324; Rpb4/RPC9_sf. DR PANTHER; PTHR21297; DNA-DIRECTED RNA POLYMERASE II; 1. DR PANTHER; PTHR21297:SF0; DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB4; 1. DR Pfam; PF03874; RNA_pol_Rpb4; 1. DR SMART; SM00657; RPOL4c; 1. DR SUPFAM; SSF47819; HRDC-like; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Chromosome; DNA-directed RNA polymerase; Nucleus; KW Reference proteome; Transcription. FT CHAIN 1..139 FT /note="DNA-directed RNA polymerase II subunit Rpb4" FT /id="PRO_0000283732" FT CONFLICT 124..126 FT /note="LRQ -> ARE (in Ref. 1; AAN88031/AAN88032)" FT /evidence="ECO:0000305" SQ SEQUENCE 139 AA; 16212 MW; F7541C9A08C23CB1 CRC64; MSFMNPVDMV DEDAADLQFP KEFENAETLL ISEVHMLLDH RKRQNESADE EQEFSEVFMK TYAYTDSFRK FKNKETIMSA RSLLMQKKLH KFELAALGNL CPEAPEEAKA LIPSLEGRFE DEELRQILDD IGTKRSLQY //