RPB2_DROME
ID RPB2_DROME Reviewed; 1176 AA.
AC P08266; Q04155; Q95027; Q9VFM7;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=DNA-directed RNA polymerase II subunit RPB2;
DE Short=RNA polymerase II subunit 2;
DE Short=RNA polymerase II subunit B2;
DE EC=2.7.7.6;
DE AltName: Full=DNA-directed RNA polymerase II 140 kDa polypeptide;
GN Name=RpII140; ORFNames=CG3180;
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 [GENOMIC DNA].
RC TISSUE=Embryo;
RX PubMed=3116266; DOI=10.1016/0022-2836(87)90496-7;
RA Falkenburg D., Dworniczak B., Faust D.M., Bautz E.K.F.;
RT "RNA polymerase II of Drosophila. Relation of its 140,000 Mr subunit to the
RT beta subunit of Escherichia coli RNA polymerase.";
RL J. Mol. Biol. 195:929-937(1987).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-69.
RC TISSUE=Embryo;
RX PubMed=1905256; DOI=10.1016/0378-1119(91)90361-e;
RA Sitzler S., Oldenburg I., Petersen G., Bautz E.K.F.;
RT "Analysis of the promoter region of the housekeeping gene DmRP140 by
RT sequence comparison of Drosophila melanogaster and Drosophila virilis.";
RL Gene 100:155-162(1991).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Second largest component of RNA polymerase II which synthesizes mRNA
CC precursors and many functional non-coding RNAs. Proposed to contribute
CC to the polymerase catalytic activity and forms the polymerase active
CC center together with the largest subunit. Pol II is the central
CC component of the basal RNA polymerase II transcription machinery. It is
CC composed of mobile elements that move relative to each other. RPB2 is
CC part of the core element with the central large cleft, the clamp
CC element that moves to open and close the cleft and the jaws that are
CC thought to grab the incoming DNA template (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.6;
CC -!- SUBUNIT: Component of the RNA polymerase II (Pol II) complex consisting
CC of 12 subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- MISCELLANEOUS: The binding of ribonucleoside triphosphate to the RNA
CC polymerase II transcribing complex probably involves a two-step
CC mechanism. The initial binding seems to occur at the entry (E) site and
CC involves a magnesium ion coordinated by three conserved aspartate
CC residues of the two largest RNA Pol II subunits (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA29180.2; Type=Frameshift; Note=The frameshift leads to an erroneous gene model prediction.; Evidence={ECO:0000305};
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DR EMBL; X05709; CAA29180.2; ALT_FRAME; Genomic_DNA.
DR EMBL; AE014297; AAF55024.1; -; Genomic_DNA.
DR EMBL; BT003265; AAO25022.1; -; mRNA.
DR EMBL; M62972; AAA28476.1; -; Genomic_DNA.
DR PIR; A27826; A27826.
DR RefSeq; NP_001287323.1; NM_001300394.1.
DR RefSeq; NP_476706.1; NM_057358.4.
DR AlphaFoldDB; P08266; -.
DR SMR; P08266; -.
DR BioGRID; 66798; 8.
DR DIP; DIP-17498N; -.
DR IntAct; P08266; 4.
DR STRING; 7227.FBpp0082353; -.
DR PaxDb; P08266; -.
DR PRIDE; P08266; -.
DR DNASU; 41721; -.
DR EnsemblMetazoa; FBtr0082892; FBpp0082353; FBgn0262955.
DR EnsemblMetazoa; FBtr0344600; FBpp0310926; FBgn0262955.
DR GeneID; 41721; -.
DR KEGG; dme:Dmel_CG3180; -.
DR CTD; 41721; -.
DR FlyBase; FBgn0262955; RpII140.
DR VEuPathDB; VectorBase:FBgn0262955; -.
DR eggNOG; KOG0214; Eukaryota.
DR GeneTree; ENSGT00950000183132; -.
DR HOGENOM; CLU_000524_5_2_1; -.
DR InParanoid; P08266; -.
DR OMA; RDLHGTH; -.
DR OrthoDB; 42570at2759; -.
DR PhylomeDB; P08266; -.
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-5578749; Transcriptional regulation by small RNAs.
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-6803529; FGFR2 alternative splicing.
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; 41721; 0 hits in 1 CRISPR screen.
DR ChiTaRS; RpII140; fly.
DR GenomeRNAi; 41721; -.
DR PRO; PR:P08266; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0262955; Expressed in eye disc (Drosophila) and 29 other tissues.
DR ExpressionAtlas; P08266; baseline and differential.
DR Genevisible; P08266; DM.
DR GO; GO:0005665; C:RNA polymerase II, core complex; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; NAS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR GO; GO:0006366; P:transcription by RNA polymerase II; ISS:FlyBase.
DR CDD; cd00653; RNA_pol_B_RPB2; 1.
DR Gene3D; 2.40.270.10; -; 1.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 1.
DR InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
DR InterPro; IPR007121; RNA_pol_bsu_CS.
DR InterPro; IPR007644; RNA_pol_bsu_protrusion.
DR InterPro; IPR007642; RNA_pol_Rpb2_2.
DR InterPro; IPR037034; RNA_pol_Rpb2_2_sf.
DR InterPro; IPR007645; RNA_pol_Rpb2_3.
DR InterPro; IPR007646; RNA_pol_Rpb2_4.
DR InterPro; IPR007647; RNA_pol_Rpb2_5.
DR InterPro; IPR007641; RNA_pol_Rpb2_7.
DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR PANTHER; PTHR20856; PTHR20856; 1.
DR Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR Pfam; PF04561; RNA_pol_Rpb2_2; 1.
DR Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR Pfam; PF04566; RNA_pol_Rpb2_4; 1.
DR Pfam; PF04567; RNA_pol_Rpb2_5; 1.
DR Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR PROSITE; PS01166; RNA_POL_BETA; 1.
PE 2: Evidence at transcript level;
KW DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Transcription;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1176
FT /note="DNA-directed RNA polymerase II subunit RPB2"
FT /id="PRO_0000048084"
FT ZN_FING 1121..1142
FT /note="C4-type"
FT BINDING 794
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="ligand shared with RPB1"
FT /evidence="ECO:0000250"
FT BINDING 1121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT CONFLICT 72
FT /note="A -> R (in Ref. 1; CAA29180)"
FT /evidence="ECO:0000305"
FT CONFLICT 666..667
FT /note="ID -> MY (in Ref. 1; CAA29180)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1176 AA; 134043 MW; 224821B335BED7F0 CRC64;
MMYDNEEELY EEENAEEISH ELWQEACWIV INAYFDEKGL VRQQLDSFDE FIQMSVQRIV
EDSPAIELQA EAQHTSGEVE TPPRFSLKFE QIYLSKPTHW EKDGSPSPMM PNEARLRNLT
YSAPLYVDIT KTKNVEGLDP VETQHQKTFI GKIPIMLRST YCLLSQLTDR DLTELNECPL
DPGGYFIING SEKVLIAQEK MATNTVYVFS MKDGKYAFKT EIRSCLEHSS RPTSTLWVNM
MARGSQNIKK SAIGQRIIAI LPYIKQEIPI MIVFRALGFV ADRDILEHII YDFDDPEMME
MVKPSLDEAF VVQEQNVALN FIGARGARPG VTKDKRIKYA KEILQKEMLP HVGVSDFCET
KKAYFLGYMV HRLLLASLGR RELDDRDHYG NKRLDLAGPL LAFLFRGLFK NLMKEVRMYT
QKFIDRGKDF NLELAIKTNI ITDGLRYSLA TGNWGDQKKA HQARAGVSQV LNRLTFASTL
SHLRRVNSPI GRDGKLAKPR QLHNTLWGML CPAETPEGAA VGLVKNLALM AYISVGSQPS
PILEFLEEWS MENLEEIAPS AIADATKIFV NGCWVGIHRD PEQLMATLRK LRRQMDIIVS
EVSMIRDIRD REIRIYTDAG RICRPLLIVE NGSLLLKKTH VEMLKERDYN NYSWQVLVAS
GVVEYIDTLE EETVMIAMSP YDLKQDKDYA YCTTYTHCEI HPAMILGVCA SIIPFPDHNQ
SPRNTYQSAM GKQAMGVYIT NFHVRMDTLA HVLYYPMKPL VTTRSMEYLR FRELPAGINS
IVAILCYTGY NQEDSVILNA SAVERGFFRS VFYRSYKDSE NKRVGDQEEN FEKPHRGTCQ
GMRNAHYDKL DDDGIIAPGI RVSGDDVVIG KTITLPENDD ELDSNTKRFS KRDASTFLRN
SETGIVDQVM LTLNSEGYKF CKIRVRSVRI PQIGDKFASR HGQKGTCGIQ YRQEDMAFTC
EGLAPDIIIN PHAIPSRMTI GHLIECLQGK LGSNKGEIGD ATPFNDAVNV QKISTFLQEY
GYHLRGNEVM YNGHTGRKIN AQVFLGPTYY QRLKHMVDDK IHSRARGPVQ ILVRQPMEGR
ARDGGLRFGE MERDCQISHG AAQFLRERLF EVSDPYRVHI CNFCGLIAIA NLRNNTFECK
GCKNKTQISQ VRLPYAAKLL FQELMSMNIA PRLMVT
