RPB3_MOUSE
ID RPB3_MOUSE Reviewed; 275 AA.
AC P97760; Q99M46;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2016, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=DNA-directed RNA polymerase II subunit RPB3 {ECO:0000305};
DE Short=RNA polymerase II subunit 3;
DE Short=RNA polymerase II subunit B3;
DE AltName: Full=DNA-directed RNA polymerase II 33 kDa polypeptide;
DE Short=RPB33;
DE AltName: Full=DNA-directed RNA polymerase II subunit C;
DE AltName: Full=RPB31 {ECO:0000303|PubMed:9034305};
GN Name=Polr2c {ECO:0000312|MGI:MGI:109299}; Synonyms=Rpo2-3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9034305; DOI=10.1016/s0378-1119(96)00626-9;
RA Korobko I.V., Yamamoto K., Nogi Y., Muramatsu M.;
RT "Protein interaction cloning in yeast of the mouse third largest RNA
RT polymerase II subunit, mRPB31.";
RL Gene 185:1-4(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Component of RNA polymerase II which synthesizes mRNA precursors and
CC many functional non-coding RNAs. Pol II is the central component of the
CC basal RNA polymerase II transcription machinery. It is composed of
CC mobile elements that move relative to each other. RPB3 is part of the
CC core element with the central large cleft and the clamp element that
CC moves to open and close the cleft (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the RNA polymerase II (Pol II) complex consisting
CC of 12 subunits. RPB11/POLR2J and RPB3/POLR2C subunits interact with
CC each other.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the archaeal Rpo3/eukaryotic RPB3 RNA polymerase
CC subunit family. {ECO:0000305}.
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DR EMBL; D83999; BAA12205.1; -; mRNA.
DR EMBL; AK146763; BAE27415.1; -; mRNA.
DR EMBL; AK151270; BAE30257.1; -; mRNA.
DR EMBL; AK160053; BAE35592.1; -; mRNA.
DR EMBL; AC129606; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002023; AAH02023.1; -; mRNA.
DR EMBL; BC099548; AAH99548.1; -; mRNA.
DR CCDS; CCDS40442.1; -.
DR PIR; JC6181; JC6181.
DR RefSeq; NP_033116.2; NM_009090.5.
DR AlphaFoldDB; P97760; -.
DR SMR; P97760; -.
DR IntAct; P97760; 5.
DR MINT; P97760; -.
DR STRING; 10090.ENSMUSP00000105147; -.
DR iPTMnet; P97760; -.
DR PhosphoSitePlus; P97760; -.
DR EPD; P97760; -.
DR PaxDb; P97760; -.
DR PeptideAtlas; P97760; -.
DR PRIDE; P97760; -.
DR ProteomicsDB; 260836; -.
DR TopDownProteomics; P97760; -.
DR Antibodypedia; 28873; 181 antibodies from 27 providers.
DR DNASU; 20021; -.
DR Ensembl; ENSMUST00000109521; ENSMUSP00000105147; ENSMUSG00000031783.
DR GeneID; 20021; -.
DR KEGG; mmu:20021; -.
DR UCSC; uc009mxe.2; mouse.
DR CTD; 5432; -.
DR MGI; MGI:109299; Polr2c.
DR VEuPathDB; HostDB:ENSMUSG00000031783; -.
DR eggNOG; KOG1522; Eukaryota.
DR GeneTree; ENSGT00950000183100; -.
DR InParanoid; P97760; -.
DR OMA; PENIVMM; -.
DR OrthoDB; 834009at2759; -.
DR PhylomeDB; P97760; -.
DR TreeFam; TF103038; -.
DR Reactome; R-MMU-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-MMU-113418; Formation of the Early Elongation Complex.
DR Reactome; R-MMU-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-MMU-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-MMU-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-MMU-6782135; Dual incision in TC-NER.
DR Reactome; R-MMU-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-MMU-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-MMU-6803529; FGFR2 alternative splicing.
DR Reactome; R-MMU-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-MMU-72086; mRNA Capping.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-MMU-72165; mRNA Splicing - Minor Pathway.
DR Reactome; R-MMU-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR Reactome; R-MMU-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-MMU-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-MMU-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-MMU-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-MMU-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR Reactome; R-MMU-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR Reactome; R-MMU-9018519; Estrogen-dependent gene expression.
DR BioGRID-ORCS; 20021; 26 hits in 71 CRISPR screens.
DR ChiTaRS; Polr2c; mouse.
DR PRO; PR:P97760; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P97760; protein.
DR Bgee; ENSMUSG00000031783; Expressed in epithelium of small intestine and 104 other tissues.
DR ExpressionAtlas; P97760; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005665; C:RNA polymerase II, core complex; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0006366; P:transcription by RNA polymerase II; ISS:UniProtKB.
DR Gene3D; 2.170.120.12; -; 1.
DR Gene3D; 3.30.1360.10; -; 1.
DR HAMAP; MF_00320; RNApol_arch_Rpo3; 1.
DR InterPro; IPR001514; DNA-dir_RNA_pol_30-40kDasu_CS.
DR InterPro; IPR011262; DNA-dir_RNA_pol_insert.
DR InterPro; IPR011263; DNA-dir_RNA_pol_RpoA/D/Rpb3.
DR InterPro; IPR036603; RBP11-like.
DR InterPro; IPR022842; RNAP_Rpo3/Rpb3/RPAC1.
DR InterPro; IPR036643; RNApol_insert_sf.
DR Pfam; PF01000; RNA_pol_A_bac; 1.
DR Pfam; PF01193; RNA_pol_L; 1.
DR SMART; SM00662; RPOLD; 1.
DR SUPFAM; SSF55257; SSF55257; 1.
DR SUPFAM; SSF56553; SSF56553; 1.
DR PROSITE; PS00446; RNA_POL_D_30KD; 1.
PE 1: Evidence at protein level;
KW DNA-directed RNA polymerase; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription.
FT CHAIN 1..275
FT /note="DNA-directed RNA polymerase II subunit RPB3"
FT /id="PRO_0000132744"
FT REGION 203..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19387"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19387"
FT CONFLICT 54
FT /note="A -> G (in Ref. 1; BAA12205)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="A -> V (in Ref. 1; BAA12205)"
FT /evidence="ECO:0000305"
FT CONFLICT 168..169
FT /note="GF -> RS (in Ref. 1; BAA12205)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="A -> G (in Ref. 1; BAA12205)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="W -> G (in Ref. 1; BAA12205)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="V -> G (in Ref. 1; BAA12205)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 275 AA; 31443 MW; 64C3E2F61B91B352 CRC64;
MPYANQPTVR ITELTEENVK FIIENTDLAV ANSIRRVFIA EVPIIAIDWV QIDANSSVLH
DEFIAHRLGL IPLTSDDIVD KLQYSRDCTC EEFCPECSVE FTLDVRCNED QTRHVTSRDL
ISNSPRVIPV TSRNRDNDPN DYVEQDDILI VKLRKGQELR LRAYAKKGFG KEHAKWNPTA
GVAFEYDPDN ALRHTVYPKP EEWPKSEYSE LDEDESQAPY DPNGKPERFY YNVESCGSLR
PETIVLSALS GLKKKLSDLQ TQLSHEIQSD VLTIN
