RPC4_MOUSE
ID RPC4_MOUSE Reviewed; 398 AA.
AC Q91WD1; Q3U0T3; Q9CZ02;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=DNA-directed RNA polymerase III subunit RPC4;
DE Short=RNA polymerase III subunit C4;
DE AltName: Full=DNA-directed RNA polymerase III subunit D;
GN Name=Polr3d; Synonyms=Bn51t;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, and Spleen;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Salivary gland;
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).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Specific component of RNA polymerase III which synthesizes small RNAs,
CC such as 5S rRNA and tRNAs. Plays a key role in sensing and limiting
CC infection by intracellular bacteria and DNA viruses. Acts as nuclear
CC and cytosolic DNA sensor involved in innate immune response. Can sense
CC non-self dsDNA that serves as template for transcription into dsRNA.
CC The non-self RNA polymerase III transcripts induce type I interferon
CC and NF- Kappa-B through the RIG-I pathway (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Component of the RNA polymerase III (Pol III) complex
CC consisting of 17 subunits. Interacts with POLR3E/RPC5 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the eukaryotic RPC4/POLR3D RNA polymerase
CC subunit family. {ECO:0000305}.
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DR EMBL; AK013165; BAB28687.1; -; mRNA.
DR EMBL; AK156587; BAE33768.1; -; mRNA.
DR EMBL; CH466535; EDL35903.1; -; Genomic_DNA.
DR EMBL; BC016102; AAH16102.1; -; mRNA.
DR CCDS; CCDS27253.1; -.
DR RefSeq; NP_001157554.1; NM_001164082.1.
DR RefSeq; NP_080221.3; NM_025945.3.
DR AlphaFoldDB; Q91WD1; -.
DR BioGRID; 211914; 1.
DR STRING; 10090.ENSMUSP00000000793; -.
DR iPTMnet; Q91WD1; -.
DR PhosphoSitePlus; Q91WD1; -.
DR EPD; Q91WD1; -.
DR MaxQB; Q91WD1; -.
DR PaxDb; Q91WD1; -.
DR PeptideAtlas; Q91WD1; -.
DR PRIDE; Q91WD1; -.
DR ProteomicsDB; 299942; -.
DR Antibodypedia; 22571; 187 antibodies from 28 providers.
DR DNASU; 67065; -.
DR Ensembl; ENSMUST00000000793; ENSMUSP00000000793; ENSMUSG00000000776.
DR Ensembl; ENSMUST00000180358; ENSMUSP00000137614; ENSMUSG00000000776.
DR GeneID; 67065; -.
DR KEGG; mmu:67065; -.
DR UCSC; uc007uny.2; mouse.
DR CTD; 661; -.
DR MGI; MGI:1914315; Polr3d.
DR VEuPathDB; HostDB:ENSMUSG00000000776; -.
DR eggNOG; KOG3122; Eukaryota.
DR GeneTree; ENSGT00390000013948; -.
DR HOGENOM; CLU_042288_0_0_1; -.
DR InParanoid; Q91WD1; -.
DR OMA; QAENTCT; -.
DR OrthoDB; 1381418at2759; -.
DR PhylomeDB; Q91WD1; -.
DR Reactome; R-MMU-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter.
DR Reactome; R-MMU-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter.
DR Reactome; R-MMU-76071; RNA Polymerase III Transcription Initiation From Type 3 Promoter.
DR BioGRID-ORCS; 67065; 24 hits in 75 CRISPR screens.
DR ChiTaRS; Polr3d; mouse.
DR PRO; PR:Q91WD1; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q91WD1; protein.
DR Bgee; ENSMUSG00000000776; Expressed in otic placode and 219 other tissues.
DR Genevisible; Q91WD1; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IC:MGI.
DR GO; GO:0005666; C:RNA polymerase III complex; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0045089; P:positive regulation of innate immune response; ISS:UniProtKB.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; ISS:UniProtKB.
DR GO; GO:0006383; P:transcription by RNA polymerase III; IEA:InterPro.
DR InterPro; IPR007811; RPC4.
DR PANTHER; PTHR13408; PTHR13408; 1.
DR Pfam; PF05132; RNA_pol_Rpc4; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Antiviral defense; DNA-directed RNA polymerase; Immunity;
KW Innate immunity; Isopeptide bond; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P05423"
FT CHAIN 2..398
FT /note="DNA-directed RNA polymerase III subunit RPC4"
FT /id="PRO_0000073968"
FT REGION 1..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P05423"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05423"
FT MOD_RES 95
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P05423"
FT MOD_RES 97
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P05423"
FT MOD_RES 99
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P05423"
FT CROSSLNK 68
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05423"
FT CROSSLNK 78
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05423"
FT CROSSLNK 141
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05423"
FT CROSSLNK 152
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05423"
FT CROSSLNK 160
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05423"
FT CROSSLNK 190
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05423"
FT CROSSLNK 199
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05423"
FT CROSSLNK 206
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05423"
FT CROSSLNK 220
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05423"
FT CROSSLNK 285
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05423"
FT CROSSLNK 302
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05423"
FT CROSSLNK 396
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05423"
FT CONFLICT 201
FT /note="F -> L (in Ref. 3; AAH16102)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 398 AA; 44357 MW; B70179A124C1231B CRC64;
MSEGNAAGEP SNPGGPRPLL SGGRGLIGRR PAPPLTPGRL PSIRSRDLTL GGVKKKTFTP
NIISRKIKEE PKEEVTMKKE KRERDRDRQR EGHGRGRGRP EVIQSHSIFE QGPAEMMKKK
GNWDKTVDMS DMGPSHIINI KKEKRETDEE TKQILRMLEK DDFIDDPGLK NDTRNMPVQL
PLAHSGWLFK EESEEPEAKP FSAGPKEEDM EVDVPAVKVK EEPRDEEEEA KVKAPPRAAR
KTPGLPKDVS VAELLRELSL MKDEELLFLQ LPDTLPGQPP TQDIKPVKTE VQGEDGQMVV
IKQEKDREAR LAENACTLAD LTEGQVGKLL IRKSGKVQLL LGKVTLDVTM GTTCSFLQEL
VSVGLGDSRT GEMTVLGHVK HKLVCSPDFE SLLDHKHR
