RPA49_MOUSE
ID RPA49_MOUSE Reviewed; 482 AA.
AC Q8K202; B1AXQ6; B1AXQ7; Q62034; Q8BQG9;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=DNA-directed RNA polymerase I subunit RPA49;
DE Short=RNA polymerase I subunit A49;
DE AltName: Full=DNA-directed RNA polymerase I subunit E;
DE AltName: Full=RNA polymerase I-associated factor 1;
DE AltName: Full=RNA polymerase I-associated factor 53;
GN Name=Polr1e; Synonyms=Paf53, Praf1;
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] (ISOFORM 2), PROTEIN SEQUENCE OF 110-178
RP (ISOFORMS 2/3), PROTEIN SEQUENCE OF 222-230 AND 301-305, FUNCTION,
RP SUBCELLULAR LOCATION, AND INTERACTION WITH UBTF.
RX PubMed=8641287; DOI=10.1002/j.1460-2075.1996.tb00575.x;
RA Hanada K., Song C.Z., Yamamoto K., Yano K., Maeda Y., Yamaguchi K.,
RA Muramatsu M.;
RT "RNA polymerase I associated factor 53 binds to the nucleolar transcription
RT factor UBF and functions in specific rDNA transcription.";
RL EMBO J. 15:2217-2226(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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] (ISOFORM 1).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 FUNCTION, IDENTIFICATION IN THE DNA-DIRECTED RNA POLYMERASE I COMPLEX, AND
RP SUBCELLULAR LOCATION.
RX PubMed=9254723; DOI=10.1007/s004120050242;
RA Seither P., Zatsepina O., Hoffmann M., Grummt I.;
RT "Constitutive and strong association of PAF53 with RNA polymerase I.";
RL Chromosoma 106:216-225(1997).
RN [6]
RP INTERACTION WITH POLR1G.
RX PubMed=15226435; DOI=10.1128/mcb.24.14.6338-6349.2004;
RA Yamamoto K., Yamamoto M., Hanada K., Nogi Y., Matsuyama T., Muramatsu M.;
RT "Multiple protein-protein interactions by RNA polymerase I-associated
RT factor PAF49 and role of PAF49 in rRNA transcription.";
RL Mol. Cell. Biol. 24:6338-6349(2004).
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 I which synthesizes ribosomal RNA
CC precursors (PubMed:8641287, PubMed:9254723). Appears to be involved in
CC the formation of the initiation complex at the promoter by mediating
CC the interaction between Pol I and UBTF/UBF (PubMed:8641287).
CC {ECO:0000269|PubMed:8641287, ECO:0000269|PubMed:9254723}.
CC -!- SUBUNIT: Component of the RNA polymerase I (Pol I) complex consisting
CC of at least 13 subunits (PubMed:9254723). Interacts with POLR1G
CC (PubMed:15226435). Also binds UBTF/UBF (PubMed:8641287). Interacts with
CC PWP1 (By similarity). {ECO:0000250|UniProtKB:Q9GZS1,
CC ECO:0000269|PubMed:15226435, ECO:0000269|PubMed:8641287,
CC ECO:0000269|PubMed:9254723}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:8641287,
CC ECO:0000269|PubMed:9254723}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8K202-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K202-2; Sequence=VSP_013536;
CC Name=3;
CC IsoId=Q8K202-3; Sequence=VSP_013536, VSP_013537, VSP_013538;
CC -!- PTM: Acetylated at Lys-436 by CREBBP/CBP, leading to decreased RNA
CC polymerase I transcription. In normal conditions, deacetylated by
CC SIRT7, promoting the association of RNA polymerase I with the rDNA
CC promoter region and coding region. In response to stress, SIRT7 is
CC released from nucleoli leading to hyperacetylation of POLR1E/PAF53 and
CC decreased association of RNA polymerase I with the rDNA promoter
CC region. {ECO:0000250|UniProtKB:Q9GZS1}.
CC -!- SIMILARITY: Belongs to the eukaryotic RPA49/POLR1E RNA polymerase
CC subunit family. {ECO:0000305}.
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DR EMBL; D14336; BAA03266.1; -; mRNA.
DR EMBL; AK050780; BAC34409.1; -; mRNA.
DR EMBL; AL824706; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC034783; AAH34783.1; -; mRNA.
DR CCDS; CCDS18131.1; -. [Q8K202-2]
DR CCDS; CCDS71378.1; -. [Q8K202-1]
DR PIR; S69245; S69245.
DR RefSeq; NP_001272729.1; NM_001285800.1. [Q8K202-1]
DR RefSeq; NP_073722.1; NM_022811.3. [Q8K202-2]
DR AlphaFoldDB; Q8K202; -.
DR SMR; Q8K202; -.
DR BioGRID; 211074; 31.
DR STRING; 10090.ENSMUSP00000121007; -.
DR iPTMnet; Q8K202; -.
DR PhosphoSitePlus; Q8K202; -.
DR EPD; Q8K202; -.
DR MaxQB; Q8K202; -.
DR PeptideAtlas; Q8K202; -.
DR PRIDE; Q8K202; -.
DR ProteomicsDB; 301596; -. [Q8K202-1]
DR ProteomicsDB; 301597; -. [Q8K202-2]
DR ProteomicsDB; 301598; -. [Q8K202-3]
DR Antibodypedia; 12019; 165 antibodies from 27 providers.
DR DNASU; 64424; -.
DR Ensembl; ENSMUST00000029999; ENSMUSP00000029999; ENSMUSG00000028318. [Q8K202-1]
DR Ensembl; ENSMUST00000107814; ENSMUSP00000103444; ENSMUSG00000028318. [Q8K202-3]
DR Ensembl; ENSMUST00000133157; ENSMUSP00000121007; ENSMUSG00000028318. [Q8K202-2]
DR GeneID; 64424; -.
DR KEGG; mmu:64424; -.
DR UCSC; uc012ddk.2; mouse. [Q8K202-1]
DR CTD; 64425; -.
DR MGI; MGI:1929022; Polr1e.
DR VEuPathDB; HostDB:ENSMUSG00000028318; -.
DR eggNOG; KOG4183; Eukaryota.
DR GeneTree; ENSGT00390000018004; -.
DR InParanoid; Q8K202; -.
DR OMA; DVYPFDE; -.
DR PhylomeDB; Q8K202; -.
DR TreeFam; TF331685; -.
DR Reactome; R-MMU-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-MMU-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-MMU-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-MMU-73863; RNA Polymerase I Transcription Termination.
DR BioGRID-ORCS; 64424; 25 hits in 75 CRISPR screens.
DR ChiTaRS; Polr1e; mouse.
DR PRO; PR:Q8K202; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8K202; protein.
DR Bgee; ENSMUSG00000028318; Expressed in otic placode and 258 other tissues.
DR ExpressionAtlas; Q8K202; baseline and differential.
DR Genevisible; Q8K202; MM.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005736; C:RNA polymerase I complex; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0001179; F:RNA polymerase I general transcription initiation factor binding; IDA:MGI.
DR GO; GO:0042790; P:nucleolar large rRNA transcription by RNA polymerase I; ISS:UniProtKB.
DR GO; GO:0001188; P:RNA polymerase I preinitiation complex assembly; IDA:MGI.
DR GO; GO:0006362; P:transcription elongation from RNA polymerase I promoter; IBA:GO_Central.
DR InterPro; IPR009668; RNA_pol-assoc_fac_A49-like.
DR PANTHER; PTHR14440; PTHR14440; 1.
DR Pfam; PF06870; RNA_pol_I_A49; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Direct protein sequencing;
KW DNA-directed RNA polymerase; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription.
FT CHAIN 1..482
FT /note="DNA-directed RNA polymerase I subunit RPA49"
FT /id="PRO_0000073957"
FT REGION 460..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZS1"
FT MOD_RES 436
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZS1"
FT VAR_SEQ 130..177
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:8641287"
FT /id="VSP_013536"
FT VAR_SEQ 431..441
FT /note="MIEIAKAMRLK -> PSTSSSSWIWI (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013537"
FT VAR_SEQ 442..482
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013538"
FT CONFLICT 3
FT /note="T -> A (in Ref. 4; AAH34783)"
FT /evidence="ECO:0000305"
FT CONFLICT 258..260
FT /note="DGV -> YDA (in Ref. 4; AAH34783)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="M -> Y (in Ref. 4; AAH34783)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 482 AA; 54034 MW; 4237E14E1B90BB31 CRC64;
MATLESPGMD DQAGDTETEA LQSARWLYCG EPDDRQKAVL VQFSNGKLQN PGDMRFTLYN
STDLVNPRQR SHRIVAAETD RLSYVGNNFG TGALKCNALC RHFVGILNKT SGQMEVYDAE
LFNMQPLFAG MGTEVIKLGG QHLYLLAFCQ PSKNLAEAGD LLLSRHRQGH CIAVLLDDDA
IEREPPLENQ NKTFRDKLDS CIEAFGSTKQ KRSLNSRRMN KVGSESLNLS VAKAAESIID
TKGVNALVSD AMQDDLQDGV LYLPPCYADA AKPEDVYRFE DILSPAEYDA LESPSEAFRK
VTSEDILKMI EENSHCSYVI EMLKSLPIDE VHRNRQARSI WFLDALIRFR AQKVIKGKRA
LGPGIPHIIN TKLLKQFTCL TYNNGRLQNL ISSSMRAKIT SYAIILALHI NNFQVDLTAL
QKDLKLSEKR MIEIAKAMRL KISKQKVSLA DGREESHRLG TLSVPLPPAQ NSDRQSKRRK
MN
