RPA1_MOUSE
ID RPA1_MOUSE Reviewed; 1717 AA.
AC O35134; Q7TSA9;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=DNA-directed RNA polymerase I subunit RPA1;
DE Short=RNA polymerase I subunit A1;
DE EC=2.7.7.6;
DE AltName: Full=DNA-directed RNA polymerase I largest subunit;
DE AltName: Full=DNA-directed RNA polymerase I subunit A;
DE AltName: Full=RNA polymerase I 194 kDa subunit;
DE Short=RPA194;
GN Name=Polr1a; Synonyms=Rpa1, Rpo1-4;
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=9236775; DOI=10.1007/s004380050487;
RA Seither P., Coy J.F., Pouska A., Grummt I.;
RT "Molecular cloning and characterization of the cDNA encoding the largest
RT subunit of mouse RNA polymerase I.";
RL Mol. Gen. Genet. 255:180-186(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Limb;
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 [3]
RP INTERACTION WITH MYO1C.
RX PubMed=16514417; DOI=10.1038/sj.embor.7400657;
RA Percipalle P., Fomproix N., Cavellan E., Voit R., Reimer G., Krueger T.,
RA Thyberg J., Scheer U., Grummt I., Oestlund Farrants A.-K.O.;
RT "The chromatin remodelling complex WSTF-SNF2h interacts with nuclear myosin
RT 1 and has a role in RNA polymerase I transcription.";
RL EMBO Rep. 7:525-530(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas, 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).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=30272023; DOI=10.1038/s42003-018-0154-z;
RA Zhang Q., Shao J., Fan H.Y., Yu C.;
RT "Evolutionarily-conserved MZIP2 is essential for crossover formation in
RT mammalian meiosis.";
RL Commun. Biol. 1:147-147(2018).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=30746471; DOI=10.1126/sciadv.aau9780;
RA Zhang Q., Ji S.Y., Busayavalasa K., Yu C.;
RT "SPO16 binds SHOC1 to promote homologous recombination and crossing-over in
RT meiotic prophase I.";
RL Sci. Adv. 5:eaau9780-eaau9780(2019).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Largest and catalytic core component of RNA polymerase I which
CC synthesizes ribosomal RNA precursors. Forms the polymerase active
CC center together with the second largest subunit. A single stranded DNA
CC template strand of the promoter is positioned within the central active
CC site cleft of Pol I. A bridging helix emanates from RPA1 and crosses
CC the cleft near the catalytic site and is thought to promote
CC translocation of Pol I by acting as a ratchet that moves the RNA-DNA
CC hybrid through the active site by switching from straight to bent
CC conformations at each step of nucleotide addition (By similarity).
CC {ECO:0000250|UniProtKB:P10964}.
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 I (Pol I) complex consisting
CC of at least 13 subunits (By similarity). Interacts with MYO1C
CC (PubMed:16514417). Interacts with ERBB2 (By similarity). Interacts with
CC DDX11 (By similarity). Interacts with RECQL5 (By similarity).
CC {ECO:0000250|UniProtKB:O95602, ECO:0000269|PubMed:16514417}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P10964}. Chromosome
CC {ECO:0000269|PubMed:30272023, ECO:0000269|PubMed:30746471}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000305}.
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; AF000938; AAB66718.1; -; mRNA.
DR EMBL; BC053744; AAH53744.1; -; mRNA.
DR CCDS; CCDS20236.1; -.
DR PIR; T13961; T13961.
DR RefSeq; NP_033114.3; NM_009088.3.
DR AlphaFoldDB; O35134; -.
DR SMR; O35134; -.
DR BioGRID; 202995; 27.
DR IntAct; O35134; 7.
DR MINT; O35134; -.
DR STRING; 10090.ENSMUSP00000060858; -.
DR iPTMnet; O35134; -.
DR PhosphoSitePlus; O35134; -.
DR EPD; O35134; -.
DR MaxQB; O35134; -.
DR PaxDb; O35134; -.
DR PeptideAtlas; O35134; -.
DR PRIDE; O35134; -.
DR ProteomicsDB; 300512; -.
DR Antibodypedia; 4117; 124 antibodies from 27 providers.
DR DNASU; 20019; -.
DR Ensembl; ENSMUST00000055296; ENSMUSP00000060858; ENSMUSG00000049553.
DR GeneID; 20019; -.
DR KEGG; mmu:20019; -.
DR UCSC; uc009chv.2; mouse.
DR CTD; 25885; -.
DR MGI; MGI:1096397; Polr1a.
DR VEuPathDB; HostDB:ENSMUSG00000049553; -.
DR eggNOG; KOG0262; Eukaryota.
DR GeneTree; ENSGT00920000149138; -.
DR HOGENOM; CLU_000487_2_4_1; -.
DR InParanoid; O35134; -.
DR OMA; RFFNRED; -.
DR OrthoDB; 591636at2759; -.
DR PhylomeDB; O35134; -.
DR TreeFam; TF103033; -.
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; 20019; 26 hits in 75 CRISPR screens.
DR ChiTaRS; Polr1a; mouse.
DR PRO; PR:O35134; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; O35134; protein.
DR Bgee; ENSMUSG00000049553; Expressed in granulocyte and 254 other tissues.
DR ExpressionAtlas; O35134; baseline and differential.
DR Genevisible; O35134; MM.
DR GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005736; C:RNA polymerase I complex; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; ISO:MGI.
DR GO; GO:0001054; F:RNA polymerase I activity; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:1904750; P:negative regulation of protein localization to nucleolus; ISO:MGI.
DR GO; GO:0009303; P:rRNA transcription; ISO:MGI.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.274.100; -; 1.
DR Gene3D; 4.10.860.120; -; 1.
DR InterPro; IPR015699; DNA-dir_RNA_pol1_lsu.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR000722; RNA_pol_asu.
DR InterPro; IPR006592; RNA_pol_N.
DR InterPro; IPR007080; RNA_pol_Rpb1_1.
DR InterPro; IPR007066; RNA_pol_Rpb1_3.
DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR InterPro; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; PTHR19376; 1.
DR PANTHER; PTHR19376:SF11; PTHR19376:SF11; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 1.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR SMART; SM00663; RPOLA_N; 1.
PE 1: Evidence at protein level;
KW Chromosome; DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transferase; Zinc.
FT CHAIN 1..1717
FT /note="DNA-directed RNA polymerase I subunit RPA1"
FT /id="PRO_0000073924"
FT REGION 968..980
FT /note="Bridging helix"
FT /evidence="ECO:0000250"
FT REGION 1372..1493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1379..1399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1400..1416
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1417..1431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1432..1451
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1452..1493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 595
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 597
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 599
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT MOD_RES 1393
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95602"
FT CONFLICT 821
FT /note="R -> H (in Ref. 2; AAH53744)"
FT /evidence="ECO:0000305"
FT CONFLICT 1246
FT /note="M -> T (in Ref. 1; AAB66718)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1717 AA; 194110 MW; E78B7E3F6F7129F1 CRC64;
MLASKHTPWR RLQGISFGMY SAEELKKLSV KSITNPRYVD YLGNPSANGL YDLALGPADS
KEVCATCVQD FNNCSGHLGH IDLPLTVYNP FLFDKLYLLL RGSCLSCHML TCPRAAIYLL
ISQLRVLEVG ALQAVYELER ILSRFLEETG DPSAFEIQEE LEEYTSKILQ NNLLGSQGTH
VKNVCESRSK LVAQFWKTHM AAKQCPHCKT GRSVVRKEHN SKLIITYPAT VHKKSDQEGT
ELPEGVPEAP GIDKAQMGKR GYLTPSSAQE HLFAIWKNEG FFLNYLFSGL DDIGPESSFN
PSMFFLDFIV VPPSRYRPVN RLGDQMFTNG QTVNLQAVMK DAVLIRKLLA LMAQEQKLPC
EMTELTIDKE NDSSVAIDRS FLGLLPGPSL TDKLYNIWIR LQSHVNIVFD SEMDKLMLEK
YPGIRQILEK KEGLFRKHMM GKRVDYAARS VICPDMYINT NEIGIPMVFA TKLTYPQPVT
PWNVQELRQA VINGPNVHPG ASMVINEDGS RTALSSVDAA QREAVAKQLL TPATGAPKPQ
GTKVVCRHVK NGDILLLNRQ PTLHRPSIQA HRARILPEEK VLRLHYANCK AYNADFDGDE
MNAHFPQSEL GRAEAYVLAC TDQQYLVPKD GQPLAGLIQD HMVSGANMTI RGCFFTREQY
MELVYRGLTD KVGRVKLFPP AILKPFPLWT GKQVVSTLLI NIIPEDYAPL NLSGKAKIGS
KAWVKEKPRP IPDFDPDSMC ESQVIIREGE LLCGVLDKAH YGSSAYGLVH CCYEIYGGET
SGRVLTCLAR LFTAYLQLYR GFTLGVEDIL VKPNADVVRQ RIIEESTQCG PQAVKAALSL
PETASCDEIQ GKWQDAHLSK DQRDFNMIDM KFKEEVNHYS NEINKACMPL GLHRQFPENN
LQMMVQSGAK GSTVNTMQIS CLLGQIELEG RRPPLMASGK SLPCFEPYEF TPRAGGFVTG
RFLTGIRPPE FFFHCMAGRE GLVDTAVKTS RSGYLQRCII KHLEGLVIQY DLTVRDSDGS
VVQFLYGEDG LDIPKTQFLQ PKQFPFLAGN YEVIMKSKHL HEVLSRADPQ KVLGHIKAIK
KWHHKHSGAL LRKGAFLSFS QKIQAAVKAL NLKGSIQNGR SPETQQMLQM WYDLDEESRW
KYQKRAAPCP DPSLSVWRPD IYFASVSETF EKKIDDFSQE WAAQAERSYK KSELSLDRLR
TLLQLKWQRS LCDPGEAVGL LAAQSIGEPS TQMTLNTFHF AGRGEMNVTL GIPRLREILM
VASANIKTPM MSVPVFDTKK ALKKVKSLKK RLTRVCLGEV LQKVDIQESF CMGEKRNKFQ
VYELRFQFLP HAYYQQEKCL RPEDILHFME TRFFKLLMEA IKKKKNKASA FRNVNSRRAT
QKDLNDTEDS GRSQREEERD EEEEGNIVDA EAEEGDADAS DTKRKEKQEE EVDYESEEEG
EEEEEEEVQE EGNIKGDGVH QGHEPDEEEH LGLEEEESSQ KPPRRHSRPQ GAEAIKRRIQ
AVRESYSFIE DYQYDTEESL WCQVTVKLPL MKINFDMSSL VVSLAHKAIV YTTKGITRCL
LNETTNSKNE KELVLNTEGI NLPELFKYSE ILDLRRLYSN DIHAMANTYG IEAALRVIEK
EIKDVFAVYG IAVDPRHLSL VADYMCFEGV YKPLNRFGIQ SSSSPLQQMT FETSFQFLKQ
ATMMGSHDEL KSPSACLVVG KVVKGGTGLF ELKQPLR
