RPA1_RAT
ID RPA1_RAT Reviewed; 1716 AA.
AC O54889;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 137.
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=A194;
DE Short=RPA194;
GN Name=Polr1a; Synonyms=Rpa1, Rpo1-4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION IN THE RNA POL I COMPLEX, AND
RP PHOSPHORYLATION.
RX PubMed=9422795; DOI=10.1074/jbc.273.2.1257;
RA Hannan R.D., Hempel W.M., Cavanaugh A., Arino T., Dimitrov S.I., Moss T.,
RA Rothblum L.;
RT "Affinity purification of mammalian RNA polymerase I. Identification of an
RT associated kinase.";
RL J. Biol. Chem. 273:1257-1267(1998).
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 (PubMed:9422795). Interacts with MYO1C (By
CC similarity). Interacts with ERBB2 (By similarity). Interacts with DDX11
CC (By similarity). Interacts with RECQL5 (By similarity).
CC {ECO:0000250|UniProtKB:O35134, ECO:0000250|UniProtKB:O95602,
CC ECO:0000269|PubMed:9422795}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P10964}. Chromosome
CC {ECO:0000250|UniProtKB:O35134}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:9422795}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000305}.
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DR EMBL; AF025425; AAB94601.1; -; mRNA.
DR PIR; T14103; T14103.
DR RefSeq; NP_113960.1; NM_031772.1.
DR AlphaFoldDB; O54889; -.
DR SMR; O54889; -.
DR IntAct; O54889; 1.
DR MINT; O54889; -.
DR STRING; 10116.ENSRNOP00000013587; -.
DR PhosphoSitePlus; O54889; -.
DR PaxDb; O54889; -.
DR PRIDE; O54889; -.
DR GeneID; 83581; -.
DR KEGG; rno:83581; -.
DR UCSC; RGD:620824; rat.
DR CTD; 25885; -.
DR RGD; 620824; Polr1a.
DR eggNOG; KOG0262; Eukaryota.
DR InParanoid; O54889; -.
DR OrthoDB; 591636at2759; -.
DR PhylomeDB; O54889; -.
DR Reactome; R-RNO-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-RNO-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-RNO-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-RNO-73863; RNA Polymerase I Transcription Termination.
DR PRO; PR:O54889; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005694; C:chromosome; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005736; C:RNA polymerase I complex; IDA:RGD.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0001054; F:RNA polymerase I activity; ISO:RGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:1904750; P:negative regulation of protein localization to nucleolus; ISO:RGD.
DR GO; GO:0009303; P:rRNA transcription; IDA:RGD.
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..1716
FT /note="DNA-directed RNA polymerase I subunit RPA1"
FT /id="PRO_0000073925"
FT REGION 968..980
FT /note="Bridging helix"
FT /evidence="ECO:0000250"
FT REGION 1368..1493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1378..1401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1402..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..1452
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1453..1467
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"
SQ SEQUENCE 1716 AA; 194192 MW; E8EE15BC23E60941 CRC64;
MLASKHTPWR RLQGISFGMY SAEELKKLSV KSITNPRYVD SLGNPSADGL YDLALGPADS
KEVCSTCVQD FNNCSGHLGH IDLPLTVYNP LLFDKLYLLL RGSCLNCHML TCPRAAIHLL
VCQLKVLDVG ALQAVYELER ILSRFLEETS DPSAFEIQEE LEEYTSKILQ NNLLGSQGAH
VKNVCESRSK LVAHFWKTHM AAKRCPHCKT GRSVVRKEHN SKLTITYPAM VHKKSGQKDA
ELPEGAPAAP GIDEAQMGKR GYLTPSSAQE HLFAIWKNEG FFLNYLFSGL DDIGPESSFN
PSMFFLDFIV VPPSRYRPIN RLGDQMFTNG QTVNLQAVMK DAVLIRKLLA VMAQEQKLPC
EMTEITIDKE NDSSGAIDRS FLSLLPGQSL TDKLYNIWIR LQSHVNIVFD SDMDKLMLEK
YPGIRQILEK KEGLFRKHMM GKRVDYAARS VICPDMYINT NEIGIPMVFA TKLTYPQPVT
PWNVQELRQA VINGPNVHPG ASMVINEDGS RTALSAVDAT QREAVAKQLL TPSTGIPKPQ
GAKVVCRHVK NGDILLLNRQ PTLHRPSIQA HRAHILPEEK VLRLHYANCK AYNADFDGDE
MNAHFPQSEL GRAEAYVLAC TDQQYLVPKD GQPLAGLIQD HMVSGANMTI RGCFFTREQY
MELVYRGLTD KVGRVKLFPP AILKPFPLWT GKQVVSTLLI NIIPEDYTPL NLTGKAKIGS
KAWVKEKPRP VPDFDPDSMC ESQVIIREGE LLCGVLDKAH YGSSAYGLVH CCYEIYGGET
SGRVLTCLAR LFTAYLQLYR GFTLGVEDIL VKPNADVMRQ RIIEESTQCG PRAVRAALNL
PEAASCDEIQ GKWQDAIWRK DQRDFNMIDM KFKEEVNHYS NEINKACMPF GLHRQFPENN
LQMMVQSGAK GSTVNTMQIS CLLGQIELEG RRPPLMASGK SLPCFEPYEF TPRAGGFVTG
RFLTGIRPPE FFFHCMAGRE GLVDTAVKTS RSGYLQRCII KHLEGLVIQY DLTVRDSDGS
VVQFLYGEDG LDIPKTQFLQ PKQFPFLASN YEVIMKSKHL HEVLSRADPQ KVLRHFRAIK
KWHHRHSSAL LRKGAFLSFS QKIQAAVKAL NLEGKTQNGR SPETQQMLQM WHELDEQSRR
KYQKRAAPCP DPSLSVWRPD IHFASVSETF EKKIDDYSQE WAAQAEKSHN RSELSLDRLR
TLLQLKWQRS LCDPGEAVGL LAAQSIGEPS TQMTLNTFHF AGRGEMNVTL GIPRLREILM
VASANIKTPM MSVPVFNTKK ALRRVKSLKK QLTRVCLGEV LQKVDIQESF CMGEKQNKFR
VYELRFQFLP HAYYQQEKCL RPEDILHFME TRFFKLLMEA IKKKNSKASA FRSVNTRRAT
QKDLDDTEDS GRNRREEERD EEEEGNIVDA EAEEGDADAS DTKRKEKQEE EVDYESEEEG
EEEEEEDVQE EENIKGEGAH QTHEPDEEEG SGLEEESSQN PPCRHSRPQG AEAMERRIQA
VRESHSFIED YQYDTEESLW CQVTVKLPLM KINFDMSSLV VSLAHNAIVY TTKGITRCLL
NETINSKNEK EFVLNTEGIN LPELFKYSEV LDLRRLYSND IHAVANTYGI EAALRVIEKE
IKDVFAVYGI AVDPRHLSLV ADYMCFEGVY KPLNRFGIQS SSSPLQQMTF ETSFQFLKQA
TMMGSHDELK SPSACLVVGK VVKGGTGLFE LKQPLR
