Polr1a
entrez
20019
canonical
uniprot
O35134
canonical
ensembl
ENSMUSG00000049553
resolver
ensp
ENSMUSP00000060858
resolver
enst
ENSMUST00000055296
resolver
genesymbol
Polr1a
resolver
genesymbol_syn
Rpa1
resolver
genesymbol_syn
Rpo1-4
resolver
uniprot
Q3TU49
resolver
uniprot
Q3UHI3
resolver
uniprot
Q7TSA9
resolver
uniprot_entry
Q3TU49_MOUSE
resolver
uniprot_entry
Q3UHI3_MOUSE
resolver
uniprot_entry
RPA1_MOUSE
resolver
uniprot_sec
Q7TSA9
resolver
amino_acid_sequence
MLASKHTPWRRLQGISFGMYSAEELKKLSVKSITNPRYVDYLGNPSANGLYDLALGPADSKEVCATCVQDFNNCSGHLGHIDLPLTVYNPFLFDKLYLLLRGSCLSCHMLTCPRAAIYLLISQLRVLEVGALQAVYELERILSRFLEETGDPSAFEIQEELEEYTSKILQNNLLGSQGTHVKNVCESRSKLVAQFWKTHMAAKQCPHCKTGRSVVRKEHNSKLIITYPATVHKKSDQEGTELPEGVPEAPGIDKAQMGKRGYLTPSSAQEHLFAIWKNEGFFLNYLFSGLDDIGPESSFNPSMFFLDFIVVPPSRYRPVNRLGDQMFTNGQTVNLQAVMKDAVLIRKLLALMAQEQKLPCEMTELTIDKENDSSVAIDRSFLGLLPGPSLTDKLYNIWIRLQSHVNIVFDSEMDKLMLEKYPGIRQILEKKEGLFRKHMMGKRVDYAARSVICPDMYINTNEIGIPMVFATKLTYPQPVTPWNVQELRQAVINGPNVHPGASMVINEDGSRTALSSVDAAQREAVAKQLLTPATGAPKPQGTKVVCRHVKNGDILLLNRQPTLHRPSIQAHRARILPEEKVLRLHYANCKAYNADFDGDEMNAHFPQSELGRAEAYVLACTDQQYLVPKDGQPLAGLIQDHMVSGANMTIRGCFFTREQYMELVYRGLTDKVGRVKLFPPAILKPFPLWTGKQVVSTLLINIIPEDYAPLNLSGKAKIGSKAWVKEKPRPIPDFDPDSMCESQVIIREGELLCGVLDKAHYGSSAYGLVHCCYEIYGGETSGRVLTCLARLFTAYLQLYRGFTLGVEDILVKPNADVVRQRIIEESTQCGPQAVKAALSLPETASCDEIQGKWQDAHLSKDQRDFNMIDMKFKEEVNHYSNEINKACMPLGLHRQFPENNLQMMVQSGAKGSTVNTMQISCLLGQIELEGRRPPLMASGKSLPCFEPYEFTPRAGGFVTGRFLTGIRPPEFFFHCMAGREGLVDTAVKTSRSGYLQRCIIKHLEGLVIQYDLTVRDSDGSVVQFLYGEDGLDIPKTQFLQPKQFPFLAGNYEVIMKSKHLHEVLSRADPQKVLGHIKAIKKWHHKHSGALLRKGAFLSFSQKIQAAVKALNLKGSIQNGRSPETQQMLQMWYDLDEESRWKYQKRAAPCPDPSLSVWRPDIYFASVSETFEKKIDDFSQEWAAQAERSYKKSELSLDRLRTLLQLKWQRSLCDPGEAVGLLAAQSIGEPSTQMTLNTFHFAGRGEMNVTLGIPRLREILMVASANIKTPMMSVPVFDTKKALKKVKSLKKRLTRVCLGEVLQKVDIQESFCMGEKRNKFQVYELRFQFLPHAYYQQEKCLRPEDILHFMETRFFKLLMEAIKKKKNKASAFRNVNSRRATQKDLNDTEDSGRSQREEERDEEEEGNIVDAEAEEGDADASDTKRKEKQEEEVDYESEEEGEEEEEEEVQEEGNIKGDGVHQGHEPDEEEHLGLEEEESSQKPPRRHSRPQGAEAIKRRIQAVRESYSFIEDYQYDTEESLWCQVTVKLPLMKINFDMSSLVVSLAHKAIVYTTKGITRCLLNETTNSKNEKELVLNTEGINLPELFKYSEILDLRRLYSNDIHAMANTYGIEAALRVIEKEIKDVFAVYGIAVDPRHLSLVADYMCFEGVYKPLNRFGIQSSSSPLQQMTFETSFQFLKQATMMGSHDELKSPSACLVVGKVVKGGTGLFELKQPLR
uniprot
proteins
ec_number
2.7.7.6
uniprot
proteins
function
FUNCTION: Catalytic core component of RNA polymerase I (Pol I), a DNA-dependent RNA polymerase which synthesizes ribosomal RNA precursors using the four ribonucleoside triphosphates as substrates. Transcribes 47S pre-rRNAs from multicopy rRNA gene clusters, giving rise to 5.8S, 18S and 28S ribosomal RNAs (By similarity). Pol I-mediated transcription cycle proceeds through transcription initiation, transcription elongation and transcription termination stages. During transcription initiation, Pol I pre-initiation complex (PIC) is recruited by the selectivity factor 1 (SL1/TIF-IB) complex bound to the core promoter that precedes an rDNA repeat unit. The PIC assembly bends the promoter favoring the formation of the transcription bubble and promoter escape. Once the polymerase has escaped from the promoter it enters the elongation phase during which RNA is actively polymerized, based on complementarity with the template DNA strand. Highly processive, assembles in structures referred to as 'Miller trees' where many elongating Pol I complexes queue and transcribe the same rDNA coding regions. At terminator sequences downstream of the rDNA gene, PTRF interacts with Pol I and halts Pol I transcription leading to the release of the RNA transcript and polymerase from the DNA (By similarity). Forms Pol I active center together with the second largest subunit POLR1B/RPA2. Appends one nucleotide at a time to the 3' end of the nascent RNA, with POLR1A/RPA1 contributing a Mg(2+)-coordinating DxDGD motif, and POLR1B/RPA2 participating in the coordination of a second Mg(2+) ion and providing lysine residues believed to facilitate Watson-Crick base pairing between the incoming nucleotide and the template base. Typically, Mg(2+) ions direct a 5' nucleoside triphosphate to form a phosphodiester bond with the 3' hydroxyl of the preceding nucleotide of the nascent RNA, with the elimination of pyrophosphate. Has proofreading activity: Pauses and backtracks to allow the cleavage of a missincorporated nucleotide via POLR1H/RPA12. High Pol I processivity is associated with decreased transcription fidelity (By similarity) (PubMed:10589839). {ECO:0000250|UniProtKB:O95602, ECO:0000250|UniProtKB:P10964, ECO:0000269|PubMed:10589839}.
uniprot
proteins
mass_dalton
194110
uniprot
proteins
mutagenesis
MUTAGEN 1559; /note="C->F: Embryonic lethal at homozygosity."; /evidence="ECO:0000269|PubMed:37075751
uniprot
proteins
post_translational_modification
PTM: Phosphorylated. {ECO:0000250}.
uniprot
proteins
protein_family
RNA polymerase beta' chain family
uniprot
proteins
pubmed
10589839
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16514417
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
30272023
uniprot
proteins
pubmed
30746471
uniprot
proteins
pubmed
37075751
uniprot
proteins
pubmed
9236775
uniprot
proteins
sequence_length
1717
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:O95602}. Chromosome {ECO:0000269|PubMed:30272023, ECO:0000269|PubMed:30746471}.
uniprot
proteins