Legends: 1, Magnesium; catalytic. {ECO:0000250}; 2, Phosphoserine. {ECO:0000250|UniProtKB:O95602}; 3, CONFLICT R -> H (in Ref. 2; AAH53744). {ECO:0000305}; 4, CONFLICT M -> T (in Ref. 1; AAB66718). {ECO:0000305}; 5, REGION Bridging helix. {ECO:0000250}; 6, ipfam:RNA_pol_Rpb1_3 [T]; 7, ipfam:RNA_pol_Rpb1_4 [T]; 8, ipfam:RNA_pol_Rpb1_2 [T]; 9, ipfam:RNA_pol_Rpb1_1 [T].
|
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 30-NOV-2016, entry version 141.
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;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; 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
RT largest 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
RT project: 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.,
RA Krueger T., Thyberg J., Scheer U., Grummt I.,
RA Oestlund Farrants A.-K.O.;
RT "The chromatin remodelling complex WSTF-SNF2h interacts with nuclear
RT myosin 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
RT expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription
CC of DNA into RNA using the four ribonucleoside triphosphates as
CC substrates. Largest and catalytic core component of RNA polymerase
CC I which synthesizes ribosomal RNA precursors. Forms the polymerase
CC active center together with the second largest subunit. A single
CC stranded DNA template strand of the promoter is positioned within
CC the central active site cleft of Pol I. A bridging helix emanates
CC from RPA1 and crosses the cleft near the catalytic site and is
CC thought to promote translocation of Pol I by acting as a ratchet
CC that moves the RNA-DNA hybrid through the active site by switching
CC from straight to bent conformations at each step of nucleotide
CC addition (By similarity). {ECO:0000250|UniProtKB:P10964}.
CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
CC + RNA(n+1).
CC -!- SUBUNIT: Component of the RNA polymerase I (Pol I) complex
CC consisting of at least 13 subunits (By similarity). Interacts with
CC MYO1C (PubMed:16514417). Interacts with ERBB2 (By similarity).
CC Interacts with DDX11 (By similarity).
CC {ECO:0000250|UniProtKB:O95602, ECO:0000269|PubMed:16514417}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000305}.
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 UniGene; Mm.135581; -.
DR ProteinModelPortal; O35134; -.
DR SMR; O35134; -.
DR BioGrid; 202995; 8.
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 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 eggNOG; KOG0262; Eukaryota.
DR eggNOG; COG0086; LUCA.
DR GeneTree; ENSGT00550000074861; -.
DR HOGENOM; HOG000205401; -.
DR HOVERGEN; HBG017741; -.
DR InParanoid; O35134; -.
DR KO; K02999; -.
DR OMA; QAVMKDM; -.
DR OrthoDB; EOG091G00IM; -.
DR PhylomeDB; O35134; -.
DR TreeFam; TF103033; -.
DR Reactome; R-MMU-427413; NoRC negatively regulates rRNA expression.
DR Reactome; R-MMU-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-MMU-573389; NoRC negatively 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-73777; RNA Polymerase I Chain Elongation.
DR Reactome; R-MMU-73863; RNA Polymerase I Transcription Termination.
DR ChiTaRS; Polr1a; mouse.
DR PRO; PR:O35134; -.
DR Proteomes; UP000000589; Chromosome 6.
DR Bgee; ENSMUSG00000049553; -.
DR CleanEx; MM_RPA1; -.
DR ExpressionAtlas; O35134; baseline and differential.
DR Genevisible; O35134; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005736; C:DNA-directed RNA polymerase I complex; IDA:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; 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 RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000183; P:chromatin silencing at rDNA; TAS:Reactome.
DR GO; GO:0006361; P:transcription initiation from RNA polymerase I promoter; TAS:Reactome.
DR InterPro; IPR015699; DNA-dir_RNA_pol1_lsu.
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; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR PANTHER; PTHR19376:SF11; PTHR19376:SF11; 4.
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 Complete proteome; DNA-directed RNA polymerase; Magnesium;
KW Metal-binding; Nucleotidyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transferase; Zinc.
FT CHAIN 1 1717 DNA-directed RNA polymerase I subunit
FT RPA1.
FT /FTId=PRO_0000073924.
FT REGION 968 980 Bridging helix. {ECO:0000250}.
FT METAL 64 64 Zinc. {ECO:0000250}.
FT METAL 67 67 Zinc. {ECO:0000250}.
FT METAL 74 74 Zinc. {ECO:0000250}.
FT METAL 77 77 Zinc. {ECO:0000250}.
FT METAL 595 595 Magnesium; catalytic. {ECO:0000250}.
FT METAL 597 597 Magnesium; catalytic. {ECO:0000250}.
FT METAL 599 599 Magnesium; catalytic. {ECO:0000250}.
FT MOD_RES 1393 1393 Phosphoserine.
FT {ECO:0000250|UniProtKB:O95602}.
FT CONFLICT 821 821 R -> H (in Ref. 2; AAH53744).
FT {ECO:0000305}.
FT CONFLICT 1246 1246 M -> T (in Ref. 1; AAB66718).
FT {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 302 649 ismart:RPOLA_N [T]
FT MYHIT 965 1665 ipfam:RNA_pol_Rpb1_5 [T]
FT MYHIT 624 809 ipfam:RNA_pol_Rpb1_3 [T]
FT MYHIT 850 958 ipfam:RNA_pol_Rpb1_4 [T]
FT MYHIT 441 620 ipfam:RNA_pol_Rpb1_2 [T]
FT MYHIT 11 358 ipfam:RNA_pol_Rpb1_1 [T]
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
//
|