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DescriptionRecName: Full=DNA-directed RNA polymerase I subunit RPA1; Short=RNA polymerase I subunit A1; EC=2.7.7.6; AltName: Full=DNA-directed RNA polymerase I largest subunit; AltName: Full=DNA-directed RNA polymerase I subunit A; AltName: Full=RNA polymerase I 194 kDa subunit; Short=RPA194;
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MyHits synonymsRPA1_MOUSE , O35134 , Q7TSA9 , E78B7E3F6F7129F1
match map segment
ismart:RPOLA_N ipfam:RNA_pol_Rpb1_5 ipfam:RNA_pol_Rpb1_3 ipfam:RNA_pol_Rpb1_4 ipfam:RNA_pol_Rpb1_2 ipfam:RNA_pol_Rpb1_1  
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
//