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O35134 (RPA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA-directed RNA polymerase I subunit RPA1

Short name=RNA polymerase I subunit A1
EC=2.7.7.6
Alternative name(s):
DNA-directed RNA polymerase I largest subunit
DNA-directed RNA polymerase I subunit A
RNA polymerase I 194 kDa subunit
Short name=RPA194
Gene names
Name:Polr1a
Synonyms:Rpa1, Rpo1-4
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1717 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic core component of RNA polymerase I which synthesizes ribosomal RNA precursors. Forms the polymerase active center together with the second largest subunit. A single stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol I. A bridging helix emanates from RPA1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol I by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition By similarity.

Catalytic activity

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).

Subunit structure

Component of the RNA polymerase I (Pol I) complex consisting of at least 13 subunits. The RNA polymerase complex associates with several transcription factors to form the respective holoenzyme complex By similarity. Interacts with MYO1C. Interacts with ERBB2 By similarity. Ref.3

Subcellular location

Nucleusnucleolus By similarity.

Post-translational modification

Phosphorylated By similarity.

Sequence similarities

Belongs to the RNA polymerase beta' chain family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 17171717DNA-directed RNA polymerase I subunit RPA1
PRO_0000073924

Regions

Region968 – 98013Bridging helix By similarity

Sites

Metal binding641Zinc By similarity
Metal binding671Zinc By similarity
Metal binding741Zinc By similarity
Metal binding771Zinc By similarity
Metal binding5951Magnesium; catalytic By similarity
Metal binding5971Magnesium; catalytic By similarity
Metal binding5991Magnesium; catalytic By similarity

Amino acid modifications

Modified residue13931Phosphoserine By similarity
Modified residue15771Phosphothreonine By similarity

Experimental info

Sequence conflict8211R → H in AAH53744. Ref.2
Sequence conflict12461M → T in AAB66718. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O35134 [UniParc].

Last modified December 7, 2004. Version 2.
Checksum: E78B7E3F6F7129F1

FASTA1,717194,110
        10         20         30         40         50         60 
MLASKHTPWR RLQGISFGMY SAEELKKLSV KSITNPRYVD YLGNPSANGL YDLALGPADS 

        70         80         90        100        110        120 
KEVCATCVQD FNNCSGHLGH IDLPLTVYNP FLFDKLYLLL RGSCLSCHML TCPRAAIYLL 

       130        140        150        160        170        180 
ISQLRVLEVG ALQAVYELER ILSRFLEETG DPSAFEIQEE LEEYTSKILQ NNLLGSQGTH 

       190        200        210        220        230        240 
VKNVCESRSK LVAQFWKTHM AAKQCPHCKT GRSVVRKEHN SKLIITYPAT VHKKSDQEGT 

       250        260        270        280        290        300 
ELPEGVPEAP GIDKAQMGKR GYLTPSSAQE HLFAIWKNEG FFLNYLFSGL DDIGPESSFN 

       310        320        330        340        350        360 
PSMFFLDFIV VPPSRYRPVN RLGDQMFTNG QTVNLQAVMK DAVLIRKLLA LMAQEQKLPC 

       370        380        390        400        410        420 
EMTELTIDKE NDSSVAIDRS FLGLLPGPSL TDKLYNIWIR LQSHVNIVFD SEMDKLMLEK 

       430        440        450        460        470        480 
YPGIRQILEK KEGLFRKHMM GKRVDYAARS VICPDMYINT NEIGIPMVFA TKLTYPQPVT 

       490        500        510        520        530        540 
PWNVQELRQA VINGPNVHPG ASMVINEDGS RTALSSVDAA QREAVAKQLL TPATGAPKPQ 

       550        560        570        580        590        600 
GTKVVCRHVK NGDILLLNRQ PTLHRPSIQA HRARILPEEK VLRLHYANCK AYNADFDGDE 

       610        620        630        640        650        660 
MNAHFPQSEL GRAEAYVLAC TDQQYLVPKD GQPLAGLIQD HMVSGANMTI RGCFFTREQY 

       670        680        690        700        710        720 
MELVYRGLTD KVGRVKLFPP AILKPFPLWT GKQVVSTLLI NIIPEDYAPL NLSGKAKIGS 

       730        740        750        760        770        780 
KAWVKEKPRP IPDFDPDSMC ESQVIIREGE LLCGVLDKAH YGSSAYGLVH CCYEIYGGET 

       790        800        810        820        830        840 
SGRVLTCLAR LFTAYLQLYR GFTLGVEDIL VKPNADVVRQ RIIEESTQCG PQAVKAALSL 

       850        860        870        880        890        900 
PETASCDEIQ GKWQDAHLSK DQRDFNMIDM KFKEEVNHYS NEINKACMPL GLHRQFPENN 

       910        920        930        940        950        960 
LQMMVQSGAK GSTVNTMQIS CLLGQIELEG RRPPLMASGK SLPCFEPYEF TPRAGGFVTG 

       970        980        990       1000       1010       1020 
RFLTGIRPPE FFFHCMAGRE GLVDTAVKTS RSGYLQRCII KHLEGLVIQY DLTVRDSDGS 

      1030       1040       1050       1060       1070       1080 
VVQFLYGEDG LDIPKTQFLQ PKQFPFLAGN YEVIMKSKHL HEVLSRADPQ KVLGHIKAIK 

      1090       1100       1110       1120       1130       1140 
KWHHKHSGAL LRKGAFLSFS QKIQAAVKAL NLKGSIQNGR SPETQQMLQM WYDLDEESRW 

      1150       1160       1170       1180       1190       1200 
KYQKRAAPCP DPSLSVWRPD IYFASVSETF EKKIDDFSQE WAAQAERSYK KSELSLDRLR 

      1210       1220       1230       1240       1250       1260 
TLLQLKWQRS LCDPGEAVGL LAAQSIGEPS TQMTLNTFHF AGRGEMNVTL GIPRLREILM 

      1270       1280       1290       1300       1310       1320 
VASANIKTPM MSVPVFDTKK ALKKVKSLKK RLTRVCLGEV LQKVDIQESF CMGEKRNKFQ 

      1330       1340       1350       1360       1370       1380 
VYELRFQFLP HAYYQQEKCL RPEDILHFME TRFFKLLMEA IKKKKNKASA FRNVNSRRAT 

      1390       1400       1410       1420       1430       1440 
QKDLNDTEDS GRSQREEERD EEEEGNIVDA EAEEGDADAS DTKRKEKQEE EVDYESEEEG 

      1450       1460       1470       1480       1490       1500 
EEEEEEEVQE EGNIKGDGVH QGHEPDEEEH LGLEEEESSQ KPPRRHSRPQ GAEAIKRRIQ 

      1510       1520       1530       1540       1550       1560 
AVRESYSFIE DYQYDTEESL WCQVTVKLPL MKINFDMSSL VVSLAHKAIV YTTKGITRCL 

      1570       1580       1590       1600       1610       1620 
LNETTNSKNE KELVLNTEGI NLPELFKYSE ILDLRRLYSN DIHAMANTYG IEAALRVIEK 

      1630       1640       1650       1660       1670       1680 
EIKDVFAVYG IAVDPRHLSL VADYMCFEGV YKPLNRFGIQ SSSSPLQQMT FETSFQFLKQ 

      1690       1700       1710 
ATMMGSHDEL KSPSACLVVG KVVKGGTGLF ELKQPLR 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of the cDNA encoding the largest subunit of mouse RNA polymerase I."
Seither P., Coy J.F., Pouska A., Grummt I.
Mol. Gen. Genet. 255:180-186(1997) [PubMed: 9236775] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Limb.
[3]"The chromatin remodelling complex WSTF-SNF2h interacts with nuclear myosin 1 and has a role in RNA polymerase I transcription."
Percipalle P., Fomproix N., Cavellan E., Voit R., Reimer G., Krueger T., Thyberg J., Scheer U., Grummt I., Oestlund Farrants A.-K.O.
EMBO Rep. 7:525-530(2006) [PubMed: 16514417] [Abstract]
Cited for: INTERACTION WITH MYO1C.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF000938 mRNA. Translation: AAB66718.1.
BC053744 mRNA. Translation: AAH53744.1.
IPIIPI00313726.
PIRT13961.
RefSeqNP_033114.3. NM_009088.3.
UniGeneMm.135581.

3D structure databases

ProteinModelPortalO35134.
SMRO35134. Positions 3-1717.
ModBaseSearch...

Protein-protein interaction databases

STRINGO35134.

PTM databases

PhosphoSiteO35134.

Proteomic databases

PRIDEO35134.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000055296; ENSMUSP00000060858; ENSMUSG00000049553.
GeneID20019.
KEGGmmu:20019.
UCSCuc009chv.2. mouse.

Organism-specific databases

CTD25885.
MGIMGI:1096397. Polr1a.

Phylogenomic databases

eggNOGroNOG13453.
HOGENOMHBG598940.
HOVERGENHBG017741.
InParanoidO35134.
OMARRATQKD.
OrthoDBEOG41VK23.
PhylomeDBO35134.

Enzyme and pathway databases

ReactomeREACT_107193. Transcription.

Gene expression databases

ArrayExpressO35134.
BgeeO35134.
CleanExMM_RPA1.
GenevestigatorO35134.
GermOnlineENSMUSG00000049553. Mus musculus.

Family and domain databases

InterProIPR015699. DNA-dir_RNA_pol1_lsu.
IPR000722. RNA_pol_asu.
IPR006592. RNA_pol_N.
IPR007080. RNA_pol_Rpb1_1.
IPR007066. RNA_pol_Rpb1_3.
IPR007083. RNA_pol_Rpb1_4.
IPR007081. RNA_pol_Rpb1_5.
[Graphical view]
KOK02999.
PANTHERPTHR19376:SF11. RNA_polyI. 1 hit.
PfamPF04997. RNA_pol_Rpb1_1. 1 hit.
PF00623. RNA_pol_Rpb1_2. 1 hit.
PF04983. RNA_pol_Rpb1_3. 1 hit.
PF05000. RNA_pol_Rpb1_4. 1 hit.
PF04998. RNA_pol_Rpb1_5. 1 hit.
[Graphical view]
SMARTSM00663. RPOLA_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio297531.
SOURCESearch...

Entry information

Entry nameRPA1_MOUSE
AccessionPrimary (citable) accession number: O35134
Secondary accession number(s): Q7TSA9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 7, 2004
Last modified: November 16, 2011
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families