RPA2_MOUSE
ID RPA2_MOUSE Reviewed; 1135 AA.
AC P70700; Q3UMX7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=DNA-directed RNA polymerase I subunit RPA2;
DE Short=RNA polymerase I subunit 2;
DE EC=2.7.7.6 {ECO:0000250|UniProtKB:Q9H9Y6};
DE AltName: Full=DNA-directed RNA polymerase I 135 kDa polypeptide;
DE Short=RPA135;
GN Name=Polr1b; Synonyms=Rpa2, Rpo1-2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8921381; DOI=10.1006/geno.1996.0531;
RA Seither P., Grummt I.;
RT "Molecular cloning of RPA2, the gene encoding the second largest subunit of
RT mouse RNA polymerase I.";
RL Genomics 37:135-139(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=30272023; DOI=10.1038/s42003-018-0154-z;
RA Zhang Q., Shao J., Fan H.Y., Yu C.;
RT "Evolutionarily-conserved MZIP2 is essential for crossover formation in
RT mammalian meiosis.";
RL Commun. Biol. 1:147-147(2018).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=30949703; DOI=10.1093/nar/gkz226;
RA Liu H., Huang T., Li M., Li M., Zhang C., Jiang J., Yu X., Yin Y.,
RA Zhang F., Lu G., Luo M.C., Zhang L.R., Li J., Liu K., Chen Z.J.;
RT "SCRE serves as a unique synaptonemal complex fastener and is essential for
RT progression of meiosis prophase I in mice.";
RL Nucleic Acids Res. 47:5670-5683(2019).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=30746471; DOI=10.1126/sciadv.aau9780;
RA Zhang Q., Ji S.Y., Busayavalasa K., Yu C.;
RT "SPO16 binds SHOC1 to promote homologous recombination and crossing-over in
RT meiotic prophase I.";
RL Sci. Adv. 5:eaau9780-eaau9780(2019).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Second largest core component of RNA polymerase I which synthesizes
CC ribosomal RNA precursors. Proposed to contribute to the polymerase
CC catalytic activity and forms the polymerase active center together with
CC the largest subunit. Pol I is composed of mobile elements and RPA2 is
CC part of the core element with the central large cleft and probably a
CC clamp element that moves to open and close the cleft.
CC {ECO:0000250|UniProtKB:Q9H9Y6}.
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; Evidence={ECO:0000250|UniProtKB:Q9H9Y6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21249;
CC Evidence={ECO:0000250|UniProtKB:Q9H9Y6};
CC -!- SUBUNIT: Component of the RNA polymerase I (Pol I) complex consisting
CC of at least 13 subunits. {ECO:0000250|UniProtKB:Q9H9Y6}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q9H9Y6}. Chromosome
CC {ECO:0000269|PubMed:30272023, ECO:0000269|PubMed:30746471,
CC ECO:0000269|PubMed:30949703}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U58280; AAC52850.1; -; mRNA.
DR EMBL; AK143501; BAE25401.1; -; mRNA.
DR EMBL; AK144616; BAE25971.1; -; mRNA.
DR EMBL; AL833780; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX000699; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466519; EDL28227.1; -; Genomic_DNA.
DR CCDS; CCDS16720.1; -.
DR PIR; T42723; T42723.
DR RefSeq; NP_033112.2; NM_009086.2.
DR AlphaFoldDB; P70700; -.
DR SMR; P70700; -.
DR BioGRID; 202993; 8.
DR IntAct; P70700; 2.
DR STRING; 10090.ENSMUSP00000099494; -.
DR iPTMnet; P70700; -.
DR PhosphoSitePlus; P70700; -.
DR EPD; P70700; -.
DR MaxQB; P70700; -.
DR PaxDb; P70700; -.
DR PeptideAtlas; P70700; -.
DR PRIDE; P70700; -.
DR ProteomicsDB; 260919; -.
DR Antibodypedia; 18109; 127 antibodies from 24 providers.
DR DNASU; 20017; -.
DR Ensembl; ENSMUST00000103205; ENSMUSP00000099494; ENSMUSG00000027395.
DR GeneID; 20017; -.
DR KEGG; mmu:20017; -.
DR UCSC; uc008mhf.2; mouse.
DR CTD; 84172; -.
DR MGI; MGI:108014; Polr1b.
DR VEuPathDB; HostDB:ENSMUSG00000027395; -.
DR eggNOG; KOG0216; Eukaryota.
DR GeneTree; ENSGT00950000183132; -.
DR HOGENOM; CLU_000524_5_1_1; -.
DR InParanoid; P70700; -.
DR OMA; FFGVVHY; -.
DR OrthoDB; 42570at2759; -.
DR PhylomeDB; P70700; -.
DR TreeFam; TF103055; -.
DR Reactome; R-MMU-5250924; B-WICH complex positively 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-73863; RNA Polymerase I Transcription Termination.
DR BioGRID-ORCS; 20017; 28 hits in 73 CRISPR screens.
DR ChiTaRS; Polr1b; mouse.
DR PRO; PR:P70700; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P70700; protein.
DR Bgee; ENSMUSG00000027395; Expressed in ileal epithelium and 203 other tissues.
DR ExpressionAtlas; P70700; baseline and differential.
DR Genevisible; P70700; MM.
DR GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005736; C:RNA polymerase I complex; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR GO; GO:0007566; P:embryo implantation; IMP:MGI.
DR GO; GO:0014029; P:neural crest formation; ISS:UniProtKB.
DR GO; GO:0017126; P:nucleologenesis; IMP:MGI.
DR GO; GO:0009303; P:rRNA transcription; IMP:MGI.
DR CDD; cd00653; RNA_pol_B_RPB2; 1.
DR Gene3D; 2.40.270.10; -; 1.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 1.
DR InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
DR InterPro; IPR007121; RNA_pol_bsu_CS.
DR InterPro; IPR007644; RNA_pol_bsu_protrusion.
DR InterPro; IPR007642; RNA_pol_Rpb2_2.
DR InterPro; IPR037034; RNA_pol_Rpb2_2_sf.
DR InterPro; IPR007645; RNA_pol_Rpb2_3.
DR InterPro; IPR007641; RNA_pol_Rpb2_7.
DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR InterPro; IPR009674; Rpa2_dom_4.
DR PANTHER; PTHR20856; PTHR20856; 1.
DR Pfam; PF06883; RNA_pol_Rpa2_4; 1.
DR Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR Pfam; PF04561; RNA_pol_Rpb2_2; 1.
DR Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR PROSITE; PS01166; RNA_POL_BETA; 1.
PE 1: Evidence at protein level;
KW Chromosome; DNA-directed RNA polymerase; Metal-binding;
KW Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1135
FT /note="DNA-directed RNA polymerase I subunit RPA2"
FT /id="PRO_0000048073"
FT ZN_FING 1070..1101
FT /note="C4-type"
FT /evidence="ECO:0000250|UniProtKB:P22138"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1051
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H9Y6"
FT CONFLICT 184
FT /note="V -> E (in Ref. 1; AAC52850)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="I -> V (in Ref. 1; AAC52850)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="C -> G (in Ref. 1; AAC52850)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="L -> R (in Ref. 1; AAC52850)"
FT /evidence="ECO:0000305"
FT CONFLICT 449
FT /note="Q -> E (in Ref. 1; AAC52850)"
FT /evidence="ECO:0000305"
FT CONFLICT 525..526
FT /note="VY -> GD (in Ref. 1; AAC52850)"
FT /evidence="ECO:0000305"
FT CONFLICT 541..542
FT /note="PV -> GA (in Ref. 1; AAC52850)"
FT /evidence="ECO:0000305"
FT CONFLICT 814
FT /note="F -> S (in Ref. 1; AAC52850)"
FT /evidence="ECO:0000305"
FT CONFLICT 1069
FT /note="M -> V (in Ref. 1; AAC52850)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1135 AA; 128213 MW; AF0E1BE0A98116E6 CRC64;
MDVDGRWRNL PSGPSLKHLT DPSYGIPPEQ QKAALQDLTR AHVDSFNYAA LEGLSHAVQA
IPPFEFAFKD ERISLTIVDA VISPPSVPKG TICKDLNVYP AECRGRKSTY RGRLTADISW
AVNGVPKGII KQFLGYVPIM VKSKLCNLYN LPPRVLIEHH EEAEEMGGYF IINGIEKVIR
MLIVPRRNFP IAMVRPKWKS RGLGYTQFGV SMRCVREEHS AVNMNLHYVE NGTVMLNFIY
RKELFFLPLG FALKALVSFS DYQIFQELIK GKEEDSFFRN SVSQMLRIVI EEGCHSQKQV
LNYLGECFRV KLSLPDWYPN VEAAEFLLNQ CICIHLQSNT DKFYLLCLMT RKLFALARGE
CMDDNPDSLV NQEVLSPGQL FLMFLKEKME NWLVSIKIVL DKRAQKANVS INNENLMKIF
SMGTELTRPF EYLLATGNLR SKTGLGFLQD SGLCVVADKL NFLRYLSHFR CVHRGAAFAK
MRTTTVRRLL PESWGFLCPV HTPDGAPCGL LNHLTAVCEV VTKFVYTASI PALLCGLGVT
PVDTAPCRPY SDCYPVLLDG VMVGWVDKDL APEVADTLRR FKVLREKRIP PWMEVALIPM
TGKPSLYPGL FLFTTPCRLV RPVQNLELGR EELIGTMEQL FMNVAIFEDE VFGGISTHQE
LFPHSLLSVI ANFIPFSDHN QSPRNMYQCQ MGKQTMGFPL LTYQNRSDNK LYRLQTPQSP
LVRPCMYDFY DMDNYPIGTN AIVAVISYTG YDMEDAMIVN KASWERGFAH GSVYKSEFID
LSEKFKQGED NLVFGVKPGD PRVMQKLDDD GLPFIGAKLE YGDPYYSYLN LNTGEGFVVY
YKSKENCVVD NIKVCSNDMG SGKFKCICIT VRIPRNPTIG DKFASRHGQK GILSRLWPAE
DMPFTESGMM PDILFNPHGF PSRMTIGMLI ESMAGKSAAL HGLCHDATPF IFSEENSALE
YFGEMLKAAG YNFYGTERLY SGISGMELEA DIFIGVVYYQ RLRHMVSDKF QVRTTGARDK
VTNQPLGGRN VQGGIRFGEM ERDALLAHGT SFLLHDRLFN CSDRSVAHMC VECGSLLSPL
LEKPPPSWSA MRNRKYNCTV CGRSDTIDTV SVPYVFRYFV AELAAMNIKV KLDVI
