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RPAB5_MOUSE
ID   RPAB5_MOUSE             Reviewed;          67 AA.
AC   P62876; P52436; Q3UF14;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=DNA-directed RNA polymerases I, II, and III subunit RPABC5;
DE            Short=RNA polymerases I, II, and III subunit ABC5;
DE   AltName: Full=DNA-directed RNA polymerase III subunit L;
DE   AltName: Full=RPB10 homolog;
GN   Name=Polr2l;
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and DBA/2J; TISSUE=Liver, and Sympathetic ganglion;
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).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       Common component of RNA polymerases I, II and III which synthesize
CC       ribosomal RNA precursors, mRNA precursors and many functional non-
CC       coding RNAs, and a small RNAs, such as 5S rRNA and tRNAs, respectively.
CC       Pol II is the central component of the basal RNA polymerase II
CC       transcription machinery. Pols are composed of mobile elements that move
CC       relative to each other. In Pol II, POLR2L/RBP10 is part of the core
CC       element with the central large cleft (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the RNA polymerase I (Pol I), RNA polymerase II
CC       (Pol II) and RNA polymerase III (Pol III) complexes consisting of at
CC       least 13, 12 and 17 subunits, respectively. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the archaeal Rpo10/eukaryotic RPB10 RNA
CC       polymerase subunit family. {ECO:0000305}.
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DR   EMBL; AK011021; BAB27338.1; -; mRNA.
DR   EMBL; AK149137; BAE28747.1; -; mRNA.
DR   EMBL; AK168159; BAE40122.1; -; mRNA.
DR   CCDS; CCDS52446.1; -.
DR   RefSeq; NP_079869.1; NM_025593.1.
DR   AlphaFoldDB; P62876; -.
DR   SMR; P62876; -.
DR   IntAct; P62876; 1.
DR   MINT; P62876; -.
DR   STRING; 10090.ENSMUSP00000043204; -.
DR   iPTMnet; P62876; -.
DR   PhosphoSitePlus; P62876; -.
DR   EPD; P62876; -.
DR   MaxQB; P62876; -.
DR   PaxDb; P62876; -.
DR   PRIDE; P62876; -.
DR   ProteomicsDB; 260834; -.
DR   Antibodypedia; 22712; 103 antibodies from 20 providers.
DR   Ensembl; ENSMUST00000043870; ENSMUSP00000043204; ENSMUSG00000038489.
DR   GeneID; 66491; -.
DR   KEGG; mmu:66491; -.
DR   UCSC; uc009klm.2; mouse.
DR   CTD; 5441; -.
DR   MGI; MGI:1913741; Polr2l.
DR   VEuPathDB; HostDB:ENSMUSG00000038489; -.
DR   eggNOG; KOG3497; Eukaryota.
DR   GeneTree; ENSGT00390000007087; -.
DR   HOGENOM; CLU_143122_1_1_1; -.
DR   InParanoid; P62876; -.
DR   OMA; YCCRRMF; -.
DR   OrthoDB; 1639063at2759; -.
DR   PhylomeDB; P62876; -.
DR   TreeFam; TF103046; -.
DR   Reactome; R-MMU-112382; Formation of RNA Pol II elongation complex.
DR   Reactome; R-MMU-113418; Formation of the Early Elongation Complex.
DR   Reactome; R-MMU-5250924; B-WICH complex positively regulates rRNA expression.
DR   Reactome; R-MMU-5578749; Transcriptional regulation by small RNAs.
DR   Reactome; R-MMU-674695; RNA Polymerase II Pre-transcription Events.
DR   Reactome; R-MMU-6781823; Formation of TC-NER Pre-Incision Complex.
DR   Reactome; R-MMU-6782135; Dual incision in TC-NER.
DR   Reactome; R-MMU-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   Reactome; R-MMU-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR   Reactome; R-MMU-6803529; FGFR2 alternative splicing.
DR   Reactome; R-MMU-6807505; RNA polymerase II transcribes snRNA genes.
DR   Reactome; R-MMU-72086; mRNA Capping.
DR   Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR   Reactome; R-MMU-72165; mRNA Splicing - Minor Pathway.
DR   Reactome; R-MMU-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR   Reactome; R-MMU-73762; RNA Polymerase I Transcription Initiation.
DR   Reactome; R-MMU-73772; RNA Polymerase I Promoter Escape.
DR   Reactome; R-MMU-73776; RNA Polymerase II Promoter Escape.
DR   Reactome; R-MMU-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR   Reactome; R-MMU-73863; RNA Polymerase I Transcription Termination.
DR   Reactome; R-MMU-75953; RNA Polymerase II Transcription Initiation.
DR   Reactome; R-MMU-75955; RNA Polymerase II Transcription Elongation.
DR   Reactome; R-MMU-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR   Reactome; R-MMU-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter.
DR   Reactome; R-MMU-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter.
DR   Reactome; R-MMU-76071; RNA Polymerase III Transcription Initiation From Type 3 Promoter.
DR   Reactome; R-MMU-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR   Reactome; R-MMU-9018519; Estrogen-dependent gene expression.
DR   BioGRID-ORCS; 66491; 28 hits in 70 CRISPR screens.
DR   ChiTaRS; Polr2l; mouse.
DR   PRO; PR:P62876; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; P62876; protein.
DR   Bgee; ENSMUSG00000038489; Expressed in morula and 115 other tissues.
DR   Genevisible; P62876; MM.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005736; C:RNA polymerase I complex; IBA:GO_Central.
DR   GO; GO:0005665; C:RNA polymerase II, core complex; ISS:UniProtKB.
DR   GO; GO:0005666; C:RNA polymerase III complex; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR   GO; GO:0006360; P:transcription by RNA polymerase I; IBA:GO_Central.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0042797; P:tRNA transcription by RNA polymerase III; IBA:GO_Central.
DR   HAMAP; MF_00250; RNApol_arch_Rpo10; 1.
DR   InterPro; IPR023580; RNA_pol_su_RPB10.
DR   InterPro; IPR020789; RNA_pol_suN_Zn-BS.
DR   InterPro; IPR000268; RPABC5/Rpb10.
DR   PANTHER; PTHR23431; PTHR23431; 1.
DR   Pfam; PF01194; RNA_pol_N; 1.
DR   PIRSF; PIRSF005653; RNA_pol_N/8_sub; 1.
DR   SUPFAM; SSF46924; SSF46924; 1.
DR   PROSITE; PS01112; RNA_POL_N_8KD; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase; Metal-binding; Nucleus; Reference proteome;
KW   Transcription; Zinc.
FT   CHAIN           1..67
FT                   /note="DNA-directed RNA polymerases I, II, and III subunit
FT                   RPABC5"
FT                   /id="PRO_0000121334"
FT   BINDING         7
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         10
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         44
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         45
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   67 AA;  7645 MW;  9E8A72F667FE7EC5 CRC64;
     MIIPVRCFTC GKIVGNKWEA YLGLLQAEYT EGDALDALGL KRYCCRRMLL AHVDLIEKLL
     NYAPLEK
 
 
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