RPA12_MOUSE
ID RPA12_MOUSE Reviewed; 123 AA.
AC Q791N7;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=DNA-directed RNA polymerase I subunit RPA12 {ECO:0000305|Ref.1};
DE AltName: Full=DNA-directed RNA polymerase I subunit H {ECO:0000250|UniProtKB:Q9P1U0};
DE AltName: Full=Zinc ribbon domain-containing protein 1 {ECO:0000312|MGI:MGI:1913386};
GN Name=Polr1h {ECO:0000250|UniProtKB:Q9P1U0};
GN Synonyms=Rpa12 {ECO:0000303|Ref.1}, Znrd1 {ECO:0000312|MGI:MGI:1913386};
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 [GENOMIC DNA / MRNA].
RA Shematorova E.K., Lebedenko E.N., Shpakovski G.V.;
RT "Complementation studies of Rpa12, small specific subunit of nuclear RNA
RT polymerase I.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Component of RNA polymerase I which synthesizes ribosomal RNA
CC precursors.
CC -!- SUBUNIT: Component of the RNA polymerase I (Pol I) complex consisting
CC of at least 13 subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P32529}.
CC -!- SIMILARITY: Belongs to the archaeal RpoM/eukaryotic RPA12/RPB9/RPC11
CC RNA polymerase family. {ECO:0000305}.
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DR EMBL; AF230339; AAG50161.1; -; mRNA.
DR EMBL; AF230340; AAG50162.1; -; Genomic_DNA.
DR EMBL; AK003714; BAB22954.1; -; mRNA.
DR EMBL; BC043016; AAH43016.1; -; mRNA.
DR EMBL; AK005976; BAB24350.1; -; mRNA.
DR CCDS; CCDS28730.1; -.
DR RefSeq; NP_075651.1; NM_023162.4.
DR RefSeq; XP_006524855.1; XM_006524792.1.
DR AlphaFoldDB; Q791N7; -.
DR SMR; Q791N7; -.
DR BioGRID; 211240; 1.
DR STRING; 10090.ENSMUSP00000109299; -.
DR EPD; Q791N7; -.
DR MaxQB; Q791N7; -.
DR PaxDb; Q791N7; -.
DR PeptideAtlas; Q791N7; -.
DR PRIDE; Q791N7; -.
DR ProteomicsDB; 300511; -.
DR Antibodypedia; 26188; 155 antibodies from 21 providers.
DR DNASU; 66136; -.
DR Ensembl; ENSMUST00000113669; ENSMUSP00000109299; ENSMUSG00000036315.
DR Ensembl; ENSMUST00000172518; ENSMUSP00000133651; ENSMUSG00000036315.
DR GeneID; 66136; -.
DR KEGG; mmu:66136; -.
DR UCSC; uc008clo.1; mouse.
DR CTD; 30834; -.
DR MGI; MGI:1913386; Polr1h.
DR VEuPathDB; HostDB:ENSMUSG00000036315; -.
DR eggNOG; KOG2907; Eukaryota.
DR GeneTree; ENSGT00390000008126; -.
DR HOGENOM; CLU_093932_1_2_1; -.
DR InParanoid; Q791N7; -.
DR OMA; EMQYHTL; -.
DR OrthoDB; 1456544at2759; -.
DR PhylomeDB; Q791N7; -.
DR TreeFam; TF313881; -.
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; 66136; 24 hits in 76 CRISPR screens.
DR ChiTaRS; Znrd1; mouse.
DR PRO; PR:Q791N7; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q791N7; protein.
DR Bgee; ENSMUSG00000036315; Expressed in primitive streak and 265 other tissues.
DR ExpressionAtlas; Q791N7; baseline and differential.
DR Genevisible; Q791N7; MM.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005736; C:RNA polymerase I complex; IBA:GO_Central.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006379; P:mRNA cleavage; IEA:InterPro.
DR GO; GO:0006363; P:termination of RNA polymerase I transcription; IBA:GO_Central.
DR CDD; cd10507; Zn-ribbon_RPA12; 1.
DR InterPro; IPR019761; DNA-dir_RNA_pol-M_15_CS.
DR InterPro; IPR012164; Rpa12/Rpb9/Rpc10/TFS.
DR InterPro; IPR034004; Zn_ribbon_RPA12_C.
DR InterPro; IPR001222; Znf_TFIIS.
DR PANTHER; PTHR11239; PTHR11239; 1.
DR Pfam; PF01096; TFIIS_C; 1.
DR PIRSF; PIRSF005586; RNApol_RpoM; 1.
DR SMART; SM00440; ZnF_C2C2; 1.
DR PROSITE; PS01030; RNA_POL_M_15KD; 1.
DR PROSITE; PS00466; ZF_TFIIS_1; 1.
DR PROSITE; PS51133; ZF_TFIIS_2; 1.
PE 1: Evidence at protein level;
KW DNA-directed RNA polymerase; Metal-binding; Nucleus; Reference proteome;
KW Transcription; Zinc; Zinc-finger.
FT CHAIN 1..123
FT /note="DNA-directed RNA polymerase I subunit RPA12"
FT /id="PRO_0000121462"
FT ZN_FING 17..38
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT ZN_FING 80..120
FT /note="TFIIS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
SQ SEQUENCE 123 AA; 13650 MW; 23F3407757502D61 CRC64;
MELARPRSNF QSDLDFCPDC GSVLPLPGIQ DTVICSRCGF SIDVRDCEGK VVKTSVVFNK
LGATIPLSVD EGPELQGPVI DRRCPRCGHE GMAYHTRQMR SADEGQTVFY TCINCKFQEK
EDS
