RPAC1_MOUSE
ID RPAC1_MOUSE Reviewed; 346 AA.
AC P52432; Q3UJZ9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=DNA-directed RNA polymerases I and III subunit RPAC1;
DE Short=DNA-directed RNA polymerase I subunit C;
DE Short=RNA polymerases I and III subunit AC1;
DE AltName: Full=AC40;
DE AltName: Full=DNA-directed RNA polymerases I and III 40 kDa polypeptide;
DE Short=RPA40;
DE AltName: Full=RPC40;
GN Name=Polr1c; Synonyms=Rpo1-1;
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=7929437; DOI=10.1016/s0021-9258(18)47114-1;
RA Song C.Z., Hanada K., Yano K., Maeda Y., Yamamoto K., Muramatsu M.;
RT "High conservation of subunit composition of RNA polymerase I(A) between
RT yeast and mouse and the molecular cloning of mouse RNA polymerase I 40-kDa
RT subunit RPA40.";
RL J. Biol. Chem. 269:26976-26981(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and DBA/2J; TISSUE=Head;
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].
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 [4]
RP MUTAGENESIS OF ALA-73.
RX PubMed=9099876; DOI=10.1016/s0378-1119(96)00739-1;
RA Nishi Y., Yamamoto K., Yao Y., Yamamoto M., Nogi Y., Matsuo H.,
RA Muramatsu M.;
RT "Isolation and characterization of cDNA encoding mouse RNA polymerase II
RT subunit RPB14.";
RL Gene 187:165-170(1997).
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).
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 and III which synthesize
CC ribosomal RNA precursors and small RNAs, such as 5S rRNA and tRNAs,
CC respectively. RPAC1 is part of the Pol core element with the central
CC large cleft and probably a clamp element that moves to open and close
CC the cleft (By similarity). {ECO:0000250|UniProtKB:O15160,
CC ECO:0000250|UniProtKB:P07703}.
CC -!- SUBUNIT: Component of the RNA polymerase I (Pol I) and RNA polymerase
CC III (Pol III) complexes consisting of at least 13 and 17 subunits,
CC respectively. {ECO:0000250|UniProtKB:O15160}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O15160}.
CC -!- SIMILARITY: Belongs to the archaeal Rpo3/eukaryotic RPB3 RNA polymerase
CC subunit family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA06735.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D31966; BAA06735.1; ALT_INIT; mRNA.
DR EMBL; AK132114; BAE20986.1; -; mRNA.
DR EMBL; AK146240; BAE27005.1; -; mRNA.
DR EMBL; CH466559; EDL23483.1; -; Genomic_DNA.
DR CCDS; CCDS37632.1; -.
DR PIR; A55082; A55082.
DR RefSeq; NP_033111.2; NM_009085.2.
DR AlphaFoldDB; P52432; -.
DR SMR; P52432; -.
DR BioGRID; 202992; 14.
DR STRING; 10090.ENSMUSP00000084252; -.
DR iPTMnet; P52432; -.
DR PhosphoSitePlus; P52432; -.
DR EPD; P52432; -.
DR MaxQB; P52432; -.
DR PaxDb; P52432; -.
DR PeptideAtlas; P52432; -.
DR PRIDE; P52432; -.
DR ProteomicsDB; 260920; -.
DR Antibodypedia; 30448; 291 antibodies from 31 providers.
DR DNASU; 20016; -.
DR Ensembl; ENSMUST00000087026; ENSMUSP00000084252; ENSMUSG00000067148.
DR GeneID; 20016; -.
DR KEGG; mmu:20016; -.
DR UCSC; uc008csc.1; mouse.
DR CTD; 9533; -.
DR MGI; MGI:103288; Polr1c.
DR VEuPathDB; HostDB:ENSMUSG00000067148; -.
DR eggNOG; KOG1521; Eukaryota.
DR GeneTree; ENSGT00950000183100; -.
DR HOGENOM; CLU_038421_0_1_1; -.
DR InParanoid; P52432; -.
DR OMA; ECLRHPE; -.
DR OrthoDB; 834009at2759; -.
DR PhylomeDB; P52432; -.
DR TreeFam; TF103034; -.
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 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 BioGRID-ORCS; 20016; 29 hits in 75 CRISPR screens.
DR ChiTaRS; Polr1c; mouse.
DR PRO; PR:P52432; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P52432; protein.
DR Bgee; ENSMUSG00000067148; Expressed in metanephric ureteric bud and 257 other tissues.
DR ExpressionAtlas; P52432; baseline and differential.
DR Genevisible; P52432; MM.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005736; C:RNA polymerase I complex; IDA:MGI.
DR GO; GO:0005666; C:RNA polymerase III complex; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0001054; F:RNA polymerase I activity; IEA:InterPro.
DR GO; GO:0001056; F:RNA polymerase III activity; IEA:InterPro.
DR CDD; cd07032; RNAP_I_II_AC40; 1.
DR Gene3D; 2.170.120.12; -; 1.
DR Gene3D; 3.30.1360.10; -; 1.
DR HAMAP; MF_00320; RNApol_arch_Rpo3; 1.
DR InterPro; IPR001514; DNA-dir_RNA_pol_30-40kDasu_CS.
DR InterPro; IPR011262; DNA-dir_RNA_pol_insert.
DR InterPro; IPR011263; DNA-dir_RNA_pol_RpoA/D/Rpb3.
DR InterPro; IPR036603; RBP11-like.
DR InterPro; IPR022842; RNAP_Rpo3/Rpb3/RPAC1.
DR InterPro; IPR033901; RNAPI/III_AC40.
DR InterPro; IPR036643; RNApol_insert_sf.
DR PANTHER; PTHR11800:SF13; PTHR11800:SF13; 1.
DR Pfam; PF01000; RNA_pol_A_bac; 1.
DR Pfam; PF01193; RNA_pol_L; 1.
DR SMART; SM00662; RPOLD; 1.
DR SUPFAM; SSF55257; SSF55257; 1.
DR SUPFAM; SSF56553; SSF56553; 1.
DR PROSITE; PS00446; RNA_POL_D_30KD; 1.
PE 1: Evidence at protein level;
KW Acetylation; DNA-directed RNA polymerase; Nucleus; Reference proteome;
KW Transcription.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O15160"
FT CHAIN 2..346
FT /note="DNA-directed RNA polymerases I and III subunit
FT RPAC1"
FT /id="PRO_0000132740"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O15160"
FT MUTAGEN 73
FT /note="A->D: Unable to interact with RPB14."
FT /evidence="ECO:0000269|PubMed:9099876"
FT MUTAGEN 73
FT /note="A->R: Temperature-sensitive defect in the
FT interaction with RPB14."
FT /evidence="ECO:0000269|PubMed:9099876"
FT CONFLICT 52
FT /note="D -> G (in Ref. 1; BAA06735)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="E -> R (in Ref. 1; BAA06735)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 346 AA; 39107 MW; C2115C1526974344 CRC64;
MAAAQAVEEM RTRVVLGEFG VRNVHTTDFP GNYAGYDDAW DQNRFEKNFR VDVVQMDEDT
LEFDMVGIDA AIANAFRRIL LAEVPTMAVE KVLVYNNTSI VQDEILAHRL GLIPILADPR
LFEYRNQGEE EGTEIDTLQF RLQVRCTRNP NAAKDSSDPN ELYVNHKVYT RHMTWVPLGN
QADVFPEGTI RPVHDDILIA QLRPGQEIDL MMHCVKGIGK DHAKFSPVAT ASYRLLPAIT
LLEPVEGEAA EELSQCFSPG VIEVEEVQGK KVARVANARL DTFSREIFRH EKLKKAVRLA
RVRDHYIFSV ESTGVLPPDV LVSEAIKILM GKCRRFLDEL DAVEMD
