RPA34_MOUSE
ID RPA34_MOUSE Reviewed; 399 AA.
AC Q76KJ5; Q8K0Y9;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=DNA-directed RNA polymerase I subunit RPA34 {ECO:0000305};
DE AltName: Full=A34.5;
DE AltName: Full=DNA-directed RNA polymerase I subunit G {ECO:0000250|UniProtKB:O15446};
DE AltName: Full=RNA polymerase I-associated factor PAF49 {ECO:0000303|PubMed:15226435};
GN Name=Polr1g {ECO:0000250|UniProtKB:O15446};
GN Synonyms=Ase1, Cd3eap {ECO:0000312|MGI:MGI:1917583},
GN Paf49 {ECO:0000303|PubMed:15226435};
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], PROTEIN SEQUENCE OF 182-196; 218-226 AND
RP 251-261, IDENTIFICATION IN THE RNA POL I COMPLEX, FUNCTION, INTERACTION
RP WITH SL1 COMPLEX AND POLR1E, AND SUBCELLULAR LOCATION.
RC TISSUE=Ascitic tumor;
RX PubMed=15226435; DOI=10.1128/mcb.24.14.6338-6349.2004;
RA Yamamoto K., Yamamoto M., Hanada K., Nogi Y., Matsuyama T., Muramatsu M.;
RT "Multiple protein-protein interactions by RNA polymerase I-associated
RT factor PAF49 and role of PAF49 in rRNA transcription.";
RL Mol. Cell. Biol. 24:6338-6349(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon, and Mammary tumor;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas, 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 Component of RNA polymerase I which synthesizes ribosomal RNA
CC precursors. Involved in UBTF-activated transcription, presumably at a
CC step following PIC formation. {ECO:0000269|PubMed:15226435}.
CC -!- SUBUNIT: Component of the RNA polymerase I (Pol I) complex consisting
CC of at least 13 subunits. Interacts with TAF1A thereby associates with
CC the SL1 complex. Interacts with UBTF (By similarity). Interacts with
CC POLR1E/PRAF1 through its N-terminal region. {ECO:0000250,
CC ECO:0000269|PubMed:15226435}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:15226435}.
CC Note=Accumulates in the nucleolus of exponentially growing cells.
CC -!- MISCELLANEOUS: It is in an antisense orientation to and overlaps the
CC gene of the DNA repair enzyme ERCC1. This gene overlap is conserved in
CC human, suggesting an important biological function.
CC -!- SIMILARITY: Belongs to the eukaryotic RPA34 RNA polymerase subunit
CC family. {ECO:0000305}.
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DR EMBL; AB091121; BAD02839.1; -; mRNA.
DR EMBL; BC029206; AAH29206.1; -; mRNA.
DR EMBL; BC071199; AAH71199.1; -; mRNA.
DR CCDS; CCDS39798.1; -.
DR RefSeq; NP_665821.1; NM_145822.2.
DR AlphaFoldDB; Q76KJ5; -.
DR SMR; Q76KJ5; -.
DR BioGRID; 213987; 2.
DR STRING; 10090.ENSMUSP00000044653; -.
DR iPTMnet; Q76KJ5; -.
DR PhosphoSitePlus; Q76KJ5; -.
DR EPD; Q76KJ5; -.
DR jPOST; Q76KJ5; -.
DR MaxQB; Q76KJ5; -.
DR PaxDb; Q76KJ5; -.
DR PeptideAtlas; Q76KJ5; -.
DR PRIDE; Q76KJ5; -.
DR ProteomicsDB; 300434; -.
DR Antibodypedia; 17932; 307 antibodies from 28 providers.
DR DNASU; 70333; -.
DR Ensembl; ENSMUST00000047036; ENSMUSP00000044653; ENSMUSG00000047649.
DR GeneID; 70333; -.
DR KEGG; mmu:70333; -.
DR UCSC; uc009fln.2; mouse.
DR CTD; 70333; -.
DR MGI; MGI:1917583; Cd3eap.
DR VEuPathDB; HostDB:ENSMUSG00000047649; -.
DR eggNOG; ENOG502S2W3; Eukaryota.
DR GeneTree; ENSGT00450000040362; -.
DR HOGENOM; CLU_035235_0_0_1; -.
DR InParanoid; Q76KJ5; -.
DR OMA; QVMMEPG; -.
DR OrthoDB; 984661at2759; -.
DR PhylomeDB; Q76KJ5; -.
DR TreeFam; TF338162; -.
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; 70333; 28 hits in 75 CRISPR screens.
DR ChiTaRS; Cd3eap; mouse.
DR PRO; PR:Q76KJ5; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q76KJ5; protein.
DR Bgee; ENSMUSG00000047649; Expressed in ear vesicle and 216 other tissues.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005736; C:RNA polymerase I complex; IDA:MGI.
DR GO; GO:0009303; P:rRNA transcription; IDA:MGI.
DR GO; GO:0006360; P:transcription by RNA polymerase I; IEA:InterPro.
DR InterPro; IPR013240; DNA-dir_RNA_pol1_su_RPA34.
DR PANTHER; PTHR15484; PTHR15484; 1.
DR Pfam; PF08208; RNA_polI_A34; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..399
FT /note="DNA-directed RNA polymerase I subunit RPA34"
FT /id="PRO_0000228121"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O15446"
FT MOD_RES 80
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O15446"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15446"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15446"
FT MOD_RES 277
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O15446"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15446"
FT CONFLICT 90
FT /note="R -> G (in Ref. 1; BAD02839)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="F -> L (in Ref. 1; BAD02839)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="Missing (in Ref. 1; BAD02839)"
FT /evidence="ECO:0000305"
FT CONFLICT 394..399
FT /note="ERGARL -> RERRTPLIPALGRQRQADF (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 399 AA; 43082 MW; E7CE66D5FFE93EC0 CRC64;
MAGTQACSAT RFSCPPHFTE MSPDSEPSRF SLEALTGPDT ELWLIQAPAD FAPQCLNGRR
VPLSGSKTVK GKLDGKKHRY RVFTSSPQAR EATLLASSSE AGGRLTCAPA PSGSLRIMEG
PQEYLLSRVP LQLIPTSLPP QIPAGLRPRF SAFGGSPPVT GPGSASALRS PTSGKRKSTR
KGTDASSDTQ EAVNRHGAME VKTALGNLGV SVKKRKRYFM QEEMEAKTME PVAELPVPSA
TSSKKRKKSK GTETSQVEHT EPVAQTEPPE GTFLFPTKKR KRQKEADGTE EVDGIVADSQ
PQVIVEAQEE TILLSPTKKR RKEKRQNLGM EAEMGPPGVL MVTEHSEHGL QAEVALVSPK
KTKKKKGKRV GETEAALPDD FEPQGALAPS KKKERGARL
