ID RPC7L_HUMAN Reviewed; 218 AA. AC Q9BT43; B1MVG5; DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 27-NOV-2024, entry version 155. DE RecName: Full=DNA-directed RNA polymerase III subunit RPC7-like; DE Short=RNA polymerase III subunit C7-like; DE AltName: Full=DNA-directed RNA polymerase III subunit G-like; DE AltName: Full=RNA polymerase III 32 kDa beta subunit; DE Short=RPC32-beta {ECO:0000303|PubMed:20154270}; GN Name=POLR3GL {ECO:0000312|HGNC:HGNC:28466}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND RP DEVELOPMENTAL STAGE. RX PubMed=20154270; DOI=10.1073/pnas.0914980107; RA Haurie V., Durrieu-Gaillard S., Dumay-Odelot H., Da Silva D., Rey C., RA Prochazkova M., Roeder R.G., Besser D., Teichmann M.; RT "Two isoforms of human RNA polymerase III with specific functions in cell RT growth and transformation."; RL Proc. Natl. Acad. Sci. U.S.A. 107:4176-4181(2010). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skeletal muscle; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Eye; 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]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [5] RP INTERACTION WITH POLR3C. RX PubMed=21358628; DOI=10.1038/nsmb.1996; RA Lefevre S., Dumay-Odelot H., El-Ayoubi L., Budd A., Legrand P., Pinaud N., RA Teichmann M., Fribourg S.; RT "Structure-function analysis of hRPC62 provides insights into RNA RT polymerase III transcription initiation."; RL Nat. Struct. Mol. Biol. 18:352-358(2011). RN [6] RP IDENTIFICATION IN RNA POL III SUBCOMPLEXES, AND DEVELOPMENTAL STAGE. RX PubMed=24107381; DOI=10.1101/gr.161570.113; RA Renaud M., Praz V., Vieu E., Florens L., Washburn M.P., l'Hote P., RA Hernandez N.; RT "Gene duplication and neofunctionalization: POLR3G and POLR3GL."; RL Genome Res. 24:37-51(2014). RN [7] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=28494942; DOI=10.1016/j.stemcr.2017.04.016; RA Lund R.J., Rahkonen N., Malonzo M., Kauko L., Emani M.R., Kivinen V., RA Naervae E., Kemppainen E., Laiho A., Skottman H., Hovatta O., Rasool O., RA Nykter M., Laehdesmaeki H., Lahesmaa R.; RT "RNA polymerase III subunit POLR3G regulates specific subsets of polyA(+) RT and smallRNA transcriptomes and splicing in human pluripotent stem cells."; RL Stem Cell Reports 8:1442-1454(2017). RN [8] RP FUNCTION OF POL III, SUBUNIT, AND TISSUE SPECIFICITY. RX PubMed=35637192; DOI=10.1038/s41467-022-30323-6; RA Van Bortle K., Marciano D.P., Liu Q., Chou T., Lipchik A.M., Gollapudi S., RA Geller B.S., Monte E., Kamakaka R.T., Snyder M.P.; RT "A cancer-associated RNA polymerase III identity drives robust RT transcription and expression of snaR-A non-coding RNA."; RL Nat. Commun. 13:3007-3007(2022). RN [9] RP X-RAY CRYSTALLOGRAPHY (7.00 ANGSTROMS) OF 50-134 IN COMPLEX WITH POLR3C. RX PubMed=26394183; DOI=10.1016/j.jsb.2015.09.004; RA Boissier F., Dumay-Odelot H., Teichmann M., Fribourg S.; RT "Structural analysis of human RPC32beta-RPC62 complex."; RL J. Struct. Biol. 192:313-319(2015). RN [10] RP INVOLVEMENT IN SOFM. RX PubMed=31089205; DOI=10.1038/s41431-019-0427-0; RA Terhal P.A., Vlaar J.M., Middelkamp S., Nievelstein R.A.J., Nikkels P.G.J., RA Ross J., Creton M., Bos J.W., Voskuil-Kerkhof E.S.M., Cuppen E., Knoers N., RA van Gassen K.L.I.; RT "Biallelic variants in POLR3GL cause endosteal hyperostosis and RT oligodontia."; RL Eur. J. Hum. Genet. 28:31-39(2020). RN [11] RP INVOLVEMENT IN SOFM, VARIANT SOFM 120-ARG--TYR-218 DEL, AND RP CHARACTERIZATION OF VARIANT SOFM 120-ARG--TYR-218 DEL. RX PubMed=31695177; DOI=10.1038/s41431-019-0539-6; RA Beauregard-Lacroix E., Salian S., Kim H., Ehresmann S., D'Amours G., RA Gauthier J., Saillour V., Bernard G., Mitchell G.A., Soucy J.F., RA Michaud J.L., Campeau P.M.; RT "A variant of neonatal progeroid syndrome, or Wiedemann-Rautenstrauch RT syndrome, is associated with a nonsense variant in POLR3GL."; RL Eur. J. Hum. Genet. 28:461-468(2020). CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of CC DNA into RNA using the four ribonucleoside triphosphates as substrates. CC Specific peripheric component of RNA polymerase III which synthesizes CC small RNAs, such as 5S rRNA and tRNAs. {ECO:0000269|PubMed:20154270, CC ECO:0000269|PubMed:35637192}. CC -!- SUBUNIT: Component of the RNA polymerase III (Pol III) complex CC consisting of 17 subunits (By similarity). Pol III exists as two CC alternative complexes defined by the mutually exclusive incorporation CC of subunit POLR3G/RPC7alpha or POLR3GL/RPC7beta (PubMed:35637192). CC Found in a trimeric complex with POLR3C/RPC3 and POLR3F/RPC6 CC (PubMed:24107381). Directly interacts with POLR3C (PubMed:21358628, CC PubMed:24107381, PubMed:26394183). {ECO:0000250, CC ECO:0000269|PubMed:21358628, ECO:0000269|PubMed:24107381, CC ECO:0000269|PubMed:26394183, ECO:0000269|PubMed:35637192}. CC -!- INTERACTION: CC Q9BT43; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-2855862, EBI-10181188; CC Q9BT43; P30281: CCND3; NbExp=9; IntAct=EBI-2855862, EBI-375013; CC Q9BT43; P25800: LMO1; NbExp=3; IntAct=EBI-2855862, EBI-8639312; CC Q9BT43; Q8TC57: M1AP; NbExp=3; IntAct=EBI-2855862, EBI-748182; CC Q9BT43; P50221: MEOX1; NbExp=3; IntAct=EBI-2855862, EBI-2864512; CC Q9BT43; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-2855862, EBI-16439278; CC Q9BT43; P26367: PAX6; NbExp=3; IntAct=EBI-2855862, EBI-747278; CC Q9BT43; Q9BUI4: POLR3C; NbExp=10; IntAct=EBI-2855862, EBI-5452779; CC Q9BT43; Q9H1D9: POLR3F; NbExp=8; IntAct=EBI-2855862, EBI-710067; CC Q9BT43; Q12800: TFCP2; NbExp=3; IntAct=EBI-2855862, EBI-717422; CC Q9BT43; Q8IY57-5: YAF2; NbExp=3; IntAct=EBI-2855862, EBI-12111538; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20154270}. CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in CD4-positive T CC cells. {ECO:0000269|PubMed:20154270, ECO:0000269|PubMed:35637192}. CC -!- DEVELOPMENTAL STAGE: Up-regulated in embryonic stem cells upon retinoic CC acid-induced differentiation into embroid bodies (at protein level) CC (PubMed:28494942). No significant changes in mRNA levels between CC dividing and non-dividing cells, although levels tends to be slightly CC higher in non-dividing cells (PubMed:20154270, PubMed:24107381). CC {ECO:0000269|PubMed:20154270, ECO:0000269|PubMed:24107381, CC ECO:0000269|PubMed:28494942}. CC -!- DISEASE: Short stature, oligodontia, dysmorphic facies, and motor delay CC (SOFM) [MIM:619234]: An autosomal recessive disorder with phenotypic CC variability. The main clinical features include endosteal hyperostosis, CC short stature, oligodontia, mild facial dysmorphisms, and delayed motor CC development. Some patients show progeroid features. CC {ECO:0000269|PubMed:31089205, ECO:0000269|PubMed:31695177}. Note=The CC disease may be caused by variants affecting the gene represented in CC this entry. CC -!- SIMILARITY: Belongs to the eukaryotic RPC7 RNA polymerase subunit CC family. {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; DQ418461; ABD76394.1; -; mRNA. DR EMBL; AK056984; BAB71332.1; -; mRNA. DR EMBL; BC004355; AAH04355.1; -; mRNA. DR CCDS; CCDS72875.1; -. DR RefSeq; NP_001317614.1; NM_001330685.1. DR RefSeq; NP_115681.1; NM_032305.2. DR RefSeq; XP_005277488.1; XM_005277431.4. DR PDB; 5AFQ; X-ray; 7.00 A; D/E=50-134. DR PDBsum; 5AFQ; -. DR AlphaFoldDB; Q9BT43; -. DR SMR; Q9BT43; -. DR BioGRID; 123992; 39. DR ComplexPortal; CPX-7482; DNA-directed RNA polymerase III complex, POLR3GL variant. DR DIP; DIP-59080N; -. DR IntAct; Q9BT43; 39. DR MINT; Q9BT43; -. DR STRING; 9606.ENSP00000358320; -. DR iPTMnet; Q9BT43; -. DR PhosphoSitePlus; Q9BT43; -. DR BioMuta; POLR3GL; -. DR DMDM; 74733087; -. DR jPOST; Q9BT43; -. DR MassIVE; Q9BT43; -. DR PaxDb; 9606-ENSP00000358320; -. DR PeptideAtlas; Q9BT43; -. DR ProteomicsDB; 78950; -. DR Pumba; Q9BT43; -. DR Antibodypedia; 33956; 162 antibodies from 16 providers. DR DNASU; 84265; -. DR Ensembl; ENST00000369314.2; ENSP00000358320.1; ENSG00000121851.13. DR GeneID; 84265; -. DR KEGG; hsa:84265; -. DR MANE-Select; ENST00000369314.2; ENSP00000358320.1; NM_032305.3; NP_115681.1. DR UCSC; uc001enp.1; human. DR AGR; HGNC:28466; -. DR CTD; 84265; -. DR DisGeNET; 84265; -. DR GeneCards; POLR3GL; -. DR HGNC; HGNC:28466; POLR3GL. DR HPA; ENSG00000121851; Low tissue specificity. DR MalaCards; POLR3GL; -. DR MIM; 617457; gene. DR MIM; 619234; phenotype. DR neXtProt; NX_Q9BT43; -. DR PharmGKB; PA134921690; -. DR VEuPathDB; HostDB:ENSG00000121851; -. DR eggNOG; ENOG502QUPX; Eukaryota. DR GeneTree; ENSGT01060000248645; -. DR InParanoid; Q9BT43; -. DR OMA; KDLHAPF; -. DR OrthoDB; 3038863at2759; -. DR PhylomeDB; Q9BT43; -. DR TreeFam; TF103052; -. DR PathwayCommons; Q9BT43; -. DR Reactome; R-HSA-1834949; Cytosolic sensors of pathogen-associated DNA. DR Reactome; R-HSA-73780; RNA Polymerase III Chain Elongation. DR Reactome; R-HSA-73980; RNA Polymerase III Transcription Termination. DR Reactome; R-HSA-749476; RNA Polymerase III Abortive And Retractive Initiation. DR Reactome; R-HSA-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter. DR Reactome; R-HSA-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter. DR Reactome; R-HSA-76071; RNA Polymerase III Transcription Initiation From Type 3 Promoter. DR SignaLink; Q9BT43; -. DR BioGRID-ORCS; 84265; 14 hits in 1156 CRISPR screens. DR ChiTaRS; POLR3GL; human. DR GenomeRNAi; 84265; -. DR Pharos; Q9BT43; Tbio. DR PRO; PR:Q9BT43; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9BT43; protein. DR Bgee; ENSG00000121851; Expressed in gastrocnemius and 99 other cell types or tissues. DR ExpressionAtlas; Q9BT43; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005666; C:RNA polymerase III complex; IDA:MGI. DR GO; GO:0006383; P:transcription by RNA polymerase III; IDA:UniProtKB. DR InterPro; IPR024661; RNA_pol_III_Rpc31. DR PANTHER; PTHR15367; DNA-DIRECTED RNA POLYMERASE III; 1. DR PANTHER; PTHR15367:SF4; DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC7-LIKE; 1. DR Pfam; PF11705; RNA_pol_3_Rpc31; 1. DR PIRSF; PIRSF000777; RNA_polIII_C31; 1. PE 1: Evidence at protein level; KW 3D-structure; Disease variant; Dwarfism; Nucleus; KW Proteomics identification; Reference proteome. FT CHAIN 1..218 FT /note="DNA-directed RNA polymerase III subunit RPC7-like" FT /id="PRO_0000311590" FT REGION 133..218 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 133..158 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 159..197 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 204..218 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VARIANT 120..218 FT /note="Missing (in SOFM; uncertain significance; decrease FT in transcript levels, possibly due to nonsense-mediated FT mRNA decay)" FT /evidence="ECO:0000269|PubMed:31695177" FT /id="VAR_085496" SQ SEQUENCE 218 AA; 25334 MW; 01E3B35D7279E43E CRC64; MASRGGGRGR GRGQLTFNVE AVGIGKGDAL PPPTLQPSPL FPPLEFRPVP LPSGEEGEYV LALKQELRGA MRQLPYFIRP AVPKRDVERY SDKYQMSGPI DNAIDWNPDW RRLPRELKIR VRKLQKERIT ILLPKRPPKT TEDKEETIQK LETLEKKEEE VTSEEDEEKE EEEEKEEEEE EEYDEEEHEE ETDYIMSYFD NGEDFGGDSD DNMDEAIY //