ID RRN11_YEAST Reviewed; 507 AA. AC Q04712; D6VZD2; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 27-MAR-2024, entry version 160. DE RecName: Full=RNA polymerase I-specific transcription initiation factor RRN11; GN Name=RRN11; OrderedLocusNames=YML043C; ORFNames=YM9827.09C; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169872; RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."; RL Nature 387:90-93(1997). RN [2] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., RA LaBaer J.; RT "Approaching a complete repository of sequence-verified protein-encoding RT clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [4] RP IDENTIFICATION IN THE CF COMPLEX. RX PubMed=7958901; DOI=10.1101/gad.8.19.2349; RA Keys D.A., Vu L., Steffan J.S., Dodd J.A., Yamamoto R.T., Nogi Y., RA Nomura M.; RT "RRN6 and RRN7 encode subunits of a multiprotein complex essential for the RT initiation of rDNA transcription by RNA polymerase I in Saccharomyces RT cerevisiae."; RL Genes Dev. 8:2349-2362(1994). RN [5] RP IDENTIFICATION IN THE CF COMPLEX, AND INTERACTION WITH RRN6; RRN7 AND RP SPT15. RX PubMed=8702872; DOI=10.1074/jbc.271.35.21062; RA Lalo D., Steffan J.S., Dodd J.A., Nomura M.; RT "RRN11 encodes the third subunit of the complex containing Rrn6p and Rrn7p RT that is essential for the initiation of rDNA transcription by yeast RNA RT polymerase I."; RL J. Biol. Chem. 271:21062-21067(1996). RN [6] RP FUNCTION OF THE CF COMPLEX. RX PubMed=8887672; DOI=10.1128/mcb.16.11.6436; RA Lin C.W., Moorefield B., Payne J., Aprikian P., Mitomo K., Reeder R.H.; RT "A novel 66-kilodalton protein complexes with Rrn6, Rrn7, and TATA-binding RT protein to promote polymerase I transcription initiation in Saccharomyces RT cerevisiae."; RL Mol. Cell. Biol. 16:6436-6443(1996). RN [7] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=14562095; DOI=10.1038/nature02026; RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., RA Weissman J.S., O'Shea E.K.; RT "Global analysis of protein localization in budding yeast."; RL Nature 425:686-691(2003). RN [8] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). CC -!- FUNCTION: Acts as a component of the core factor (CF) complex which is CC essential for the initiation of rDNA transcription by RNA polymerase I. CC After binding of UAF (upstream activation factor) to an upstream CC element of the promoter, CF is recruited in a SPT15/TBP-dependent CC manner to form a preinitiation complex. {ECO:0000269|PubMed:8887672}. CC -!- SUBUNIT: Component of the core factor (CF) complex, which consists of CC RRN6, RRN7 and RRN11. The CF heterotrimer may further dimerize to form CC a hexamer. RRN11 interacts with RRN6, RRN7 and SPT15. CC {ECO:0000269|PubMed:7958901, ECO:0000269|PubMed:8702872}. CC -!- INTERACTION: CC Q04712; P32786: RRN6; NbExp=2; IntAct=EBI-27790, EBI-15986; CC Q04712; P40992: RRN7; NbExp=2; IntAct=EBI-27790, EBI-15990; CC Q04712; P13393: SPT15; NbExp=2; IntAct=EBI-27790, EBI-19129; CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14562095}. CC -!- MISCELLANEOUS: Present with 476 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. 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; Z47816; CAA87831.1; -; Genomic_DNA. DR EMBL; AY692808; AAT92827.1; -; Genomic_DNA. DR EMBL; BK006946; DAA09856.1; -; Genomic_DNA. DR PIR; S50949; S50949. DR RefSeq; NP_013669.1; NM_001182401.1. DR PDB; 5N5Y; EM; 7.70 A; R=1-507. DR PDB; 5N5Z; EM; 7.70 A; R=1-507. DR PDB; 5N60; EM; 7.70 A; R=1-507. DR PDB; 5N61; EM; 3.40 A; R=1-507. DR PDB; 5O7X; X-ray; 3.20 A; C/F/I/L/O/R=1-507. DR PDB; 5OA1; EM; 4.40 A; W=1-507. DR PDB; 5W5Y; EM; 3.80 A; Q=1-507. DR PDB; 5W64; EM; 4.20 A; Q=1-507. DR PDB; 5W65; EM; 4.30 A; Q=1-507. DR PDB; 5W66; EM; 3.90 A; Q=1-507. DR PDB; 6RQH; EM; 3.70 A; R=1-507. DR PDB; 6RQL; EM; 2.90 A; R=1-507. DR PDB; 6RRD; EM; 3.10 A; R=1-507. DR PDB; 6RUI; EM; 2.70 A; R=1-507. DR PDB; 6RUO; EM; 3.50 A; R=1-507. DR PDB; 6RWE; EM; 3.00 A; R=1-507. DR PDB; 6TPS; EM; 3.54 A; R=1-507. DR PDBsum; 5N5Y; -. DR PDBsum; 5N5Z; -. DR PDBsum; 5N60; -. DR PDBsum; 5N61; -. DR PDBsum; 5O7X; -. DR PDBsum; 5OA1; -. DR PDBsum; 5W5Y; -. DR PDBsum; 5W64; -. DR PDBsum; 5W65; -. DR PDBsum; 5W66; -. DR PDBsum; 6RQH; -. DR PDBsum; 6RQL; -. DR PDBsum; 6RRD; -. DR PDBsum; 6RUI; -. DR PDBsum; 6RUO; -. DR PDBsum; 6RWE; -. DR PDBsum; 6TPS; -. DR AlphaFoldDB; Q04712; -. DR EMDB; EMD-10006; -. DR EMDB; EMD-10007; -. DR EMDB; EMD-10038; -. DR EMDB; EMD-10544; -. DR EMDB; EMD-3590; -. DR EMDB; EMD-3591; -. DR EMDB; EMD-3592; -. DR EMDB; EMD-3593; -. DR EMDB; EMD-3727; -. DR EMDB; EMD-4982; -. DR EMDB; EMD-4984; -. DR EMDB; EMD-4987; -. DR EMDB; EMD-8771; -. DR EMDB; EMD-8772; -. DR EMDB; EMD-8774; -. DR EMDB; EMD-8775; -. DR EMDB; EMD-8776; -. DR EMDB; EMD-8777; -. DR SMR; Q04712; -. DR BioGRID; 35126; 80. DR ComplexPortal; CPX-1836; RNA polymerase I core factor complex. DR DIP; DIP-4542N; -. DR IntAct; Q04712; 9. DR MINT; Q04712; -. DR STRING; 4932.YML043C; -. DR iPTMnet; Q04712; -. DR PaxDb; 4932-YML043C; -. DR PeptideAtlas; Q04712; -. DR EnsemblFungi; YML043C_mRNA; YML043C; YML043C. DR GeneID; 854964; -. DR KEGG; sce:YML043C; -. DR AGR; SGD:S000004507; -. DR SGD; S000004507; RRN11. DR VEuPathDB; FungiDB:YML043C; -. DR eggNOG; ENOG502R1IK; Eukaryota. DR HOGENOM; CLU_034126_0_0_1; -. DR InParanoid; Q04712; -. DR OMA; EVWFIYA; -. DR OrthoDB; 1974231at2759; -. DR BioCyc; YEAST:G3O-32641-MONOMER; -. DR BioGRID-ORCS; 854964; 0 hits in 10 CRISPR screens. DR PRO; PR:Q04712; -. DR Proteomes; UP000002311; Chromosome XIII. DR RNAct; Q04712; Protein. DR GO; GO:0005730; C:nucleolus; IDA:SGD. DR GO; GO:0005634; C:nucleus; NAS:ComplexPortal. DR GO; GO:0070860; C:RNA polymerase I core factor complex; IDA:SGD. DR GO; GO:0001164; F:RNA polymerase I core promoter sequence-specific DNA binding; IDA:SGD. DR GO; GO:0001181; F:RNA polymerase I general transcription initiation factor activity; IEA:InterPro. DR GO; GO:0017025; F:TBP-class protein binding; IDA:SGD. DR GO; GO:0042790; P:nucleolar large rRNA transcription by RNA polymerase I; IDA:SGD. DR InterPro; IPR007224; TIF_Rrn11. DR InterPro; IPR016850; TIF_Rrn11_budding_yeast. DR PANTHER; PTHR28244; RNA POLYMERASE I-SPECIFIC TRANSCRIPTION INITIATION FACTOR RRN11; 1. DR PANTHER; PTHR28244:SF1; RNA POLYMERASE I-SPECIFIC TRANSCRIPTION INITIATION FACTOR RRN11; 1. DR Pfam; PF04090; Rrn11; 1. DR PIRSF; PIRSF027133; Rrn11; 1. PE 1: Evidence at protein level; KW 3D-structure; Nucleus; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1..507 FT /note="RNA polymerase I-specific transcription initiation FT factor RRN11" FT /id="PRO_0000203257" FT REGION 37..76 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 89..124 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT HELIX 11..37 FT /evidence="ECO:0007829|PDB:6RUI" FT HELIX 75..83 FT /evidence="ECO:0007829|PDB:5O7X" FT HELIX 127..130 FT /evidence="ECO:0007829|PDB:6RUI" FT STRAND 135..139 FT /evidence="ECO:0007829|PDB:6RUI" FT STRAND 145..147 FT /evidence="ECO:0007829|PDB:6RUI" FT HELIX 159..165 FT /evidence="ECO:0007829|PDB:6RUI" FT HELIX 167..173 FT /evidence="ECO:0007829|PDB:6RUI" FT HELIX 176..179 FT /evidence="ECO:0007829|PDB:6RUI" FT HELIX 182..191 FT /evidence="ECO:0007829|PDB:6RUI" FT STRAND 196..199 FT /evidence="ECO:0007829|PDB:6RWE" FT TURN 201..203 FT /evidence="ECO:0007829|PDB:6RUI" FT HELIX 210..225 FT /evidence="ECO:0007829|PDB:6RUI" FT HELIX 229..239 FT /evidence="ECO:0007829|PDB:6RUI" FT HELIX 247..252 FT /evidence="ECO:0007829|PDB:6RUI" FT HELIX 255..258 FT /evidence="ECO:0007829|PDB:6RUI" FT STRAND 262..265 FT /evidence="ECO:0007829|PDB:5O7X" FT HELIX 268..277 FT /evidence="ECO:0007829|PDB:6RUI" FT STRAND 278..280 FT /evidence="ECO:0007829|PDB:5O7X" FT HELIX 295..298 FT /evidence="ECO:0007829|PDB:6RUI" FT STRAND 301..303 FT /evidence="ECO:0007829|PDB:5O7X" FT HELIX 307..321 FT /evidence="ECO:0007829|PDB:6RUI" FT HELIX 346..354 FT /evidence="ECO:0007829|PDB:6RUI" FT HELIX 363..378 FT /evidence="ECO:0007829|PDB:6RUI" FT TURN 379..383 FT /evidence="ECO:0007829|PDB:6RUO" FT HELIX 398..420 FT /evidence="ECO:0007829|PDB:6RUI" FT STRAND 421..423 FT /evidence="ECO:0007829|PDB:6RUI" FT HELIX 428..440 FT /evidence="ECO:0007829|PDB:6RUI" SQ SEQUENCE 507 AA; 59254 MW; 726B0963F0E79783 CRC64; MFEVPITLTN RKFAQRRKLK YQYINYISRR FDRISKKSTT TDSLPTPENS AAENNDEEEG QNSEAGTYRR SVLQQKKRRR ERHWRSVVGE IYSTTESETD SQEEETEEGG EHDTGIDKED SDEERKFWKK YEKPEKSFEI WRTVSSQNKQ PINKQKMTYH NFKKIEKIPL RKMEIPLLHC TKENKLYFQS ISRGLEPLKT STSEVRNYRT RHIVTLTDLL HLNVSRHNWS LAYKIFATLI RIPGVQIKSL WGIGVEILDN LSNSSSGLDF LQWMCQIYSS KSRFVQNINY RSIVPPFQTG SRTHTAKFAI TYLWSSLINC QKSMEPSSNI IDKPFDTEND LLQELIDKIS EWVLTPPFME DAEVWFIYAS CHLLKADTLS RQFVNDNKNN DLIGLDRDIK INQVIKHIHY VRTFLKICLD KGGFAVPSRL IENQLKSFES RLYGEAQDIQ ERDVANVYDS IDNSSVENSF GDVYETNAEF LDTQLMDLSP EDNGLDEMHY SDEDSSE //