RRN11_YEAST
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 03-AUG-2022, entry version 153.
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 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}.
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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 SMR; Q04712; -.
DR BioGRID; 35126; 78.
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; Q04712; -.
DR PRIDE; Q04712; -.
DR EnsemblFungi; YML043C_mRNA; YML043C; YML043C.
DR GeneID; 854964; -.
DR KEGG; sce:YML043C; -.
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 BioCyc; YEAST:G3O-32641-MON; -.
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; IC: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 Pfam; PF04090; RNA_pol_I_TF; 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
