RPF1_YEAST
ID RPF1_YEAST Reviewed; 295 AA.
AC P38805; D3DL40;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Ribosome production factor 1;
DE AltName: Full=Ribosome biogenesis protein RPF1;
GN Name=RPF1; OrderedLocusNames=YHR088W;
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=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11864606; DOI=10.1016/s1097-2765(02)00438-0;
RA Wehner K.A., Baserga S.J.;
RT "The sigma(70)-like motif: a eukaryotic RNA binding domain unique to a
RT superfamily of proteins required for ribosome biogenesis.";
RL Mol. Cell 9:329-339(2002).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND POSSIBLE COMPLEX COMPOSITION.
RX PubMed=12702244; DOI=10.1111/j.1567-1364.2003.tb00136.x;
RA Bogengruber E., Briza P., Doppler E., Wimmer H., Koller L., Fasiolo F.,
RA Senger B., Hegemann J.H., Breitenbach M.;
RT "Functional analysis in yeast of the Brix protein superfamily involved in
RT the biogenesis of ribosomes.";
RL FEMS Yeast Res. 3:35-43(2003).
RN [5]
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).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Essential protein. Required for biogenesis of the 60S
CC ribosomal subunit. {ECO:0000269|PubMed:11864606,
CC ECO:0000269|PubMed:12702244}.
CC -!- SUBUNIT: Part of a complex that includes BRX1, RPF1, RPF2 and SSF1 or
CC SSF2.
CC -!- INTERACTION:
CC P38805; P10962: MAK16; NbExp=3; IntAct=EBI-24614, EBI-10937;
CC P38805; P38112: MAK5; NbExp=3; IntAct=EBI-24614, EBI-10394;
CC P38805; P39744: NOC2; NbExp=3; IntAct=EBI-24614, EBI-29259;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11864606,
CC ECO:0000269|PubMed:12702244}.
CC -!- MISCELLANEOUS: Present with 784 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U00060; AAB68926.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06784.1; -; Genomic_DNA.
DR PIR; S46718; S46718.
DR RefSeq; NP_011956.1; NM_001179218.1.
DR PDB; 5Z3G; EM; 3.65 A; O=1-295.
DR PDB; 6C0F; EM; 3.70 A; I=1-295.
DR PDB; 6CB1; EM; 4.60 A; I=1-295.
DR PDB; 6EM1; EM; 3.60 A; x=1-295.
DR PDB; 6EM3; EM; 3.20 A; x=1-295.
DR PDB; 6EM4; EM; 4.10 A; x=1-295.
DR PDB; 6EM5; EM; 4.30 A; x=1-295.
DR PDB; 7OHS; EM; 4.38 A; x=1-295.
DR PDB; 7OHW; EM; 3.50 A; x=1-295.
DR PDB; 7OHX; EM; 3.30 A; x=1-295.
DR PDBsum; 5Z3G; -.
DR PDBsum; 6C0F; -.
DR PDBsum; 6CB1; -.
DR PDBsum; 6EM1; -.
DR PDBsum; 6EM3; -.
DR PDBsum; 6EM4; -.
DR PDBsum; 6EM5; -.
DR PDBsum; 7OHS; -.
DR PDBsum; 7OHW; -.
DR PDBsum; 7OHX; -.
DR AlphaFoldDB; P38805; -.
DR SMR; P38805; -.
DR BioGRID; 36523; 331.
DR DIP; DIP-6511N; -.
DR IntAct; P38805; 33.
DR MINT; P38805; -.
DR STRING; 4932.YHR088W; -.
DR iPTMnet; P38805; -.
DR MaxQB; P38805; -.
DR PaxDb; P38805; -.
DR PRIDE; P38805; -.
DR TopDownProteomics; P38805; -.
DR EnsemblFungi; YHR088W_mRNA; YHR088W; YHR088W.
DR GeneID; 856488; -.
DR KEGG; sce:YHR088W; -.
DR SGD; S000001130; RPF1.
DR VEuPathDB; FungiDB:YHR088W; -.
DR eggNOG; KOG2780; Eukaryota.
DR GeneTree; ENSGT00940000153231; -.
DR HOGENOM; CLU_040063_1_0_1; -.
DR InParanoid; P38805; -.
DR OMA; WIISNKR; -.
DR BioCyc; YEAST:G3O-31135-MON; -.
DR PRO; PR:P38805; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38805; protein.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IDA:SGD.
DR GO; GO:0042134; F:rRNA primary transcript binding; IDA:SGD.
DR GO; GO:0000460; P:maturation of 5.8S rRNA; IBA:GO_Central.
DR GO; GO:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000470; P:maturation of LSU-rRNA; IBA:GO_Central.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000055; P:ribosomal large subunit export from nucleus; IMP:SGD.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR InterPro; IPR007109; Brix.
DR InterPro; IPR044281; IMP4/RPF1.
DR PANTHER; PTHR22734; PTHR22734; 1.
DR Pfam; PF04427; Brix; 1.
DR SMART; SM00879; Brix; 1.
DR PROSITE; PS50833; BRIX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Reference proteome; Ribosome biogenesis;
KW RNA-binding; rRNA processing; rRNA-binding.
FT CHAIN 1..295
FT /note="Ribosome production factor 1"
FT /id="PRO_0000120255"
FT DOMAIN 93..276
FT /note="Brix"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00034"
FT REGION 24..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..271
FT /note="RNA-binding"
FT HELIX 12..43
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 46..54
FT /evidence="ECO:0007829|PDB:6EM3"
FT TURN 60..63
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 79..84
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 105..117
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 133..141
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 145..167
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 205..217
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 243..249
FT /evidence="ECO:0007829|PDB:6EM3"
FT TURN 250..252
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 253..260
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 272..276
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:6EM3"
SQ SEQUENCE 295 AA; 35121 MW; EC6EDB2FCE252D4A CRC64;
MALGNEINIT NKLKRQEIFA DIKHEKNKER HTMRRKRAKE ERENPELREQ RLKENVTQTI
ENTRVYDETI NKEVEGDEDD LMRYFNSNSN EPPKIFLTTN VNAKKSAYEF ANILIEILPN
VTFVKRKFGY KLKEISDICI KRNFTDIVII NEDKKKVTGL TFIHLPEGPT FYFKLSSFVE
VKKIVGHGRP TSHIPELILN NFQTRLGQTV GRLFQSILPQ NPDIEGRQVI TLHNQRDYIF
FRRHRYVFKD NERVGLQELG PQFTLKLKRL QRGIKEETEW EHKPEMDKEK KKFYL
