IPI1_YEAST
ID IPI1_YEAST Reviewed; 334 AA.
AC P38803; D3DL36;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Pre-rRNA-processing protein IPI1;
DE AltName: Full=Involved in processing IST2 protein 1;
GN Name=IPI1; OrderedLocusNames=YHR085W;
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 IDENTIFICATION IN THE RIX1 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [4]
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 [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 IN THE RIX1 COMPLEX, SUBCELLULAR LOCATION, FUNCTION OF THE
RP RIX1 COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15528184; DOI=10.1074/jbc.m406876200;
RA Galani K., Nissan T.A., Petfalski E., Tollervey D., Hurt E.;
RT "Rea1, a dynein-related nuclear AAA-ATPase, is involved in late rRNA
RT processing and nuclear export of 60 S subunits.";
RL J. Biol. Chem. 279:55411-55418(2004).
RN [7]
RP IDENTIFICATION IN THE RIX1 COMPLEX, AND FUNCTION OF THE RIX1 COMPLEX.
RX PubMed=14759368; DOI=10.1016/s1097-2765(04)00003-6;
RA Krogan N.J., Peng W.-T., Cagney G., Robinson M.D., Haw R., Zhong G.,
RA Guo X., Zhang X., Canadien V., Richards D.P., Beattie B.K., Lalev A.,
RA Zhang W., Davierwala A.P., Mnaimneh S., Starostine A., Tikuisis A.P.,
RA Grigull J., Datta N., Bray J.E., Hughes T.R., Emili A., Greenblatt J.F.;
RT "High-definition macromolecular composition of yeast RNA-processing
RT complexes.";
RL Mol. Cell 13:225-239(2004).
RN [8]
RP IDENTIFICATION IN THE RIX1 COMPLEX, INTERACTION WITH MDN1 AND PRE-60S
RP RIBOSOMAL PARTICLES, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15260980; DOI=10.1016/j.molcel.2004.06.033;
RA Nissan T.A., Galani K., Maco B., Tollervey D., Aebi U., Hurt E.;
RT "A pre-ribosome with a tadpole-like structure functions in ATP-dependent
RT maturation of 60S subunits.";
RL Mol. Cell 15:295-301(2004).
RN [9]
RP IDENTIFICATION IN THE RIX1 COMPLEX.
RX PubMed=26619264; DOI=10.1038/nsmb.3132;
RA Barrio-Garcia C., Thoms M., Flemming D., Kater L., Berninghausen O.,
RA Bassler J., Beckmann R., Hurt E.;
RT "Architecture of the Rix1-Rea1 checkpoint machinery during pre-60S-ribosome
RT remodeling.";
RL Nat. Struct. Mol. Biol. 23:37-44(2016).
CC -!- FUNCTION: Component of the RIX1 complex required for processing of ITS2
CC sequences from 35S pre-rRNA. {ECO:0000269|PubMed:14759368,
CC ECO:0000269|PubMed:15528184}.
CC -!- SUBUNIT: Component of the RIX1 complex, composed of IPI1, RIX1/IPI2 and
CC IPI3 in a 1:2:2 stoichiometry. The complex interacts (via RIX1) with
CC MDN1 (via its hexameric AAA ATPase ring) and the pre-60S ribosome
CC particles. {ECO:0000269|PubMed:14690591, ECO:0000269|PubMed:14759368,
CC ECO:0000269|PubMed:15260980, ECO:0000269|PubMed:15528184}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:15528184}.
CC -!- MISCELLANEOUS: Present with 4420 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the IPI1/TEX10 family. {ECO:0000305}.
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DR EMBL; U10556; AAB68883.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06780.1; -; Genomic_DNA.
DR PIR; S46805; S46805.
DR RefSeq; NP_011953.1; NM_001179215.1.
DR PDB; 6YLE; EM; 3.30 A; K=1-334.
DR PDBsum; 6YLE; -.
DR AlphaFoldDB; P38803; -.
DR SMR; P38803; -.
DR BioGRID; 36520; 244.
DR ComplexPortal; CPX-1711; RIX1 complex.
DR DIP; DIP-4665N; -.
DR IntAct; P38803; 28.
DR MINT; P38803; -.
DR STRING; 4932.YHR085W; -.
DR iPTMnet; P38803; -.
DR MaxQB; P38803; -.
DR PaxDb; P38803; -.
DR PRIDE; P38803; -.
DR EnsemblFungi; YHR085W_mRNA; YHR085W; YHR085W.
DR GeneID; 856485; -.
DR KEGG; sce:YHR085W; -.
DR SGD; S000001127; IPI1.
DR VEuPathDB; FungiDB:YHR085W; -.
DR eggNOG; KOG2149; Eukaryota.
DR GeneTree; ENSGT00950000182992; -.
DR HOGENOM; CLU_050252_2_0_1; -.
DR InParanoid; P38803; -.
DR OMA; CAGGWVK; -.
DR BioCyc; YEAST:G3O-31132-MON; -.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:P38803; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38803; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005654; C:nucleoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0097344; C:Rix1 complex; IDA:SGD.
DR GO; GO:0003682; F:chromatin binding; IDA:SGD.
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:0006267; P:pre-replicative complex assembly involved in nuclear cell cycle DNA replication; IMP:SGD.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IMP:SGD.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IMP:SGD.
DR GO; GO:0006364; P:rRNA processing; IMP:SGD.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR024679; Ipi1_N.
DR InterPro; IPR037947; TEX10/Ipi1.
DR PANTHER; PTHR16056:SF2; PTHR16056:SF2; 1.
DR Pfam; PF12333; Ipi1_N; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Reference proteome; Ribosome biogenesis;
KW rRNA processing.
FT CHAIN 1..334
FT /note="Pre-rRNA-processing protein IPI1"
FT /id="PRO_0000202904"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:6YLE"
SQ SEQUENCE 334 AA; 37867 MW; 1AB0B318BBFC8096 CRC64;
MTKSRKQKQK KQDFLRKKLK VGKPKEKARN ATDTSFVSKT ISIRNQHLDQ NPHDLTKRLT
LLKHHNINVR KETLTTFQKS IPSIIKSRLM TPLLTQSIPL ICDESQQVRQ GLIDLVDEIG
SHDAEILKLH CNIFVLYINM AMTHIVTQIQ ADSTKFLSHL LKYCGDEVVR KSWVKLLNGV
FGVLGWGQVG KNDSASIVQT KKRNAKYVTI HLNALYTLVE YGCQDERARS DGDTAETTED
SGTLRNPYLI PDYPQPFEHL KLFTRELKVQ DATSSGVNAT LLSLATQDID TRKAVFIEQF
LPIVRKKIEV IIKEGGECGK SANKLKTLLA KIFD
