IMP3_YEAST
ID IMP3_YEAST Reviewed; 183 AA.
AC P32899; D3DL97;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=U3 small nucleolar ribonucleoprotein protein IMP3;
DE Short=U3 snoRNP protein IMP3;
DE AltName: Full=Interacting with MPP10 protein 3;
GN Name=IMP3; OrderedLocusNames=YHR148W;
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 [GENOMIC DNA].
RX PubMed=8358820; DOI=10.1007/bf00324677;
RA Schwank S., Harrer R., Schueller H.-J., Schweizer E.;
RT "Molecular cloning and analysis of the nuclear gene MRP-L6 coding for a
RT putative mitochondrial ribosomal protein from Saccharomyces cerevisiae.";
RL Curr. Genet. 24:136-140(1993).
RN [2]
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 [3]
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 [4]
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 [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10409734; DOI=10.1128/mcb.19.8.5441;
RA Lee S.J., Baserga S.J.;
RT "Imp3p and Imp4p, two specific components of the U3 small nucleolar
RT ribonucleoprotein that are essential for pre-18S rRNA processing.";
RL Mol. Cell. Biol. 19:5441-5452(1999).
RN [6]
RP IDENTIFICATION IN SSU PROCESSOME BY MASS SPECTROMETRY.
RX PubMed=12068309; DOI=10.1038/nature00769;
RA Dragon F., Gallagher J.E.G., Compagnone-Post P.A., Mitchell B.M.,
RA Porwancher K.A., Wehner K.A., Wormsley S., Settlage R.E., Shabanowitz J.,
RA Osheim Y., Beyer A.L., Hunt D.F., Baserga S.J.;
RT "A large nucleolar U3 ribonucleoprotein required for 18S ribosomal RNA
RT biogenesis.";
RL Nature 417:967-970(2002).
RN [7]
RP FUNCTION, AND INTERACTION WITH MPP10.
RX PubMed=15489263; DOI=10.1073/pnas.0406819101;
RA Gerczei T., Correll C.C.;
RT "Imp3p and Imp4p mediate formation of essential U3-precursor rRNA (pre-
RT rRNA) duplexes, possibly to recruit the small subunit processome to the
RT pre-rRNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15301-15306(2004).
CC -!- FUNCTION: Required for the early cleavages at sites A0, A1 and A2
CC during 18S ribosomal pre-RNA processing. {ECO:0000269|PubMed:10409734,
CC ECO:0000269|PubMed:15489263}.
CC -!- SUBUNIT: Component of a heterotrimeric complex containing IMP3, IMP4
CC and MPP10. Interacts with MPP10. Component of the ribosomal small
CC subunit (SSU) processome composed of at least 40 protein subunits and
CC snoRNA U3. {ECO:0000269|PubMed:12068309, ECO:0000269|PubMed:15489263}.
CC -!- INTERACTION:
CC P32899; P38333: ENP1; NbExp=4; IntAct=EBI-9237, EBI-6482;
CC P32899; P47083: MPP10; NbExp=7; IntAct=EBI-9237, EBI-11168;
CC P32899; Q12136: SAS10; NbExp=2; IntAct=EBI-9237, EBI-36084;
CC P32899; P53866: SQS1; NbExp=2; IntAct=EBI-9237, EBI-29168;
CC P32899; P40362: UTP18; NbExp=2; IntAct=EBI-9237, EBI-4534;
CC P32899; Q04177: UTP5; NbExp=2; IntAct=EBI-9237, EBI-35844;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:10409734}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS4 family.
CC {ECO:0000305}.
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DR EMBL; X69480; CAA49237.1; -; Genomic_DNA.
DR EMBL; U10397; AAB68981.1; -; Genomic_DNA.
DR EMBL; AY558388; AAS56714.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06841.1; -; Genomic_DNA.
DR PIR; S33911; S33911.
DR RefSeq; NP_012018.1; NM_001179279.1.
DR PDB; 5WLC; EM; 3.80 A; LZ=1-183.
DR PDB; 5WXM; X-ray; 2.30 A; A/B=26-183.
DR PDB; 5WYJ; EM; 8.70 A; MA=1-183.
DR PDB; 5WYK; EM; 4.50 A; MA=1-183.
DR PDB; 6KE6; EM; 3.40 A; 5F=1-183.
DR PDB; 6LQP; EM; 3.20 A; 5F=1-183.
DR PDB; 6LQQ; EM; 4.10 A; 5F=1-183.
DR PDB; 6LQR; EM; 8.60 A; 5F=1-183.
DR PDB; 6LQS; EM; 3.80 A; 5F=1-183.
DR PDB; 6LQT; EM; 4.90 A; 5F=1-183.
DR PDB; 6LQU; EM; 3.70 A; 5F=1-183.
DR PDB; 6LQV; EM; 4.80 A; 5F=1-183.
DR PDB; 6ND4; EM; 4.30 A; Z=1-183.
DR PDB; 6ZQA; EM; 4.40 A; CI=1-183.
DR PDB; 6ZQB; EM; 3.90 A; CI=1-183.
DR PDB; 6ZQC; EM; 3.80 A; CI=1-183.
DR PDB; 6ZQD; EM; 3.80 A; CI=1-183.
DR PDB; 6ZQE; EM; 7.10 A; CI=1-183.
DR PDB; 6ZQF; EM; 4.90 A; CI=1-183.
DR PDB; 7AJT; EM; 4.60 A; CI=1-183.
DR PDB; 7AJU; EM; 3.80 A; CI=1-183.
DR PDB; 7D4I; EM; 4.00 A; 5F=1-183.
DR PDB; 7D5S; EM; 4.60 A; 5F=1-183.
DR PDB; 7D5T; EM; 6.00 A; 5F=1-183.
DR PDB; 7D63; EM; 12.30 A; 5F=1-183.
DR PDBsum; 5WLC; -.
DR PDBsum; 5WXM; -.
DR PDBsum; 5WYJ; -.
DR PDBsum; 5WYK; -.
DR PDBsum; 6KE6; -.
DR PDBsum; 6LQP; -.
DR PDBsum; 6LQQ; -.
DR PDBsum; 6LQR; -.
DR PDBsum; 6LQS; -.
DR PDBsum; 6LQT; -.
DR PDBsum; 6LQU; -.
DR PDBsum; 6LQV; -.
DR PDBsum; 6ND4; -.
DR PDBsum; 6ZQA; -.
DR PDBsum; 6ZQB; -.
DR PDBsum; 6ZQC; -.
DR PDBsum; 6ZQD; -.
DR PDBsum; 6ZQE; -.
DR PDBsum; 6ZQF; -.
DR PDBsum; 7AJT; -.
DR PDBsum; 7AJU; -.
DR PDBsum; 7D4I; -.
DR PDBsum; 7D5S; -.
DR PDBsum; 7D5T; -.
DR PDBsum; 7D63; -.
DR AlphaFoldDB; P32899; -.
DR SMR; P32899; -.
DR BioGRID; 36582; 41.
DR ComplexPortal; CPX-1893; MPP10 complex.
DR DIP; DIP-5009N; -.
DR IntAct; P32899; 25.
DR MINT; P32899; -.
DR STRING; 4932.YHR148W; -.
DR MaxQB; P32899; -.
DR PaxDb; P32899; -.
DR PRIDE; P32899; -.
DR EnsemblFungi; YHR148W_mRNA; YHR148W; YHR148W.
DR GeneID; 856553; -.
DR KEGG; sce:YHR148W; -.
DR SGD; S000001191; IMP3.
DR VEuPathDB; FungiDB:YHR148W; -.
DR eggNOG; KOG4655; Eukaryota.
DR GeneTree; ENSGT00550000075090; -.
DR HOGENOM; CLU_097281_0_0_1; -.
DR InParanoid; P32899; -.
DR OMA; KVDFLDW; -.
DR BioCyc; YEAST:G3O-31183-MON; -.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:P32899; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P32899; protein.
DR GO; GO:0030686; C:90S preribosome; HDA:SGD.
DR GO; GO:0034457; C:Mpp10 complex; IDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0032040; C:small-subunit processome; IDA:SGD.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0030515; F:snoRNA binding; IDA:SGD.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IC:ComplexPortal.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IDA:SGD.
DR GO; GO:0006364; P:rRNA processing; IDA:SGD.
DR CDD; cd00165; S4; 1.
DR Gene3D; 3.10.290.10; -; 1.
DR InterPro; IPR022801; Ribosomal_S4/S9.
DR InterPro; IPR001912; Ribosomal_S4/S9_N.
DR InterPro; IPR002942; S4_RNA-bd.
DR InterPro; IPR036986; S4_RNA-bd_sf.
DR PANTHER; PTHR11831; PTHR11831; 1.
DR Pfam; PF00163; Ribosomal_S4; 1.
DR Pfam; PF01479; S4; 1.
DR SMART; SM01390; Ribosomal_S4; 1.
DR SMART; SM00363; S4; 1.
DR PROSITE; PS50889; S4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Reference proteome; Ribonucleoprotein;
KW Ribosome biogenesis; RNA-binding; rRNA processing; rRNA-binding.
FT CHAIN 1..183
FT /note="U3 small nucleolar ribonucleoprotein protein IMP3"
FT /id="PRO_0000132712"
FT DOMAIN 109..175
FT /note="S4 RNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00182"
FT HELIX 29..35
FT /evidence="ECO:0007829|PDB:5WXM"
FT HELIX 41..62
FT /evidence="ECO:0007829|PDB:5WXM"
FT HELIX 69..84
FT /evidence="ECO:0007829|PDB:5WXM"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:5WXM"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:5WXM"
FT HELIX 103..107
FT /evidence="ECO:0007829|PDB:5WXM"
FT HELIX 111..117
FT /evidence="ECO:0007829|PDB:5WXM"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:5WXM"
FT HELIX 124..132
FT /evidence="ECO:0007829|PDB:5WXM"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:5WXM"
FT TURN 152..156
FT /evidence="ECO:0007829|PDB:5WXM"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:5WXM"
SQ SEQUENCE 183 AA; 21885 MW; 2CA16A3425691DBD CRC64;
MVRKLKHHEQ KLLKKVDFLE WKQDQGHRDT QVMRTYHIQN REDYHKYNRI CGDIRRLANK
LSLLPPTDPF RRKHEQLLLD KLYAMGVLTT KSKISDLENK VTVSAICRRR LPVIMHRLKM
AETIQDAVKF IEQGHVRVGP NLINDPAYLV TRNMEDYVTW VDNSKIKKTL LRYRNQIDDF
DFS
