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   27-MAR-2024, entry version 192.
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   PDB; 7SUK; EM; 3.99 A; LZ=2-183.
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   PDBsum; 7SUK; -.
DR   AlphaFoldDB; P32899; -.
DR   EMDB; EMD-0441; -.
DR   EMDB; EMD-0949; -.
DR   EMDB; EMD-0950; -.
DR   EMDB; EMD-0951; -.
DR   EMDB; EMD-0952; -.
DR   EMDB; EMD-0953; -.
DR   EMDB; EMD-0954; -.
DR   EMDB; EMD-0955; -.
DR   EMDB; EMD-11357; -.
DR   EMDB; EMD-11358; -.
DR   EMDB; EMD-11359; -.
DR   EMDB; EMD-11360; -.
DR   EMDB; EMD-11361; -.
DR   EMDB; EMD-11362; -.
DR   EMDB; EMD-11807; -.
DR   EMDB; EMD-11808; -.
DR   EMDB; EMD-25441; -.
DR   EMDB; EMD-30574; -.
DR   EMDB; EMD-30584; -.
DR   EMDB; EMD-30585; -.
DR   EMDB; EMD-30588; -.
DR   EMDB; EMD-6695; -.
DR   EMDB; EMD-6696; -.
DR   EMDB; EMD-8859; -.
DR   EMDB; EMD-9964; -.
DR   SMR; P32899; -.
DR   BioGRID; 36582; 76.
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; 4932-YHR148W; -.
DR   PeptideAtlas; P32899; -.
DR   EnsemblFungi; YHR148W_mRNA; YHR148W; YHR148W.
DR   GeneID; 856553; -.
DR   KEGG; sce:YHR148W; -.
DR   AGR; SGD:S000001191; -.
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; FRIKHEQ; -.
DR   OrthoDB; 5473811at2759; -.
DR   BioCyc; YEAST:G3O-31183-MONOMER; -.
DR   Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   BioGRID-ORCS; 856553; 2 hits in 10 CRISPR screens.
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:0015935; C:small ribosomal subunit; IEA:InterPro.
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:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0030490; P:maturation of SSU-rRNA; NAS: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; RNA-binding S4 domain; 1.
DR   InterPro; IPR022801; Ribosomal_uS4.
DR   InterPro; IPR001912; Ribosomal_uS4_N.
DR   InterPro; IPR002942; S4_RNA-bd.
DR   InterPro; IPR036986; S4_RNA-bd_sf.
DR   PANTHER; PTHR11831; 30S 40S RIBOSOMAL PROTEIN; 1.
DR   PANTHER; PTHR11831:SF1; U3 SMALL NUCLEOLAR RIBONUCLEOPROTEIN PROTEIN IMP3; 1.
DR   Pfam; PF00163; Ribosomal_S4; 1.
DR   Pfam; PF01479; S4; 1.
DR   SMART; SM01390; Ribosomal_S4; 1.
DR   SMART; SM00363; S4; 1.
DR   SUPFAM; SSF55174; Alpha-L RNA-binding motif; 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
//