IMP4_YEAST
ID IMP4_YEAST Reviewed; 290 AA.
AC P53941; D6W1A4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=U3 small nucleolar ribonucleoprotein protein IMP4;
DE Short=U3 snoRNP protein IMP4;
DE AltName: Full=Interacting with MPP10 protein 4;
GN Name=IMP4; OrderedLocusNames=YNL075W; ORFNames=N2353;
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].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8701611;
RX DOI=10.1002/(sici)1097-0061(19960330)12:4<391::aid-yea921>3.0.co;2-n;
RA Poehlmann R., Philippsen P.;
RT "Sequencing a cosmid clone of Saccharomyces cerevisiae chromosome XIV
RT reveals 12 new open reading frames (ORFs) and an ancient duplication of six
RT ORFs.";
RL Yeast 12:391-402(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
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 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 [5]
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 [6]
RP FUNCTION, INTERACTION WITH MPP10, AND MUTAGENESIS OF ARG-119; ARG-201;
RP ARG-220 AND ARG-253.
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 P53941; P36009: DHR2; NbExp=2; IntAct=EBI-9243, EBI-5844;
CC P53941; P38333: ENP1; NbExp=6; IntAct=EBI-9243, EBI-6482;
CC P53941; P47083: MPP10; NbExp=7; IntAct=EBI-9243, EBI-11168;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:10409734}.
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DR EMBL; X86470; CAA60184.1; -; Genomic_DNA.
DR EMBL; Z71351; CAA95949.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10470.1; -; Genomic_DNA.
DR PIR; S53904; S53904.
DR RefSeq; NP_014324.3; NM_001182913.3.
DR PDB; 5WLC; EM; 3.80 A; SM=1-290.
DR PDB; 5WYJ; EM; 8.70 A; MB=1-290.
DR PDB; 5WYK; EM; 4.50 A; MB=1-290.
DR PDB; 6KE6; EM; 3.40 A; 5G=1-290.
DR PDB; 6LQP; EM; 3.20 A; 5G=1-290.
DR PDB; 6LQQ; EM; 4.10 A; 5G=1-290.
DR PDB; 6LQR; EM; 8.60 A; 5G=1-290.
DR PDB; 6LQS; EM; 3.80 A; 5G=1-290.
DR PDB; 6LQT; EM; 4.90 A; 5G=1-290.
DR PDB; 6LQU; EM; 3.70 A; 5G=1-290.
DR PDB; 6LQV; EM; 4.80 A; 5G=1-290.
DR PDB; 6ZQA; EM; 4.40 A; CJ=1-290.
DR PDB; 6ZQB; EM; 3.90 A; CJ=1-290.
DR PDB; 6ZQC; EM; 3.80 A; CJ=1-290.
DR PDB; 6ZQD; EM; 3.80 A; CJ=1-290.
DR PDB; 6ZQE; EM; 7.10 A; CJ=1-290.
DR PDB; 6ZQF; EM; 4.90 A; CJ=1-290.
DR PDB; 6ZQG; EM; 3.50 A; CJ=1-290.
DR PDB; 7AJT; EM; 4.60 A; CJ=1-290.
DR PDB; 7AJU; EM; 3.80 A; CJ=1-290.
DR PDB; 7D4I; EM; 4.00 A; 5G=1-290.
DR PDB; 7D5S; EM; 4.60 A; 5G=1-290.
DR PDB; 7D5T; EM; 6.00 A; 5G=1-290.
DR PDB; 7D63; EM; 12.30 A; 5G=1-290.
DR PDBsum; 5WLC; -.
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; 6ZQA; -.
DR PDBsum; 6ZQB; -.
DR PDBsum; 6ZQC; -.
DR PDBsum; 6ZQD; -.
DR PDBsum; 6ZQE; -.
DR PDBsum; 6ZQF; -.
DR PDBsum; 6ZQG; -.
DR PDBsum; 7AJT; -.
DR PDBsum; 7AJU; -.
DR PDBsum; 7D4I; -.
DR PDBsum; 7D5S; -.
DR PDBsum; 7D5T; -.
DR PDBsum; 7D63; -.
DR AlphaFoldDB; P53941; -.
DR SMR; P53941; -.
DR BioGRID; 35748; 74.
DR ComplexPortal; CPX-1893; MPP10 complex.
DR DIP; DIP-4362N; -.
DR IntAct; P53941; 28.
DR MINT; P53941; -.
DR STRING; 4932.YNL075W; -.
DR iPTMnet; P53941; -.
DR MaxQB; P53941; -.
DR PaxDb; P53941; -.
DR PRIDE; P53941; -.
DR EnsemblFungi; YNL075W_mRNA; YNL075W; YNL075W.
DR GeneID; 855649; -.
DR KEGG; sce:YNL075W; -.
DR SGD; S000005019; IMP4.
DR VEuPathDB; FungiDB:YNL075W; -.
DR eggNOG; KOG2781; Eukaryota.
DR GeneTree; ENSGT00940000153231; -.
DR HOGENOM; CLU_040063_2_0_1; -.
DR InParanoid; P53941; -.
DR OMA; IGTMSEQ; -.
DR BioCyc; YEAST:G3O-33104-MON; -.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:P53941; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53941; 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:0042134; F:rRNA primary transcript binding; IDA:SGD.
DR GO; GO:0043047; F:single-stranded telomeric DNA binding; IDA:SGD.
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 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; Ribonucleoprotein;
KW Ribosome biogenesis; rRNA processing.
FT CHAIN 1..290
FT /note="U3 small nucleolar ribonucleoprotein protein IMP4"
FT /id="PRO_0000120245"
FT DOMAIN 86..267
FT /note="Brix"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00034"
FT MUTAGEN 119
FT /note="R->A: No effect on RNA binding."
FT /evidence="ECO:0000269|PubMed:15489263"
FT MUTAGEN 201
FT /note="R->A: No effect on RNA binding."
FT /evidence="ECO:0000269|PubMed:15489263"
FT MUTAGEN 220
FT /note="R->A: Loss of RNA binding."
FT /evidence="ECO:0000269|PubMed:15489263"
FT MUTAGEN 253
FT /note="R->A: Loss of RNA binding."
FT /evidence="ECO:0000269|PubMed:15489263"
SQ SEQUENCE 290 AA; 33482 MW; DF9F863364848B63 CRC64;
MLRRQARERR EYLYRKAQEL QDSQLQQKRQ IIKQALAQGK PLPKELAEDE SLQKDFRYDQ
SLKESEEADD LQVDDEYAAT SGIMDPRIIV TTSRDPSTRL SQFAKEIKLL FPNAVRLNRG
NYVMPNLVDA CKKSGTTDLV VLHEHRGVPT SLTISHFPHG PTAQFSLHNV VMRHDIINAG
NQSEVNPHLI FDNFTTALGK RVVCILKHLF NAGPKKDSER VITFANRGDF ISVRQHVYVR
TREGVEIAEV GPRFEMRLFE LRLGTLENKD ADVEWQLRRF IRTANKKDYL
