UTP23_YEAST
ID UTP23_YEAST Reviewed; 254 AA.
AC Q12339; D6W270;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=rRNA-processing protein UTP23;
DE AltName: Full=U three protein 23;
DE AltName: Full=U3 small nucleolar RNA-associated protein 23;
DE Short=U3 snoRNA-associated protein 23;
GN Name=UTP23; OrderedLocusNames=YOR004W;
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=8896276;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1091::aid-yea22>3.0.co;2-i;
RA Sterky F., Holmberg A., Pettersson B., Uhlen M.;
RT "The sequence of a 30 kb fragment on the left arm of chromosome XV from
RT Saccharomyces cerevisiae reveals 15 open reading frames, five of which
RT correspond to previously identified genes.";
RL Yeast 12:1091-1095(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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.
RX PubMed=12089522; DOI=10.1038/ng906;
RA Wu L.F., Hughes T.R., Davierwala A.P., Robinson M.D., Stoughton R.,
RA Altschuler S.J.;
RT "Large-scale prediction of Saccharomyces cerevisiae gene function using
RT overlapping transcriptional clusters.";
RL Nat. Genet. 31:255-265(2002).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
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 [6]
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 [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: Involved in rRNA-processing and ribosome biogenesis.
CC {ECO:0000269|PubMed:12089522}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095}.
CC Nucleus, nucleolus {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14690591}.
CC -!- MISCELLANEOUS: Present with 6960 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the UTP23/FCF1 family. UTP23 subfamily.
CC {ECO:0000305}.
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DR EMBL; U43491; AAC49483.1; -; Genomic_DNA.
DR EMBL; Z74912; CAA99192.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10786.1; -; Genomic_DNA.
DR PIR; S61987; S61987.
DR RefSeq; NP_014646.1; NM_001183423.1.
DR PDB; 4MJ7; X-ray; 2.51 A; A/B=1-159.
DR PDBsum; 4MJ7; -.
DR AlphaFoldDB; Q12339; -.
DR SMR; Q12339; -.
DR BioGRID; 34407; 110.
DR ComplexPortal; CPX-1604; Small ribosomal subunit processome, variant 1.
DR ComplexPortal; CPX-1607; Small ribosomal subunit processome, variant 2.
DR ComplexPortal; CPX-1608; Small ribosomal subunit processome, variant 3.
DR DIP; DIP-4352N; -.
DR IntAct; Q12339; 23.
DR MINT; Q12339; -.
DR STRING; 4932.YOR004W; -.
DR iPTMnet; Q12339; -.
DR MaxQB; Q12339; -.
DR PaxDb; Q12339; -.
DR PRIDE; Q12339; -.
DR EnsemblFungi; YOR004W_mRNA; YOR004W; YOR004W.
DR GeneID; 854165; -.
DR KEGG; sce:YOR004W; -.
DR SGD; S000005530; UTP23.
DR VEuPathDB; FungiDB:YOR004W; -.
DR eggNOG; KOG3164; Eukaryota.
DR GeneTree; ENSGT00940000153117; -.
DR HOGENOM; CLU_053567_1_1_1; -.
DR InParanoid; Q12339; -.
DR OMA; ASKKWVQ; -.
DR BioCyc; YEAST:G3O-33554-MON; -.
DR PRO; PR:Q12339; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12339; protein.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0032040; C:small-subunit processome; IDA:SGD.
DR GO; GO:0070181; F:small ribosomal subunit rRNA binding; IDA:SGD.
DR GO; GO:0000480; P:endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000472; P:endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IC:ComplexPortal.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:GO_Central.
DR InterPro; IPR006984; Fcf1/Utp23.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR Pfam; PF04900; Fcf1; 1.
DR SUPFAM; SSF88723; SSF88723; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Mitochondrion; Nucleus; Phosphoprotein; Reference proteome;
KW Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..254
FT /note="rRNA-processing protein UTP23"
FT /id="PRO_0000245250"
FT REGION 172..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT HELIX 4..18
FT /evidence="ECO:0007829|PDB:4MJ7"
FT STRAND 24..30
FT /evidence="ECO:0007829|PDB:4MJ7"
FT HELIX 32..41
FT /evidence="ECO:0007829|PDB:4MJ7"
FT HELIX 45..52
FT /evidence="ECO:0007829|PDB:4MJ7"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:4MJ7"
FT HELIX 63..72
FT /evidence="ECO:0007829|PDB:4MJ7"
FT HELIX 75..81
FT /evidence="ECO:0007829|PDB:4MJ7"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:4MJ7"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:4MJ7"
FT HELIX 99..107
FT /evidence="ECO:0007829|PDB:4MJ7"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:4MJ7"
FT HELIX 124..131
FT /evidence="ECO:0007829|PDB:4MJ7"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:4MJ7"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:4MJ7"
FT HELIX 153..158
FT /evidence="ECO:0007829|PDB:4MJ7"
SQ SEQUENCE 254 AA; 28801 MW; 27D00C72F6B492F6 CRC64;
MRQKRAKSYR KQLLVYSHTF KFREPYQVLV DNQLVLECNN SNFNLPSGLK RTLQADVKVM
ITQCCIQALY ETRNDGAINL AKQFERRRCN HSFKDPKSPA ECIESVVNIS GANKHRYVVA
SQDIDLRRKL RTVPGVPLIH LTRSVMVMEP LSTASAKASK ITEEQKLYKG LNDPNIEKLQ
ESGDGSGKES ITKKRKLGPK APNPLSVKKK KKVNSPSDEV KDKEDTSKEK KKRRRRKHKS
NTNVPVSNGT TAAQ
