UTP17_YEAST
ID UTP17_YEAST Reviewed; 896 AA.
AC Q02931; D6W3P1;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=NET1-associated nuclear protein 1;
DE AltName: Full=U three protein 17;
DE Short=t-17;
DE AltName: Full=U3 protein 17 required for transcription;
DE AltName: Full=U3 small nucleolar RNA-associated protein 17;
DE Short=U3 snoRNA-associated protein 17;
GN Name=NAN1; Synonyms=UTP17; OrderedLocusNames=YPL126W;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
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 FUNCTION, INTERACTION WITH MPP10 AND SNORNA U3, IDENTIFICATION IN SSU
RP PROCESSOME BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
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 [4]
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 [5]
RP FUNCTION, IDENTIFICATION IN COMPLEX WITH OTHER T-UTPS, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15489292; DOI=10.1101/gad.1226604;
RA Gallagher J.E.G., Dunbar D.A., Granneman S., Mitchell B.M., Osheim Y.,
RA Beyer A.L., Baserga S.J.;
RT "RNA polymerase I transcription and pre-rRNA processing are linked by
RT specific SSU processome components.";
RL Genes Dev. 18:2506-2517(2004).
RN [6]
RP IDENTIFICATION BY 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 nucleolar processing of pre-18S ribosomal RNA.
CC Required for optimal pre-ribosomal RNA transcription by RNA polymerase
CC I together with a subset of U3 proteins required for transcription (t-
CC UTPs). {ECO:0000269|PubMed:12068309, ECO:0000269|PubMed:15489292}.
CC -!- SUBUNIT: Interacts with snoRNA U3. Interacts with MPP10. Component of
CC the ribosomal small subunit (SSU) processome composed of at least 40
CC protein subunits and snoRNA U3. In the absence of snoRNA3, forms a
CC complex with other t-UTPs. This complex can associate with pre-18S
CC ribosomal RNAs. {ECO:0000269|PubMed:12068309,
CC ECO:0000269|PubMed:15489292}.
CC -!- INTERACTION:
CC Q02931; P42945: UTP10; NbExp=7; IntAct=EBI-37773, EBI-1884;
CC Q02931; P53276: UTP8; NbExp=5; IntAct=EBI-37773, EBI-23301;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12068309,
CC ECO:0000269|PubMed:15489292}. Note=Associated with ribosomal chromatin,
CC even in the absence of transcription.
CC -!- MISCELLANEOUS: Present with 6560 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U43503; AAB68236.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11307.1; -; Genomic_DNA.
DR PIR; S61996; S61996.
DR RefSeq; NP_015199.1; NM_001183940.1.
DR PDB; 5WLC; EM; 3.80 A; LH=1-896.
DR PDB; 6KE6; EM; 3.40 A; AG=1-896.
DR PDB; 6LQP; EM; 3.20 A; AG=1-896.
DR PDB; 6LQQ; EM; 4.10 A; AG=1-896.
DR PDB; 6LQR; EM; 8.60 A; AG=1-896.
DR PDB; 6LQS; EM; 3.80 A; AG=1-896.
DR PDB; 6LQT; EM; 4.90 A; AG=1-896.
DR PDB; 6LQU; EM; 3.70 A; AG=1-896.
DR PDB; 6LQV; EM; 4.80 A; AG=1-896.
DR PDB; 6ND4; EM; 4.30 A; H=1-896.
DR PDB; 6ZQA; EM; 4.40 A; UQ=1-896.
DR PDB; 6ZQB; EM; 3.90 A; UQ=1-896.
DR PDB; 6ZQC; EM; 3.80 A; UQ=1-896.
DR PDB; 6ZQD; EM; 3.80 A; UQ=1-896.
DR PDB; 6ZQE; EM; 7.10 A; UQ=1-896.
DR PDB; 7AJT; EM; 4.60 A; UQ=1-896.
DR PDB; 7AJU; EM; 3.80 A; UQ=1-896.
DR PDB; 7D4I; EM; 4.00 A; AG=1-896.
DR PDB; 7D5S; EM; 4.60 A; AG=1-896.
DR PDB; 7D5T; EM; 6.00 A; AG=1-896.
DR PDB; 7D63; EM; 12.30 A; AG=1-896.
DR PDBsum; 5WLC; -.
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; 7AJT; -.
DR PDBsum; 7AJU; -.
DR PDBsum; 7D4I; -.
DR PDBsum; 7D5S; -.
DR PDBsum; 7D5T; -.
DR PDBsum; 7D63; -.
DR AlphaFoldDB; Q02931; -.
DR SMR; Q02931; -.
DR BioGRID; 36055; 92.
DR ComplexPortal; CPX-1409; UTP-A complex.
DR DIP; DIP-3999N; -.
DR IntAct; Q02931; 47.
DR MINT; Q02931; -.
DR STRING; 4932.YPL126W; -.
DR iPTMnet; Q02931; -.
DR MaxQB; Q02931; -.
DR PaxDb; Q02931; -.
DR PRIDE; Q02931; -.
DR EnsemblFungi; YPL126W_mRNA; YPL126W; YPL126W.
DR GeneID; 855977; -.
DR KEGG; sce:YPL126W; -.
DR SGD; S000006047; NAN1.
DR VEuPathDB; FungiDB:YPL126W; -.
DR eggNOG; KOG1963; Eukaryota.
DR HOGENOM; CLU_348179_0_0_1; -.
DR InParanoid; Q02931; -.
DR OMA; KWHIDSV; -.
DR BioCyc; YEAST:G3O-34025-MON; -.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:Q02931; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q02931; protein.
DR GO; GO:0030686; C:90S preribosome; HDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0033553; C:rDNA heterochromatin; IDA:SGD.
DR GO; GO:0032040; C:small-subunit processome; IDA:SGD.
DR GO; GO:0034455; C:t-UTP complex; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0034511; F:U3 snoRNA binding; IDA: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:SGD.
DR GO; GO:2000234; P:positive regulation of rRNA processing; IBA:GO_Central.
DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; IMP:SGD.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 3.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Reference proteome; Repeat; Ribonucleoprotein;
KW Ribosome biogenesis; rRNA processing; Transcription; WD repeat.
FT CHAIN 1..896
FT /note="NET1-associated nuclear protein 1"
FT /id="PRO_0000051088"
FT REPEAT 295..334
FT /note="WD 1"
FT REPEAT 490..542
FT /note="WD 2"
FT REPEAT 552..595
FT /note="WD 3"
FT REPEAT 605..645
FT /note="WD 4"
SQ SEQUENCE 896 AA; 101237 MW; F4E3687BD328230E CRC64;
MTQSLGIEQY KLSVVSGGKP ALNNLSSVTG NKNIARLSQD QRNYIIPFNN QIKVYSVETR
QCVKTLKFAN NSLLSGIFLQ EEENNESIVK ILLGDITVPQ QEDAHLITVF TNNGHVIVLN
YKGKLVESPK HFKISLADEK LANVFHSEGN YRILTTFKDP SQKAHNSLQS YRLYALTFDD
AKKQFEVAHQ AEWHNVILSN ISSNGKLLAH MCKDVSTKDH EHKSISVVSL FDDSVNLSFP
LGSILSSQTQ SLSYNTRYVS SMAIDNMGQQ LAVGFASGVI SIVSLADLQI RLLKWHIDSV
LSLSFSHDGS YLLSGGWEKV MSLWQLETNS QQFLPRLNGI IIDCQVLGPQ GNYYSLILQM
TENNSNSDYQ FLLLNASDLT SKLSINGPLP VFNSTIKHIQ QPISAMNTKN SNSITSLNHS
KKKQSRKLIK SRRQDFTTNV EINPINKNLY FPHISAVQIF DFYKNEQVNY QYLTSGVNNS
MGKVRFELNL QDPIITDLKF TKDGQWMITY EIEYPPNDLL SSKDLTHILK FWTKNDNETN
WNLKTKVINP HGISVPITKI LPSPRSVNNS QGCLTADNNG GLKFWSFDSH ESNWCLKKIS
LPNFNHFSNS VSLAWSQDGS LIFHGFDDKL QILDFDTFKK FESLENTKTV SEFTLDSEIQ
TVKLINDTNL IVATRTTLNA INLLRGQVIN SFDLYPFVNG VYKNGHMDRL ITCDERTGNI
ALVINQQLTD LDGVPTINYK SRIIIFDSDL STKLGNFTHH EYISWIGWNY DTDFIFLDIE
STLGVVGTTV NTQLSDEVNN EGILDGLVSN TITTSASNSD IFAEQLHKLS SRGKKSDTRD
KNTNDNDEDE EDIALEFING EKKDKLVNMN SFTSMFDNIQ NVQMDTFFDR VMKVLT
