UTP10_YEAST
ID UTP10_YEAST Reviewed; 1769 AA.
AC P42945; D6VW75;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=U3 small nucleolar RNA-associated protein 10;
DE Short=U3 snoRNA-associated protein 10;
DE AltName: Full=U three protein 10;
DE AltName: Full=U3 protein 10 required for transcription;
DE AltName: Full=t-UTP10;
GN Name=UTP10; OrderedLocusNames=YJL109C; ORFNames=J0808;
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=7483851; DOI=10.1002/yea.320110909;
RA Rasmussen S.W.;
RT "A 37.5 kb region of yeast chromosome X includes the SME1, MEF2, GSH1 and
RT CSD3 genes, a TCP-1-related gene, an open reading frame similar to the
RT DAL80 gene, and a tRNA(Arg).";
RL Yeast 11:873-883(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
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, 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 [5]
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 [6]
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 [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [8]
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 [9]
RP FUNCTION.
RX PubMed=16544271; DOI=10.1002/yea.1353;
RA Wade C.H., Umbarger M.A., McAlear M.A.;
RT "The budding yeast rRNA and ribosome biosynthesis (RRB) regulon contains
RT over 200 genes.";
RL Yeast 23:293-306(2006).
RN [10]
RP FUNCTION, INTERACTION WITH SNORNA U3 AND PRE-RIBOSOMAL RNA, AND SUBCELLULAR
RP LOCATION.
RX PubMed=17652137; DOI=10.1261/rna.609807;
RA Dez C., Dlakic M., Tollervey D.;
RT "Roles of the HEAT repeat proteins Utp10 and Utp20 in 40S ribosome
RT maturation.";
RL RNA 13:1516-1527(2007).
RN [11]
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).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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). Involved in ribosome biosynthesis. {ECO:0000269|PubMed:12068309,
CC ECO:0000269|PubMed:15489292, ECO:0000269|PubMed:16544271,
CC ECO:0000269|PubMed:17652137}.
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, ECO:0000269|PubMed:17652137}.
CC -!- INTERACTION:
CC P42945; P47083: MPP10; NbExp=7; IntAct=EBI-1884, EBI-11168;
CC P42945; Q02931: NAN1; NbExp=7; IntAct=EBI-1884, EBI-37773;
CC P42945; Q06512: NOC4; NbExp=3; IntAct=EBI-1884, EBI-36459;
CC P42945; Q05022: RRP5; NbExp=4; IntAct=EBI-1884, EBI-16011;
CC P42945; Q06679: UTP4; NbExp=4; IntAct=EBI-1884, EBI-35712;
CC P42945; P40055: UTP7; NbExp=6; IntAct=EBI-1884, EBI-22597;
CC P42945; P53276: UTP8; NbExp=4; IntAct=EBI-1884, EBI-23301;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Mitochondrion.
CC Note=Associated with ribosomal chromatin, even in the absence of
CC transcription.
CC -!- MISCELLANEOUS: Present with 18200 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the HEATR1/UTP10 family. {ECO:0000305}.
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DR EMBL; X85021; CAA59385.1; -; Genomic_DNA.
DR EMBL; Z49384; CAA89404.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08691.1; -; Genomic_DNA.
DR PIR; S53378; S53378.
DR RefSeq; NP_012426.1; NM_001181542.1.
DR PDB; 5WLC; EM; 3.80 A; LM=1-1769.
DR PDB; 5WYJ; EM; 8.70 A; AE=1-808.
DR PDB; 5WYK; EM; 4.50 A; AE=1-1769.
DR PDB; 6KE6; EM; 3.40 A; AE=1-1769.
DR PDB; 6LQP; EM; 3.20 A; AE=1-1769.
DR PDB; 6LQQ; EM; 4.10 A; AE=1-1769.
DR PDB; 6LQR; EM; 8.60 A; AE=1-1769.
DR PDB; 6LQS; EM; 3.80 A; AE=1-1769.
DR PDB; 6LQT; EM; 4.90 A; AE=1-1769.
DR PDB; 6LQU; EM; 3.70 A; AE=1-1769.
DR PDB; 6LQV; EM; 4.80 A; AE=1-1769.
DR PDB; 6ND4; EM; 4.30 A; M=1-1769.
DR PDB; 6ZQA; EM; 4.40 A; UJ=1-1769.
DR PDB; 6ZQB; EM; 3.90 A; UJ=1-1769.
DR PDB; 6ZQC; EM; 3.80 A; UJ=1-1769.
DR PDB; 6ZQD; EM; 3.80 A; UJ=1-1769.
DR PDB; 6ZQE; EM; 7.10 A; UJ=1-1769.
DR PDB; 7AJT; EM; 4.60 A; UJ=1-1769.
DR PDB; 7AJU; EM; 3.80 A; UJ=1-1769.
DR PDB; 7D4I; EM; 4.00 A; AE=1-1769.
DR PDB; 7D5S; EM; 4.60 A; AE=1-1769.
DR PDB; 7D5T; EM; 6.00 A; AE=1-1769.
DR PDB; 7D63; EM; 12.30 A; AE=1-1769.
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; 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; P42945; -.
DR SMR; P42945; -.
DR BioGRID; 33647; 462.
DR ComplexPortal; CPX-1409; UTP-A complex.
DR DIP; DIP-6466N; -.
DR IntAct; P42945; 65.
DR MINT; P42945; -.
DR STRING; 4932.YJL109C; -.
DR iPTMnet; P42945; -.
DR MaxQB; P42945; -.
DR PaxDb; P42945; -.
DR PRIDE; P42945; -.
DR TopDownProteomics; P42945; -.
DR EnsemblFungi; YJL109C_mRNA; YJL109C; YJL109C.
DR GeneID; 853335; -.
DR KEGG; sce:YJL109C; -.
DR SGD; S000003645; UTP10.
DR VEuPathDB; FungiDB:YJL109C; -.
DR eggNOG; KOG1837; Eukaryota.
DR GeneTree; ENSGT00390000015845; -.
DR HOGENOM; CLU_001128_3_1_1; -.
DR InParanoid; P42945; -.
DR OMA; YTNQLLF; -.
DR BioCyc; YEAST:G3O-31563-MON; -.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:P42945; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P42945; protein.
DR GO; GO:0030686; C:90S preribosome; IDA:SGD.
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:0030688; C:preribosome, small subunit precursor; IDA:GO_Central.
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:0030515; F:snoRNA binding; IBA:GO_Central.
DR GO; GO:0034511; F:U3 snoRNA 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:SGD.
DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; IMP:SGD.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR012954; BP28_C_dom.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR022125; U3snoRNP10_N.
DR InterPro; IPR040191; UTP10.
DR PANTHER; PTHR13457; PTHR13457; 1.
DR Pfam; PF08146; BP28CT; 1.
DR Pfam; PF12397; U3snoRNP10; 1.
DR SMART; SM01036; BP28CT; 1.
DR SUPFAM; SSF48371; SSF48371; 3.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Mitochondrion; Nucleus; Reference proteome;
KW Ribonucleoprotein; Ribosome biogenesis; rRNA processing; Transcription.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..1769
FT /note="U3 small nucleolar RNA-associated protein 10"
FT /id="PRO_0000186207"
FT REPEAT 1729..1767
FT /note="HEAT"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 1769 AA; 200082 MW; 064480D1D249B241 CRC64;
MSSLSDQLAQ VASNNATVAL DRKRRQKLHS ASLIYNSKTA ATQDYDFIFE NASKALEELS
QIEPKFAIFS RTLFSESSIS LDRNVQTKEE IKDLDNAINA YLLLASSKWY LAPTLHATEW
LVRRFQIHVK NTEMLLLSTL NYYQTPVFKR ILSIIKLPPL FNCLSNFVRS EKPPTALTMI
KLFNDMDFLK LYTSYLDQCI KHNATYTNQL LFTTCCFINV VAFNSNNDEK LNQLVPILLE
ISAKLLASKS KDCQIAAHTI LVVFATALPL KKTIILAAME TILSNLDAKE AKHSALLTIC
KLFQTLKGQG NVDQLPSKIF KLFDSKFDTV SILTFLDKED KPVCDKFITS YTRSIARYDR
SKLNIILSLL KKIRLERYEV RLIITDLIYL SEILEDKSQL VELFEYFISI NEDLVLKCLK
SLGLTGELFE IRLTTSLFTN ADVNTDIVKQ LSDPVETTKK DTASFQTFLD KHSELINTTN
VSMLTETGER YKKVLSLFTE AIGKGYKASS FLTSFFTTLE SRITFLLRVT ISPAAPTALK
LISLNNIAKY INSIEKEVNI FTLVPCLICA LRDASIKVRT GVKKILSLIA KRPSTKHYFL
SDKLYGENVT IPMLNPKDSE AWLSGFLNEY VTENYDISRI LTPKRNEKVF LMFWANQALL
IPSPYAKTVL LDNLNKSPTY ASSYSSLFEE FISHYLENRS SWEKSCIANK TNFEHFERSL
VNLVSPKEKQ SFMIDFVLSA LNSDYEQLAN IAAERLISIF ASLNNAQKLK IVQNIVDSSS
NVESSYDTVG VLQSLPLDSD IFVSILNQNS ISNEMDQTDF SKRRRRRSST SKNAFLKEEV
SQLAELHLRK LTIILEALDK VRNVGSEKLL FTLLSLLSDL ETLDQDGGLP VLYAQETLIS
CTLNTITYLK EHGCTELTNV RADILVSAIR NSASPQVQNK LLLVIGSLAT LSSEVILHSV
MPIFTFMGAH SIRQDDEFTT KVVERTILTV VPALIKNSKG NEKEEMEFLL LSFTTALQHV
PRHRRVKLFS TLIKTLDPVK ALGSFLFLIA QQYSSALVNF KIGEARILIE FIKALLVDLH
VNEELSGLND LLDIIKLLTS SKSSSEKKKS LESRVLFSNG VLNFSESEFL TFMNNTFEFI
NKITEETDQD YYDVRRNLRL KVYSVLLDET SDKKLIRNIR EEFGTLLEGV LFFINSVELT
FSCITSQENE EASDSETSLS DHTTEIKEIL FKVLGNVLQI LPVDEFVNAV LPLLSTSTNE
DIRYHLTLVI GSKFELEGSE AIPIVNNVMK VLLDRMPLES KSVVISQVIL NTMTALVSKY
GKKLEGSILT QALTLATEKV SSDMTEVKIS SLALITNCVQ VLGVKSIAFY PKIVPPSIKL
FDASLADSSN PLKEQLQVAI LLLFAGLIKR IPSFLMSNIL DVLHVIYFSR EVDSSIRLSV
ISLIIENIDL KEVLKVLFRI WSTEIATSND TVAVSLFLST LESTVENIDK KSATSQSPIF
FKLLLSLFEF RSISSFDNNT ISRIEASVHE ISNSYVLKMN DKVFRPLFVI LVRWAFDGEG
VTNAGITETE RLLAFFKFFN KLQENLRGII TSYFTYLLEP VDMLLKRFIS KDMENVNLRR
LVINSLTSSL KFDRDEYWKS TSRFELISVS LVNQLSNIEN SIGKYLVKAI GALASNNSGV
DEHNQILNKL IVEHMKASCS SNEKLWAIRA MKLIYSKIGE SWLVLLPQLV PVIAELLEDD
DEEIEREVRT GLVKVVENVL GEPFDRYLD
