ID UTP12_YEAST Reviewed; 943 AA. AC Q12220; D6VYC4; Q05386; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 189. DE RecName: Full=U3 small nucleolar RNA-associated protein 12; DE Short=U3 snoRNA-associated protein 12; DE AltName: Full=DOM34-interacting protein 2; DE AltName: Full=U three protein 12; GN Name=DIP2; Synonyms=UTP12; OrderedLocusNames=YLR129W; GN ORFNames=L3116, L9233.1; 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=9169871; RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J., RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., RA Zollner A., Hani J., Hoheisel J.D.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."; RL Nature 387:87-90(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). CC -!- FUNCTION: Involved in nucleolar processing of pre-18S ribosomal RNA. CC {ECO:0000269|PubMed:12068309}. 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. {ECO:0000269|PubMed:12068309}. CC -!- INTERACTION: CC Q12220; P25635: PWP2; NbExp=11; IntAct=EBI-5896, EBI-14332; CC Q12220; Q05946: UTP13; NbExp=7; IntAct=EBI-5896, EBI-34702; CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12068309}. CC -!- MISCELLANEOUS: Present with 9620 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the WD repeat WDR3/UTP12 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U53877; AAB82375.1; -; Genomic_DNA. DR EMBL; U53881; AAB82402.1; -; Genomic_DNA. DR EMBL; X91258; CAA62640.1; -; Genomic_DNA. DR EMBL; Z73301; CAA97699.1; -; Genomic_DNA. DR EMBL; Z73302; CAA97700.1; -; Genomic_DNA. DR EMBL; X89514; CAA61707.1; -; Genomic_DNA. DR EMBL; BK006945; DAA09440.1; -; Genomic_DNA. DR PIR; S59317; S59317. DR RefSeq; NP_013230.1; NM_001182016.1. DR PDB; 5WLC; EM; 3.80 A; LQ=1-943. DR PDB; 5WYJ; EM; 8.70 A; BB=1-943. DR PDB; 5WYK; EM; 4.50 A; BB=1-943. DR PDB; 6KE6; EM; 3.40 A; B2=1-943. DR PDB; 6LQP; EM; 3.20 A; B2=1-943. DR PDB; 6LQQ; EM; 4.10 A; B2=1-943. DR PDB; 6LQR; EM; 8.60 A; B2=1-943. DR PDB; 6LQS; EM; 3.80 A; B2=1-943. DR PDB; 6LQT; EM; 4.90 A; B2=1-943. DR PDB; 6LQU; EM; 3.70 A; B2=1-943. DR PDB; 6LQV; EM; 4.80 A; B2=1-943. DR PDB; 6ND4; EM; 4.30 A; Q=1-943. DR PDB; 6ZQA; EM; 4.40 A; UL=1-943. DR PDB; 6ZQB; EM; 3.90 A; UL=1-943. DR PDB; 6ZQC; EM; 3.80 A; UL=1-943. DR PDB; 6ZQD; EM; 3.80 A; UL=1-943. DR PDB; 6ZQE; EM; 7.10 A; UL=1-943. DR PDB; 6ZQF; EM; 4.90 A; UL=1-943. DR PDB; 7AJT; EM; 4.60 A; UL=1-943. DR PDB; 7AJU; EM; 3.80 A; UL=1-943. DR PDB; 7D4I; EM; 4.00 A; B2=1-943. DR PDB; 7D5S; EM; 4.60 A; B2=1-943. DR PDB; 7D5T; EM; 6.00 A; B2=1-943. DR PDB; 7D63; EM; 12.30 A; B2=1-943. DR PDB; 7SUK; EM; 3.99 A; LQ=5-943. 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; 6ZQF; -. DR PDBsum; 7AJT; -. DR PDBsum; 7AJU; -. DR PDBsum; 7D4I; -. DR PDBsum; 7D5S; -. DR PDBsum; 7D5T; -. DR PDBsum; 7D63; -. DR PDBsum; 7SUK; -. DR AlphaFoldDB; Q12220; -. 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-30574; -. DR EMDB; EMD-30584; -. DR EMDB; EMD-30585; -. DR EMDB; EMD-30588; -. DR EMDB; EMD-6695; -. DR EMDB; EMD-6696; -. DR EMDB; EMD-9964; -. DR SMR; Q12220; -. DR BioGRID; 31398; 147. DR ComplexPortal; CPX-1410; UTP-B complex. DR DIP; DIP-6494N; -. DR IntAct; Q12220; 21. DR MINT; Q12220; -. DR STRING; 4932.YLR129W; -. DR iPTMnet; Q12220; -. DR MaxQB; Q12220; -. DR PaxDb; 4932-YLR129W; -. DR PeptideAtlas; Q12220; -. DR EnsemblFungi; YLR129W_mRNA; YLR129W; YLR129W. DR GeneID; 850820; -. DR KEGG; sce:YLR129W; -. DR AGR; SGD:S000004119; -. DR SGD; S000004119; DIP2. DR VEuPathDB; FungiDB:YLR129W; -. DR eggNOG; KOG0306; Eukaryota. DR GeneTree; ENSGT00940000153859; -. DR HOGENOM; CLU_005318_0_1_1; -. DR InParanoid; Q12220; -. DR OMA; MQCLRTV; -. DR OrthoDB; 168440at2759; -. DR BioCyc; YEAST:G3O-32271-MONOMER; -. DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol. DR BioGRID-ORCS; 850820; 4 hits in 10 CRISPR screens. DR PRO; PR:Q12220; -. DR Proteomes; UP000002311; Chromosome XII. DR RNAct; Q12220; 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:0034388; C:Pwp2p-containing subcomplex of 90S preribosome; IDA:SGD. DR GO; GO:0032040; C:small-subunit processome; 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; IBA:GO_Central. DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD. DR CDD; cd00200; WD40; 1. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 4. DR InterPro; IPR020472; G-protein_beta_WD-40_rep. DR InterPro; IPR007148; SSU_processome_Utp12. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR019775; WD40_repeat_CS. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR19853; WD REPEAT CONTAINING PROTEIN 3 WDR3; 1. DR PANTHER; PTHR19853:SF0; WD REPEAT-CONTAINING PROTEIN 3; 1. DR Pfam; PF04003; Utp12; 1. DR Pfam; PF00400; WD40; 10. DR PRINTS; PR00320; GPROTEINBRPT. DR SMART; SM00320; WD40; 11. DR SUPFAM; SSF117289; Nucleoporin domain; 1. DR SUPFAM; SSF50978; WD40 repeat-like; 1. DR PROSITE; PS00678; WD_REPEATS_1; 4. DR PROSITE; PS50082; WD_REPEATS_2; 8. 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; WD repeat. FT CHAIN 1..943 FT /note="U3 small nucleolar RNA-associated protein 12" FT /id="PRO_0000050955" FT REPEAT 77..107 FT /note="WD 1" FT REPEAT 119..149 FT /note="WD 2" FT REPEAT 161..190 FT /note="WD 3" FT REPEAT 202..230 FT /note="WD 4" FT REPEAT 389..418 FT /note="WD 5" FT REPEAT 428..458 FT /note="WD 6" FT REPEAT 471..501 FT /note="WD 7" FT REPEAT 571..601 FT /note="WD 8" FT REPEAT 613..643 FT /note="WD 9" FT REPEAT 655..685 FT /note="WD 10" FT REGION 715..739 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 718..739 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 943 AA; 106342 MW; 7D9AEC7AF6A9C740 CRC64; MVKSYQRFEQ AAAFGVIASN ANCVWIPASS GNSNGSGPGQ LITSALEDVN IWDIKTGDLV SKLSDGLPPG ASDARGAKPA ECTYLEAHKD TDLLAVGYAD GVIKVWDLMS KTVLLNFNGH KAAITLLQFD GTGTRLISGS KDSNIIVWDL VGEVGLYKLR SHKDSITGFW CQGEDWLIST SKDGMIKLWD LKTHQCIETH IAHTGECWGL AVKDDLLITT GTDSQVKIWK LDIENDKMGG KLTEMGIFEK QSKQRGLKIE FITNSSDKTS FFYIQNADKT IETFRIRKEE EIARGLKKRE KRLKEKGLTE EEIAKSIKES YSSFILHPFQ TIRSLYKIKS ASWTTVSSSK LELVLTTSSN TIEYYSIPYE KRDPTSPAPL KTHTIELQGQ RTDVRSIDIS DDNKLLATAS NGSLKIWNIK THKCIRTFEC GYALTCKFLP GGLLVILGTR NGELQLFDLA SSSLLDTIED AHDAAIWSLD LTSDGKRLVT GSADKTVKFW DFKVENSLVP GTKNKFLPVL KLHHDTTLEL TDDILCVRVS PDDRYLAISL LDNTVKVFFL DSMKFYLSLY GHKLPVLSID ISFDSKMIIT SSADKNIKIW GLDFGDCHKS LFAHQDSIMN VKFLPQSHNF FSCSKDAVVK YWDGEKFECI QKLYAHQSEV WALAVATDGG FVVSSSHDHS IRIWEETEDQ VFLEEEKEKE LEEQYEDTLL TSLEEGNGDD AFKADASGEG VEDEASGVHK QTLESLKAGE RLMEALDLGI AEIEGLEAYN RDMKLWQRKK LGEAPIKPQG NAVLIAVNKT PEQYIMDTLL RIRMSQLEDA LMVMPFSYVL KFLKFIDTVM QNKTLLHSHL PLICKNLFFI IKFNHKELVS QKNEELKLQI NRVKTELRSA LKSTEDDLGF NVQGLKFVKQ QWNLRHNYEF VDEYDQQEKE SNSARKRVFG TVI //