SDO1_YEAST
ID SDO1_YEAST Reviewed; 250 AA.
AC Q07953; D6VY24;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Ribosome maturation protein SDO1;
GN Name=SDO1; OrderedLocusNames=YLR022C;
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 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 [4]
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 [5]
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 [6]
RP ASSOCIATION WITH 60S RIBOSOMAL SUBUNITS.
RX PubMed=15701634; DOI=10.1074/jbc.m414421200;
RA Savchenko A., Krogan N., Cort J.R., Evdokimova E., Lew J.M., Yee A.A.,
RA Sanchez-Pulido L., Andrade M.A., Bochkarev A., Watson J.D., Kennedy M.A.,
RA Greenblatt J., Hughes T., Arrowsmith C.H., Rommens J.M., Edwards A.M.;
RT "The Shwachman-Bodian-Diamond syndrome protein family is involved in RNA
RT metabolism.";
RL J. Biol. Chem. 280:19213-19220(2005).
RN [7]
RP MUTAGENESIS OF CYS-31; ASN-34 AND LEU-71.
RX PubMed=15701631; DOI=10.1074/jbc.m414656200;
RA Shammas C., Menne T.F., Hilcenko C., Michell S.R., Goyenechea B.,
RA Boocock G.R.B., Durie P.R., Rommens J.M., Warren A.J.;
RT "Structural and mutational analysis of the SBDS protein family. Insight
RT into the leukemia-associated Shwachman-Diamond Syndrome.";
RL J. Biol. Chem. 280:19221-19229(2005).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17353896; DOI=10.1038/ng1994;
RA Menne T.F., Goyenechea B., Sanchez-Puig N., Wong C.C., Tonkin L.M.,
RA Ancliff P.J., Brost R.L., Costanzo M., Boone C., Warren A.J.;
RT "The Shwachman-Bodian-Diamond syndrome protein mediates translational
RT activation of ribosomes in yeast.";
RL Nat. Genet. 39:486-495(2007).
RN [9]
RP FUNCTION.
RX PubMed=19713223; DOI=10.3324/haematol.2009.012450;
RA Moore J.B. IV, Farrar J.E., Arceci R.J., Liu J.M., Ellis S.R.;
RT "Distinct ribosome maturation defects in yeast models of Diamond-Blackfan
RT anemia and Shwachman-Diamond syndrome.";
RL Haematologica 95:57-64(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 the biogenesis of the 60S ribosomal subunit and
CC translational activation of ribosomes. Together with the EF-2-like
CC GTPase RIA1, may trigger the GTP-dependent release of TIF6 from 60S
CC pre-ribosomes in the cytoplasm, thereby activating ribosomes for
CC translation competence by allowing 80S ribosome assembly and
CC facilitating TIF6 recycling to the nucleus, where it is required for
CC 60S rRNA processing and nuclear export. {ECO:0000269|PubMed:17353896,
CC ECO:0000269|PubMed:19713223}.
CC -!- SUBUNIT: Associates with the 60S ribosomal subunit.
CC -!- INTERACTION:
CC Q07953; P53893: RIA1; NbExp=2; IntAct=EBI-27124, EBI-28980;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14690591}. Nucleus.
CC -!- MISCELLANEOUS: Present with 5060 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SDO1/SBDS family. {ECO:0000305}.
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DR EMBL; Z73194; CAA97545.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09340.1; -; Genomic_DNA.
DR PIR; S64849; S64849.
DR RefSeq; NP_013122.1; NM_001181909.1.
DR AlphaFoldDB; Q07953; -.
DR SASBDB; Q07953; -.
DR SMR; Q07953; -.
DR BioGRID; 31296; 261.
DR IntAct; Q07953; 17.
DR MINT; Q07953; -.
DR STRING; 4932.YLR022C; -.
DR ChEMBL; CHEMBL1741198; -.
DR MaxQB; Q07953; -.
DR PaxDb; Q07953; -.
DR PRIDE; Q07953; -.
DR EnsemblFungi; YLR022C_mRNA; YLR022C; YLR022C.
DR GeneID; 850709; -.
DR KEGG; sce:YLR022C; -.
DR SGD; S000004012; SDO1.
DR VEuPathDB; FungiDB:YLR022C; -.
DR eggNOG; KOG2917; Eukaryota.
DR GeneTree; ENSGT00390000008135; -.
DR HOGENOM; CLU_043216_1_1_1; -.
DR InParanoid; Q07953; -.
DR OMA; TIISAKC; -.
DR BioCyc; YEAST:G3O-32183-MON; -.
DR PRO; PR:Q07953; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q07953; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:SGD.
DR GO; GO:0042256; P:mature ribosome assembly; IMP:SGD.
DR Gene3D; 1.10.10.900; -; 1.
DR Gene3D; 3.30.1250.10; -; 1.
DR InterPro; IPR018023; Ribosome_mat_SBDS_CS.
DR InterPro; IPR036786; Ribosome_mat_SBDS_N_sf.
DR InterPro; IPR018978; Ribosome_mat_Sdo1/SBDS_C.
DR InterPro; IPR019783; Ribosome_mat_Sdo1/SBDS_N.
DR InterPro; IPR002140; Sdo1/SBDS.
DR InterPro; IPR039100; Sdo1/SBDS-like.
DR InterPro; IPR037188; Sdo1/SBDS_central_sf.
DR PANTHER; PTHR10927; PTHR10927; 1.
DR Pfam; PF01172; SBDS; 1.
DR Pfam; PF09377; SBDS_C; 1.
DR SUPFAM; SSF109728; SSF109728; 1.
DR SUPFAM; SSF89895; SSF89895; 1.
DR TIGRFAMs; TIGR00291; RNA_SBDS; 1.
DR PROSITE; PS01267; UPF0023; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Reference proteome; Ribosome biogenesis.
FT CHAIN 1..250
FT /note="Ribosome maturation protein SDO1"
FT /id="PRO_0000123764"
FT MUTAGEN 31
FT /note="C->W: Impairs protein folding and stability. Loss of
FT function."
FT /evidence="ECO:0000269|PubMed:15701631"
FT MUTAGEN 34
FT /note="N->I: Impairs protein folding and stability. Loss of
FT function."
FT /evidence="ECO:0000269|PubMed:15701631"
FT MUTAGEN 71
FT /note="L->P: Impairs protein folding and stability. Loss of
FT function."
FT /evidence="ECO:0000269|PubMed:15701631"
SQ SEQUENCE 250 AA; 28283 MW; EFC799ADEFF73E0E CRC64;
MPINQPSGQI KLTNVSLVRL KKARKRFEVA CYQNKVQDYR KGIEKDLDEV LQIHQVFMNV
SKGLVANKED LQKCFGTTNV DDVIEEIMHK GEIQLSEKER QLMLNKVNNE MLTIVSAKCI
NPVSKKRYPP TMIHKALQEL KFSPVINKPA KLQALEAIKL LVSKQIIPIV RAKMKVKVAI
SEPSRQPELI EKISKLIASS PGESTKPELD PWTCTGLIDP VNYRDLMTLC DKKGTVQVLD
MAVIDNTTHN
