SDO1L_YEAST
ID SDO1L_YEAST Reviewed; 111 AA.
AC P38804; D3DL39;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Restriction of telomere capping protein 3;
GN Name=RTC3; OrderedLocusNames=YHR087W;
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=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
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 FUNCTION.
RX PubMed=18845848; DOI=10.1534/genetics.108.092577;
RA Addinall S.G., Downey M., Yu M., Zubko M.K., Dewar J., Leake A.,
RA Hallinan J., Shaw O., James K., Wilkinson D.J., Wipat A., Durocher D.,
RA Lydall D.;
RT "A genomewide suppressor and enhancer analysis of cdc13-1 reveals varied
RT cellular processes influencing telomere capping in Saccharomyces
RT cerevisiae.";
RL Genetics 180:2251-2266(2008).
RN [7]
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 [8]
RP STRUCTURE BY NMR.
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).
CC -!- FUNCTION: May play a role in RNA metabolism, rRNA-processing, and in a
CC process influencing telomere capping. {ECO:0000269|PubMed:18845848}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2430 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SDO1-like family. {ECO:0000305}.
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DR EMBL; U00060; AAB68927.1; -; Genomic_DNA.
DR EMBL; AY557845; AAS56171.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06783.1; -; Genomic_DNA.
DR PIR; S46719; S46719.
DR RefSeq; NP_011955.1; NM_001179217.1.
DR PDB; 1NYN; NMR; -; A=1-111.
DR PDBsum; 1NYN; -.
DR AlphaFoldDB; P38804; -.
DR BMRB; P38804; -.
DR SMR; P38804; -.
DR BioGRID; 36522; 116.
DR DIP; DIP-2925N; -.
DR IntAct; P38804; 2.
DR MINT; P38804; -.
DR STRING; 4932.YHR087W; -.
DR iPTMnet; P38804; -.
DR MaxQB; P38804; -.
DR PaxDb; P38804; -.
DR PRIDE; P38804; -.
DR TopDownProteomics; P38804; -.
DR DNASU; 856487; -.
DR EnsemblFungi; YHR087W_mRNA; YHR087W; YHR087W.
DR GeneID; 856487; -.
DR KEGG; sce:YHR087W; -.
DR SGD; S000001129; RTC3.
DR VEuPathDB; FungiDB:YHR087W; -.
DR eggNOG; ENOG502S9SB; Eukaryota.
DR HOGENOM; CLU_137480_1_1_1; -.
DR InParanoid; P38804; -.
DR OMA; VKYFYKG; -.
DR BioCyc; YEAST:G3O-31134-MON; -.
DR EvolutionaryTrace; P38804; -.
DR PRO; PR:P38804; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38804; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0016070; P:RNA metabolic process; IGI:SGD.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1250.10; -; 1.
DR InterPro; IPR036786; Ribosome_mat_SBDS_N_sf.
DR InterPro; IPR019783; Ribosome_mat_Sdo1/SBDS_N.
DR InterPro; IPR039100; Sdo1/SBDS-like.
DR PANTHER; PTHR10927; PTHR10927; 1.
DR Pfam; PF01172; SBDS; 1.
DR SUPFAM; SSF89895; SSF89895; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Nucleus; Reference proteome; Ribosome biogenesis;
KW rRNA processing.
FT CHAIN 1..111
FT /note="Restriction of telomere capping protein 3"
FT /id="PRO_0000202905"
FT REGION 89..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:1NYN"
FT STRAND 12..21
FT /evidence="ECO:0007829|PDB:1NYN"
FT HELIX 23..31
FT /evidence="ECO:0007829|PDB:1NYN"
FT HELIX 35..41
FT /evidence="ECO:0007829|PDB:1NYN"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:1NYN"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:1NYN"
FT HELIX 65..72
FT /evidence="ECO:0007829|PDB:1NYN"
FT HELIX 79..87
FT /evidence="ECO:0007829|PDB:1NYN"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:1NYN"
SQ SEQUENCE 111 AA; 12009 MW; 34A95645CAFB51BD CRC64;
MSTVTKYFYK GENTDLIVFA ASEELVDEYL KNPSIGKLSE VVELFEVFTP QDGRGAEGEL
GAASKAQVEN EFGKGKKIEE VIDLILRNGK PNSTTSSLKT KGGNAGTKAY N
