LTO1_YEAST
ID LTO1_YEAST Reviewed; 162 AA.
AC P53846; D6W0T3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Protein LTO1 {ECO:0000303|PubMed:23318452, ECO:0000305};
DE AltName: Full=LTO1 family protein YNL260C {ECO:0000305};
GN Name=LTO1 {ECO:0000303|PubMed:23318452}; OrderedLocusNames=YNL260C;
GN ORFNames=N0838;
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=9234673;
RX DOI=10.1002/(sici)1097-0061(199707)13:9<849::aid-yea106>3.0.co;2-n;
RA Sen-Gupta M., Gueldener U., Beinhauer J.D., Fiedler T.A., Hegemann J.H.;
RT "Sequence analysis of the 33 kb long region between ORC5 and SUI1 from the
RT left arm of chromosome XIV from Saccharomyces cerevisiae.";
RL Yeast 13:849-860(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
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 IDENTIFICATION BY MASS SPECTROMETRY.
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 [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, INTERACTION WITH YAE1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP GLU-11; PHE-18; LEU-19; GLN-50; VAL-57; LYS-83; PHE-94; LEU-101; ASN-103;
RP HIS-113; ARG-134; ASN-146 AND GLU-147.
RX PubMed=23318452; DOI=10.1038/onc.2012.604;
RA Zhai C., Li Y., Mascarenhas C., Lin Q., Li K., Vyrides I., Grant C.M.,
RA Panaretou B.;
RT "The function of ORAOV1/LTO1, a gene that is overexpressed frequently in
RT cancer: essential roles in the function and biogenesis of the ribosome.";
RL Oncogene 33:484-494(2014).
RN [7]
RP FUNCTION, INTERACTION WITH YAE1 AND THE CIA COMPLEX, MUTAGENESIS OF ASP-4;
RP 17-GLY--GLY-21; 33-GLY--GLY-41; 49-GLY--GLY-53 AND TRP-162, AND
RP IDENTIFICATION OF INITIATION SITE.
RX PubMed=26182403; DOI=10.7554/elife.08231;
RA Paul V.D., Muehlenhoff U., Stuempfig M., Seebacher J., Kugler K.G.,
RA Renicke C., Taxis C., Gavin A.C., Pierik A.J., Lill R.;
RT "The deca-GX3 proteins Yae1-Lto1 function as adaptors recruiting the ABC
RT protein Rli1 for iron-sulfur cluster insertion.";
RL Elife 4:E08231-E08231(2015).
CC -!- FUNCTION: Essential for life in oxygen, but nonessential under
CC anaerobic conditions. Required for biogenesis of the large ribosomal
CC subunit and initiation of translation in oxygen (PubMed:23318452). The
CC complex LTO1:YAE1 functions as a target specific adapter that recruits
CC apo-RLI1 to the cytosolic iron-sulfur protein assembly (CIA) complex
CC machinery (PubMed:26182403). {ECO:0000269|PubMed:23318452,
CC ECO:0000269|PubMed:26182403}.
CC -!- SUBUNIT: Forms a complex with YAE1; the complex bridges the interaction
CC between the CIA complex and RLI1 (PubMed:23318452). Associates with the
CC CIA complex (via its C-terminal tryptophan) (PubMed:26182403).
CC {ECO:0000269|PubMed:23318452, ECO:0000269|PubMed:26182403}.
CC -!- INTERACTION:
CC P53846; P47118: YAE1; NbExp=2; IntAct=EBI-28226, EBI-25522;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23318452}.
CC -!- MISCELLANEOUS: Present with 784 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the LTO1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA65484.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA96167.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=DAA10299.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X96722; CAA65484.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z71536; CAA96167.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006947; DAA10299.1; ALT_INIT; Genomic_DNA.
DR PIR; S63233; S63233.
DR RefSeq; NP_014139.1; NM_001183098.1.
DR AlphaFoldDB; P53846; -.
DR SMR; P53846; -.
DR BioGRID; 35579; 129.
DR DIP; DIP-4273N; -.
DR IntAct; P53846; 5.
DR MINT; P53846; -.
DR STRING; 4932.YNL260C; -.
DR PaxDb; P53846; -.
DR PRIDE; P53846; -.
DR EnsemblFungi; YNL260C_mRNA; YNL260C; YNL260C.
DR GeneID; 855461; -.
DR KEGG; sce:YNL260C; -.
DR SGD; S000005204; YNL260C.
DR eggNOG; KOG4595; Eukaryota.
DR HOGENOM; CLU_136375_0_0_1; -.
DR InParanoid; P53846; -.
DR BioCyc; YEAST:G3O-33256-MON; -.
DR ChiTaRS; LTO1; yeast.
DR PRO; PR:P53846; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53846; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0062092; C:Yae1-Lto1 complex; IDA:SGD.
DR GO; GO:0106035; P:protein maturation by [4Fe-4S] cluster transfer; IDA:UniProtKB.
DR InterPro; IPR019191; Essential_protein_Yae1_N.
DR Pfam; PF09811; Yae1_N; 1.
PE 1: Evidence at protein level;
KW Nucleus; Reference proteome.
FT CHAIN 1..162
FT /note="Protein LTO1"
FT /id="PRO_0000203382"
FT REGION 17..53
FT /note="deca-GX3 motif; required for interaction with YAE1
FT and the CIA complex"
FT /evidence="ECO:0000269|PubMed:26182403"
FT MUTAGEN 4
FT /note="D->A: No effect on interaction with YAE1 or the CIA
FT complex. No effect on iron incorporation into RLI1."
FT /evidence="ECO:0000269|PubMed:26182403"
FT MUTAGEN 11
FT /note="E->G: Lethal at 37 degrees Celsius; when associated
FT with P-19, E-83, L-113 and G-147. Lethal at 37 degrees
FT Celsius; when associated with R-0, R-50, L-94, S-101 and S-
FT 146."
FT /evidence="ECO:0000269|PubMed:23318452"
FT MUTAGEN 17..21
FT /note="GFLEG->AFLEA: Slightly decreases interaction with
FT YAE1 and the CIA complex. No effect on iron incorporation
FT into RLI1."
FT /evidence="ECO:0000269|PubMed:26182403"
FT MUTAGEN 18
FT /note="F->L: Lethal at 37 degrees Celsius; when associated
FT with D-57, D-103 and G-134."
FT /evidence="ECO:0000269|PubMed:23318452"
FT MUTAGEN 19
FT /note="L->P: Lethal at 37 degrees Celsius; when associated
FT with G-11, E-83, L-113 and G-147."
FT /evidence="ECO:0000269|PubMed:23318452"
FT MUTAGEN 33..41
FT /note="GKQYGLQVG->AKQYALQVA: Decreases interaction with
FT YAE1 and the CIA complex. Abolishes iron incorporation into
FT RLI1."
FT /evidence="ECO:0000269|PubMed:26182403"
FT MUTAGEN 49..53
FT /note="GQMEG->AQMEA: Decreases interaction with YAE1 and
FT the CIA complex. Strongly decreases iron incorporation into
FT RLI1."
FT /evidence="ECO:0000269|PubMed:26182403"
FT MUTAGEN 50
FT /note="Q->R: Lethal at 37 degrees Celsius; when associated
FT with G-11, L-94, S-101 and S-146."
FT /evidence="ECO:0000269|PubMed:23318452"
FT MUTAGEN 57
FT /note="V->D: Lethal at 37 degrees Celsius; when associated
FT with L-18, D-103 and G-134."
FT /evidence="ECO:0000269|PubMed:23318452"
FT MUTAGEN 83
FT /note="K->E: Lethal at 37 degrees Celsius; when associated
FT with G-11, P-19, L-113 and G-147."
FT /evidence="ECO:0000269|PubMed:23318452"
FT MUTAGEN 94
FT /note="F->L: Lethal at 37 degrees Celsius; when associated
FT with G-11, R-50, S-101 and S-146."
FT /evidence="ECO:0000269|PubMed:23318452"
FT MUTAGEN 101
FT /note="L->S: Lethal at 37 degrees Celsius; when associated
FT with G-11, R-50, L-94 and S-146."
FT /evidence="ECO:0000269|PubMed:23318452"
FT MUTAGEN 103
FT /note="N->D: Lethal at 37 degrees Celsius; when associated
FT with L-18, D-57 and G-134."
FT /evidence="ECO:0000269|PubMed:23318452"
FT MUTAGEN 113
FT /note="H->L: Lethal at 37 degrees Celsius; when associated
FT with G-11, P-19, E-83 and G-147."
FT /evidence="ECO:0000269|PubMed:23318452"
FT MUTAGEN 134
FT /note="R->G: Lethal at 37 degrees Celsius; when associated
FT with L-18, D-57 and D-103."
FT /evidence="ECO:0000269|PubMed:23318452"
FT MUTAGEN 146
FT /note="N->S: Lethal at 37 degrees Celsius; when associated
FT with G-11, R-50,L-94 and S-101."
FT /evidence="ECO:0000269|PubMed:23318452"
FT MUTAGEN 147
FT /note="E->G: Lethal at 37 degrees Celsius; when associated
FT with G-11, P-19, E-83 and L-113."
FT /evidence="ECO:0000269|PubMed:23318452"
FT MUTAGEN 162
FT /note="W->A: Abolishes interaction with the CIA complex. No
FT effect on interaction with YAE1. Strongly decreases iron
FT incorporation into RLI1."
FT /evidence="ECO:0000269|PubMed:26182403"
SQ SEQUENCE 162 AA; 18896 MW; 63FCBF5B30ABC714 CRC64;
MDFDNLLNLE EQYYQEGFLE GQNENIKQSF LEGKQYGLQV GFQRFTLLGQ MEGLCDVIES
YGLHSPTLEK NIHTIRTLMK GLKMNNDDES VMEFERVLIK LKNKFRTILI TLHRLVKDKR
TPTVTFEVFE DVSRAIAGEI RGFVENEDIA KNKTKQNQAQ SW
