ID RM36_YEAST Reviewed; 177 AA. AC P36531; D6VQC0; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 20-DEC-2005, sequence version 3. DT 02-JUN-2021, entry version 154. DE RecName: Full=54S ribosomal protein L36, mitochondrial; DE AltName: Full=Mitochondrial large ribosomal subunit protein bL31m {ECO:0000303|PubMed:24675956}; DE AltName: Full=YmL36; DE Flags: Precursor; GN Name=MRPL36; OrderedLocusNames=YBR122C; ORFNames=YBR0918; 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 204508 / S288c; RX PubMed=7900426; DOI=10.1002/yea.320101014; RA Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.; RT "Analysis of a 70 kb region on the right arm of yeast chromosome II."; RL Yeast 10:1363-1381(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x; RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H., RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., RA Mewes H.-W., Kleine K.; RT "Complete DNA sequence of yeast chromosome II."; RL EMBO J. 13:5795-5809(1994). 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 PROTEIN SEQUENCE OF 15-51, AND SUBUNIT. RC STRAIN=07173; RX PubMed=2060626; DOI=10.1016/0014-5793(91)80759-v; RA Grohmann L., Graack H.-R., Kruft V., Choli T., Goldschmidt-Reisin S., RA Kitakawa M.; RT "Extended N-terminal sequencing of proteins of the large ribosomal subunit RT from yeast mitochondria."; RL FEBS Lett. 284:51-56(1991). RN [5] RP FUNCTION. RX PubMed=11259585; DOI=10.1128/mcb.21.7.2359-2372.2001; RA Bonnefoy N., Bsat N., Fox T.D.; RT "Mitochondrial translation of Saccharomyces cerevisiae COX2 mRNA is RT controlled by the nucleotide sequence specifying the pre-Cox2p leader RT peptide."; RL Mol. Cell. Biol. 21:2359-2372(2001). RN [6] RP IDENTIFICATION IN THE MITOCHONDRIAL RIBOSOMAL LARGE COMPLEX, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=12392552; DOI=10.1046/j.1432-1033.2002.03226.x; RA Gan X., Kitakawa M., Yoshino K., Oshiro N., Yonezawa K., Isono K.; RT "Tag-mediated isolation of yeast mitochondrial ribosome and mass RT spectrometric identification of its new components."; RL Eur. J. Biochem. 269:5203-5214(2002). RN [7] RP IDENTIFICATION OF PROBABLE INITIATION SITE. RX PubMed=12748633; DOI=10.1038/nature01644; RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.; RT "Sequencing and comparison of yeast species to identify genes and RT regulatory elements."; RL Nature 423:241-254(2003). RN [8] 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 [9] 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 [10] RP FUNCTION, AND DOMAIN. RX PubMed=15166137; DOI=10.1534/genetics.167.1.65; RA Williams E.H., Perez-Martinez X., Fox T.D.; RT "MrpL36p, a highly diverged L31 ribosomal protein homolog with additional RT functional domains in Saccharomyces cerevisiae mitochondria."; RL Genetics 167:65-75(2004). RN [11] RP SUBCELLULAR LOCATION. RX PubMed=25609543; DOI=10.1038/ncomms7019; RA Pfeffer S., Woellhaf M.W., Herrmann J.M., Forster F.; RT "Organization of the mitochondrial translation machinery studied in situ by RT cryoelectron tomography."; RL Nat. Commun. 6:6019-6019(2015). RN [12] RP STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS), AND SUBUNIT. RX PubMed=24675956; DOI=10.1126/science.1249410; RA Amunts A., Brown A., Bai X.C., Llacer J.L., Hussain T., Emsley P., Long F., RA Murshudov G., Scheres S.H., Ramakrishnan V.; RT "Structure of the yeast mitochondrial large ribosomal subunit."; RL Science 343:1485-1489(2014). CC -!- FUNCTION: Component of the mitochondrial ribosome (mitoribosome), a CC dedicated translation machinery responsible for the synthesis of CC mitochondrial genome-encoded proteins, including at least some of the CC essential transmembrane subunits of the mitochondrial respiratory CC chain. The mitoribosomes are attached to the mitochondrial inner CC membrane and translation products are cotranslationally integrated into CC the membrane (PubMed:25609543, PubMed:24675956). Overexpression of CC bL31m suppresses mutations in the COX2 leader peptide-encoding and CC initiation codon regions (PubMed:11259585, PubMed:15166137). CC {ECO:0000269|PubMed:11259585, ECO:0000269|PubMed:15166137, CC ECO:0000305|PubMed:24675956, ECO:0000305|PubMed:25609543}. CC -!- FUNCTION: Overexpression suppresses mutations in the COX2 leader CC peptide-encoding and initiation codon regions. CC {ECO:0000269|PubMed:11259585, ECO:0000269|PubMed:15166137}. CC -!- SUBUNIT: Component of the mitochondrial large ribosomal subunit (mt- CC LSU). Mature yeast 74S mitochondrial ribosomes consist of a small (37S) CC and a large (54S) subunit. The 37S small subunit contains a 15S CC ribosomal RNA (15S mt-rRNA) and 34 different proteins. The 54S large CC subunit contains a 21S rRNA (21S mt-rRNA) and 46 different proteins. CC {ECO:0000269|PubMed:12392552, ECO:0000269|PubMed:2060626, CC ECO:0000269|PubMed:24675956}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095, CC ECO:0000269|PubMed:14576278}. Note=Mitoribosomes are tethered to the CC mitochondrial inner membrane and spatially aligned with the membrane CC insertion machinery through two distinct membrane contact sites, formed CC by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein CC MBA1. {ECO:0000269|PubMed:25609543}. CC -!- DOMAIN: Contains two functional domains. The central domain is CC sufficient for general mitochondrial translation but not suppression of CC COX2 mutants. The C-terminus sequence is sufficient for dosage CC suppression of COX2 mutants. {ECO:0000269|PubMed:15166137}. CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL31 family. CC Highly divergent. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA55624.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=CAA85079.1; Type=Erroneous initiation; Evidence={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; X78993; CAA55624.1; ALT_INIT; Genomic_DNA. DR EMBL; Z35991; CAA85079.1; ALT_INIT; Genomic_DNA. DR EMBL; BK006936; DAA07240.1; -; Genomic_DNA. DR PIR; S44701; S44701. DR RefSeq; NP_009680.2; NM_001178470.1. DR PDB; 3J6B; EM; 3.20 A; V=1-177. DR PDB; 5MRC; EM; 3.25 A; V=1-177. DR PDB; 5MRE; EM; 3.75 A; V=1-177. DR PDB; 5MRF; EM; 4.97 A; V=1-177. DR PDBsum; 3J6B; -. DR PDBsum; 5MRC; -. DR PDBsum; 5MRE; -. DR PDBsum; 5MRF; -. DR SMR; P36531; -. DR BioGRID; 32824; 136. DR ComplexPortal; CPX-1602; 54S mitochondrial large ribosomal subunit. DR DIP; DIP-4628N; -. DR IntAct; P36531; 15. DR MINT; P36531; -. DR STRING; 4932.YBR122C; -. DR MaxQB; P36531; -. DR PaxDb; P36531; -. DR PRIDE; P36531; -. DR EnsemblFungi; YBR122C_mRNA; YBR122C; YBR122C. DR GeneID; 852419; -. DR KEGG; sce:YBR122C; -. DR SGD; S000000326; MRPL36. DR VEuPathDB; FungiDB:YBR122C; -. DR eggNOG; ENOG502RZ6E; Eukaryota. DR HOGENOM; CLU_130029_1_0_1; -. DR InParanoid; P36531; -. DR OMA; GRSWDAN; -. DR PRO; PR:P36531; -. DR Proteomes; UP000002311; Chromosome II. DR RNAct; P36531; protein. DR GO; GO:0005762; C:mitochondrial large ribosomal subunit; IDA:SGD. DR GO; GO:0005739; C:mitochondrion; HDA:SGD. DR GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD. DR GO; GO:0032543; P:mitochondrial translation; IMP:SGD. DR InterPro; IPR034600; MRPL36_yeast. DR PANTHER; PTHR28174; PTHR28174; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Mitochondrion; Reference proteome; KW Ribonucleoprotein; Ribosomal protein; Transit peptide. FT TRANSIT 1..14 FT /note="Mitochondrion" FT /evidence="ECO:0000269|PubMed:2060626" FT CHAIN 15..177 FT /note="54S ribosomal protein L36, mitochondrial" FT /id="PRO_0000030580" FT REGION 36..118 FT /note="Sufficient for general mitochondrial translation" FT REGION 87..177 FT /note="Sufficient for dosage suppression of COX2 mutation" FT REGION 111..144 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 124..144 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 177 AA; 20091 MW; 7A8DF86EE899B848 CRC64; MLKSIFAKRF ASTGSYPGST RITLPRRPAK KIQLGKSRPA IYHQFNVKME LSDGSVVIRR SQYPKGEIRL IQDQRNNPLW NPSRDDLVVV DANSGGSLDR FNKRYSSLFS VDSTTPNSSS ETVELSEENK KKTQIKKEEK EDVSEKAFGM DDYLSLLDDS EQQIKSGKLA SKKRDKK //