RM27_YEAST
ID RM27_YEAST Reviewed; 146 AA.
AC P36526; D6VQS7;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=54S ribosomal protein L27, mitochondrial;
DE AltName: Full=Mitochondrial large ribosomal subunit protein mL41 {ECO:0000303|PubMed:24675956};
DE AltName: Full=YmL27;
DE Flags: Precursor;
GN Name=MRPL27; OrderedLocusNames=YBR282W; ORFNames=YBR2019;
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], AND PROTEIN SEQUENCE OF 17-32; 35-40;
RP 46-55 AND 77-92.
RX PubMed=1764528; DOI=10.1016/0300-9084(91)90063-7;
RA Graack H.-R., Grohmann L., Kitakawa M.;
RT "The nuclear coded mitoribosomal proteins YmL27 and YmL31 are both
RT essential for mitochondrial function in yeast.";
RL Biochimie 73:837-844(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091861; DOI=10.1002/yea.320100007;
RA Holmstroem K., Brandt T., Kallesoe T.;
RT "The sequence of a 32,420 bp segment located on the right arm of chromosome
RT II from Saccharomyces cerevisiae.";
RL Yeast 10:S47-S62(1994).
RN [3]
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 [4]
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 [5]
RP PROTEIN SEQUENCE OF 17-57 AND 77-92, 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 [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 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 [8]
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 [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 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 [11]
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. {ECO:0000305|PubMed:24675956,
CC ECO:0000305|PubMed:25609543}.
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 -!- MISCELLANEOUS: Present with 2250 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein
CC mL41 family. {ECO:0000305}.
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DR EMBL; S77888; AAB21096.2; -; Genomic_DNA.
DR EMBL; X76053; CAA53645.1; -; Genomic_DNA.
DR EMBL; Z36151; CAA85246.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07397.1; -; Genomic_DNA.
DR PIR; S27285; S27285.
DR RefSeq; NP_009841.1; NM_001178630.1.
DR PDB; 3J6B; EM; 3.20 A; 3=1-146.
DR PDB; 5MRC; EM; 3.25 A; 3=17-146.
DR PDB; 5MRE; EM; 3.75 A; 3=17-146.
DR PDB; 5MRF; EM; 4.97 A; 3=17-146.
DR PDBsum; 3J6B; -.
DR PDBsum; 5MRC; -.
DR PDBsum; 5MRE; -.
DR PDBsum; 5MRF; -.
DR AlphaFoldDB; P36526; -.
DR SMR; P36526; -.
DR BioGRID; 32976; 298.
DR ComplexPortal; CPX-1602; 54S mitochondrial large ribosomal subunit.
DR DIP; DIP-4961N; -.
DR IntAct; P36526; 9.
DR MINT; P36526; -.
DR STRING; 4932.YBR282W; -.
DR MaxQB; P36526; -.
DR PaxDb; P36526; -.
DR PRIDE; P36526; -.
DR EnsemblFungi; YBR282W_mRNA; YBR282W; YBR282W.
DR GeneID; 852585; -.
DR KEGG; sce:YBR282W; -.
DR SGD; S000000486; MRPL27.
DR VEuPathDB; FungiDB:YBR282W; -.
DR eggNOG; KOG4756; Eukaryota.
DR HOGENOM; CLU_1778531_0_0_1; -.
DR InParanoid; P36526; -.
DR OMA; ANLRRPW; -.
DR BioCyc; YEAST:G3O-29202-MON; -.
DR PRO; PR:P36526; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P36526; protein.
DR GO; GO:0005743; C:mitochondrial inner membrane; IC:ComplexPortal.
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; IC:SGD.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR InterPro; IPR019189; Ribosomal_L27/L41_mit.
DR PANTHER; PTHR21338; PTHR21338; 1.
DR Pfam; PF09809; MRP-L27; 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..16
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:1764528,
FT ECO:0000269|PubMed:2060626"
FT CHAIN 17..146
FT /note="54S ribosomal protein L27, mitochondrial"
FT /id="PRO_0000030574"
FT CONFLICT 17
FT /note="L -> T (in Ref. 1; AAB21096)"
FT /evidence="ECO:0000305"
FT CONFLICT 21
FT /note="W -> C (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="G -> H (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="R -> N (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="I -> M (in Ref. 1; AAB21096)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="V -> Y (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="L -> T (in Ref. 1; AAB21096)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="I -> M (in Ref. 1; AAB21096)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="I -> M (in Ref. 1; AAB21096)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 146 AA; 16492 MW; 0BB2E6D8A0E49213 CRC64;
MKGSPISQFS KTSINALTRP WKKYRDGELF YGLSKVGNKR VPLTTKQGNK TMYKGTRASG
IGRHTKFGGY VINWKKVRTY VTPDMVNFEL KPYVNANVPP LKHEFKGFSG GPLDPRLQLL
KIKEYIVNGR VQSEGATDTS CYKERG
