ID   RM36_YEAST     STANDARD;      PRT;   177 AA.
AC   P36531;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 3.
DT   03-OCT-2006, entry version 46.
DE   60S ribosomal protein L36, mitochondrial precursor (YmL36).
GN   Name=MRPL36; OrderedLocusNames=YBR122C; ORFNames=YBR0918;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   MEDLINE=95208357; PubMed=7900426;
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   MEDLINE=95112788; PubMed=7813418;
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.,
RA   Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C.,
RA   Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M.,
RA   Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L.,
RA   Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J.,
RA   Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T.,
RA   Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A.,
RA   Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B.,
RA   Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I.,
RA   Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M.,
RA   Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A.,
RA   van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I.,
RA   Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H.,
RA   Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
RN   [3]
RP   PROTEIN SEQUENCE OF 15-51.
RX   MEDLINE=91285106; 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
RT   subunit from yeast mitochondria.";
RL   FEBS Lett. 284:51-56(1991).
RN   [4]
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   [5]
RP   SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE MITOCHONDRIAL
RP   RIBOSOMAL LARGE COMPLEX.
RX   MEDLINE=22280971; PubMed=12392552;
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   [6]
RP   IDENTIFICATION OF PROBABLE INITIATION SITE.
RX   MEDLINE=22633889; 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   [7]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923954; 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   SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP   SCALE ANALYSIS].
RX   MEDLINE=22975177; PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA   Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P.,
RA   Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B.,
RA   Rehling P., Pfanner N., Meisinger C.;
RT   "The proteome of Saccharomyces cerevisiae mitochondria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN   [9]
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
RT   additional functional domains in Saccharomyces cerevisiae
RT   mitochondria.";
RL   Genetics 167:65-75(2004).
CC   -!- FUNCTION: Component of the large subunit of mitochondrial
CC       ribosome. Involved in mitochondrial translation. Overexpression
CC       suppresses mutations in the COX2 leader peptide-encoding and
CC       initiation codon regions.
CC   -!- INTERACTION:
CC       P43603:YFR024C; NbExp=1; IntAct=EBI-15582, EBI-22980;
CC       P32793:YSC84; NbExp=1; IntAct=EBI-15582, EBI-24460;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- DOMAIN: Contains two functional domains. The central domain is
CC       sufficient for general mitochondrial translation but not
CC       suppression of COX2 mutants. The C-terminus sequence is sufficient
CC       for dosage suppression of COX2 mutants.
CC   -!- SIMILARITY: In the central section; belongs to the ribosomal
CC       protein L31P family.
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DR   EMBL; X78993; CAA55624.1; ALT_INIT; Genomic_DNA.
DR   EMBL; Z35991; CAA85079.1; ALT_INIT; Genomic_DNA.
DR   PIR; S44701; S44701.
DR   IntAct; P36531; -.
DR   GermOnline; 138665; -.
DR   Ensembl; YBR122C; Saccharomyces cerevisiae.
DR   GenomeReviews; Y13134_GR; YBR122C.
DR   SGD; S000000326; MRPL36.
DR   BioCyc; SCER-S28-01:SCER-S28-01-000387-MONOMER; -.
DR   LinkHub; P36531; -.
DR   GO; GO:0005762; C:mitochondrial large ribosomal subunit; IPI.
DR   GO; GO:0005515; F:protein binding; IPI.
DR   GO; GO:0003735; F:structural constituent of ribosome; TAS.
DR   GO; GO:0016478; P:negative regulation of translation; IMP.
DR   GO; GO:0043037; P:translation; TAS.
KW   Complete proteome; Direct protein sequencing; Mitochondrion;
KW   Ribonucleoprotein; Ribosomal protein; Transit peptide.
FT   TRANSIT       1     14       Mitochondrion.
FT   CHAIN        15    177       60S ribosomal protein L36.
FT                                /FTId=PRO_0000030580.
FT   REGION       36    118       Sufficient for general mitochondrial
FT                                translation.
FT   REGION       87    177       Sufficient for dosage suppression of COX2
FT                                mutation.
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
//