RM04_YEAST
ID RM04_YEAST Reviewed; 319 AA.
AC P36517; D6VZ74;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=54S ribosomal protein L4, mitochondrial;
DE AltName: Full=Mitochondrial large ribosomal subunit protein uL29m {ECO:0000303|PubMed:24675956};
DE AltName: Full=YmL4;
DE Flags: Precursor;
GN Name=MRPL4; OrderedLocusNames=YLR439W; ORFNames=L9753.1;
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=07173;
RX PubMed=7828914; DOI=10.1016/0378-1119(94)00633-4;
RA Graack H.-R., Grohmann L., Kitakawa M., Goldschmidt-Reisin S.;
RT "Gene MRP-L4, encoding mitochondrial ribosomal protein YmL4, is
RT indispensable for proper non-respiratory cell functions in yeast.";
RL Gene 152:107-112(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 PROTEIN SEQUENCE OF 15-41, AND SUBUNIT.
RC STRAIN=07173;
RX PubMed=3060376; DOI=10.1016/0014-5793(88)80975-x;
RA Graack H.-R., Grohmann L., Choli T.;
RT "Mitochondrial ribosomes of yeast: isolation of individual proteins and N-
RT terminal sequencing.";
RL FEBS Lett. 242:4-8(1988).
RN [5]
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 [6]
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 [7]
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 [8]
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 [9]
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:24675956, ECO:0000269|PubMed:3060376}.
CC -!- INTERACTION:
CC P36517; P21560: CBP3; NbExp=3; IntAct=EBI-402, EBI-4134;
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 7700 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL29 family.
CC {ECO:0000305}.
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DR EMBL; Z30582; CAA83057.1; -; Genomic_DNA.
DR EMBL; U21094; AAB67513.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09740.1; -; Genomic_DNA.
DR PIR; S59407; S59407.
DR RefSeq; NP_013544.1; NM_001182327.1.
DR PDB; 3J6B; EM; 3.20 A; T=1-319.
DR PDB; 5MRC; EM; 3.25 A; T=15-239.
DR PDB; 5MRE; EM; 3.75 A; T=15-239.
DR PDB; 5MRF; EM; 4.97 A; T=15-239.
DR PDBsum; 3J6B; -.
DR PDBsum; 5MRC; -.
DR PDBsum; 5MRE; -.
DR PDBsum; 5MRF; -.
DR AlphaFoldDB; P36517; -.
DR SMR; P36517; -.
DR BioGRID; 31698; 96.
DR ComplexPortal; CPX-1602; 54S mitochondrial large ribosomal subunit.
DR DIP; DIP-940N; -.
DR IntAct; P36517; 19.
DR MINT; P36517; -.
DR STRING; 4932.YLR439W; -.
DR MaxQB; P36517; -.
DR PaxDb; P36517; -.
DR PRIDE; P36517; -.
DR EnsemblFungi; YLR439W_mRNA; YLR439W; YLR439W.
DR GeneID; 851160; -.
DR KEGG; sce:YLR439W; -.
DR SGD; S000004431; MRPL4.
DR VEuPathDB; FungiDB:YLR439W; -.
DR eggNOG; KOG3331; Eukaryota.
DR GeneTree; ENSGT00390000002837; -.
DR HOGENOM; CLU_872105_0_0_1; -.
DR InParanoid; P36517; -.
DR OMA; PLWQFFS; -.
DR BioCyc; YEAST:G3O-32495-MON; -.
DR PRO; PR:P36517; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P36517; 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; IMP:SGD.
DR Gene3D; 6.10.330.20; -; 1.
DR InterPro; IPR038340; MRP-L47_sf.
DR InterPro; IPR010729; Ribosomal_L47_mit.
DR PANTHER; PTHR21183; PTHR21183; 1.
DR Pfam; PF06984; MRP-L47; 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:3060376"
FT CHAIN 15..319
FT /note="54S ribosomal protein L4, mitochondrial"
FT /id="PRO_0000030570"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 168
FT /note="E -> K (in Ref. 1; CAA83057)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 319 AA; 36965 MW; 2DE880E9BFE19BC9 CRC64;
MWKRSFHSQG GPLRARTKFT KPKPKQPVLP KDKIRPPTQL THHSNNLRIT EPIPPTTSNL
RCPDDHPLWQ FFSNKKFIRS ADDLPPSSHI RPWSIPELRH KSFNDLHSLW YNCLREQNVL
ARENHLLKNI VGSTHDEFSE LSNSIRTTMW QIRHVLNERE LAYSASREFL QDESERKKFL
DTLANDYFLN KDIPDDEVAS MLTRFQLAIF GISETIQDNT VDINFIDGIK FLANLKLQRF
KDSNDLISEI SQEPITDVGE SFILFTSDFE PHAVQEACVA IKDLRKSPDN KVPKLDELPT
VRKYLKQLIH ASSVEQATA
