MNP1_YEAST
ID MNP1_YEAST Reviewed; 194 AA.
AC P53163; D6VU73;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=54S ribosomal protein L12, mitochondrial;
DE AltName: Full=Mitochondrial large ribosomal subunit protein bL12m {ECO:0000303|PubMed:24675956};
DE AltName: Full=Mitochondrial-nucleoid protein 1;
DE Flags: Precursor;
GN Name=MNP1; Synonyms=MRPL12; OrderedLocusNames=YGL068W;
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=9290212;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT chromosome VII.";
RL Yeast 13:1077-1090(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 34-48, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=15221522; DOI=10.1007/s00709-004-0040-z;
RA Sato H., Miyakawa I.;
RT "A 22 kDa protein specific for yeast mitochondrial nucleoids is an
RT unidentified putative ribosomal protein encoded in open reading frame
RT YGL068W.";
RL Protoplasma 223:175-182(2004).
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 SUBUNIT.
RX PubMed=16451194; DOI=10.1111/j.1574-6968.2005.00024.x;
RA Gan X., Arita K., Isono S., Kitakawa M., Yoshino K., Yonezawa K., Kato A.,
RA Inoue H., Isono K.;
RT "Identification and comparative analysis of the large subunit mitochondrial
RT ribosomal proteins of Neurospora crassa.";
RL FEMS Microbiol. Lett. 254:157-164(2006).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
RX PubMed=19756047; DOI=10.1038/msb.2009.64;
RA Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H.;
RT "Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals
RT new roles for protein glycosylation in eukaryotes.";
RL Mol. Syst. Biol. 5:308-308(2009).
RN [10]
RP NOMENCLATURE.
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).
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).
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) (PubMed:15221522, PubMed:16451194). Mature yeast 74S mitochondrial
CC ribosomes consist of a small (37S) and a large (54S) subunit. The 37S
CC small subunit contains a 15S ribosomal RNA (15S mt-rRNA) and 34
CC different proteins. The 54S large subunit contains a 21S rRNA (21S mt-
CC rRNA) and 46 different proteins (PubMed:24675956).
CC {ECO:0000269|PubMed:15221522, ECO:0000269|PubMed:16451194,
CC ECO:0000305|PubMed:24675956}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:15221522,
CC ECO:0000269|PubMed:19756047}. 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 -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19756047}.
CC -!- MISCELLANEOUS: Present with 6900 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL12 family.
CC {ECO:0000305}.
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DR EMBL; Z72591; CAA96773.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08034.1; -; Genomic_DNA.
DR PIR; S64075; S64075.
DR RefSeq; NP_011447.1; NM_001180933.1.
DR AlphaFoldDB; P53163; -.
DR SMR; P53163; -.
DR BioGRID; 33179; 67.
DR ComplexPortal; CPX-1602; 54S mitochondrial large ribosomal subunit.
DR DIP; DIP-6428N; -.
DR IntAct; P53163; 8.
DR MINT; P53163; -.
DR STRING; 4932.YGL068W; -.
DR MaxQB; P53163; -.
DR PaxDb; P53163; -.
DR PRIDE; P53163; -.
DR EnsemblFungi; YGL068W_mRNA; YGL068W; YGL068W.
DR GeneID; 852811; -.
DR KEGG; sce:YGL068W; -.
DR SGD; S000003036; MNP1.
DR VEuPathDB; FungiDB:YGL068W; -.
DR eggNOG; KOG1715; Eukaryota.
DR GeneTree; ENSGT00390000000190; -.
DR HOGENOM; CLU_086499_0_1_1; -.
DR InParanoid; P53163; -.
DR OMA; LEDKWGV; -.
DR BioCyc; YEAST:G3O-30572-MON; -.
DR PRO; PR:P53163; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53163; 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:0042645; C:mitochondrial nucleoid; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
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 CDD; cd00387; Ribosomal_L7_L12; 1.
DR Gene3D; 1.20.5.710; -; 1.
DR Gene3D; 3.30.1390.10; -; 1.
DR HAMAP; MF_00368; Ribosomal_L7_L12; 1.
DR InterPro; IPR000206; Ribosomal_L7/12.
DR InterPro; IPR014719; Ribosomal_L7/12_C/ClpS-like.
DR InterPro; IPR013823; Ribosomal_L7/L12_C.
DR InterPro; IPR008932; Ribosomal_L7/L12_oligo.
DR InterPro; IPR036235; Ribosomal_L7/L12_oligo_N_sf.
DR PANTHER; PTHR45987; PTHR45987; 1.
DR Pfam; PF00542; Ribosomal_L12; 1.
DR Pfam; PF16320; Ribosomal_L12_N; 1.
DR SUPFAM; SSF48300; SSF48300; 1.
DR SUPFAM; SSF54736; SSF54736; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Mitochondrion; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; Transit peptide.
FT TRANSIT 1..33
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:15221522"
FT CHAIN 34..194
FT /note="54S ribosomal protein L12, mitochondrial"
FT /id="PRO_0000030460"
FT REGION 101..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 34
FT /note="N -> D (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 194 AA; 20650 MW; D7892681B778B8A9 CRC64;
MSLRILAKRS SSIWMKTRVT PALISPITIT TRFNSTTTTA PSHKDDVRPV DPKISKIVQD
ISQLTLLETS SLINELKTVL NIPEISMPMG GFMAGAAGAG AGNVPSSTGE AGSGAEEEAK
PEAKTVFTVK LDSFDTKTKA KVIKEVKGLL GLSLVEAKKF VEAAPKVLKE NVAKDDAEKI
KKTLEDLGAK VSLE
