RM51_MOUSE
ID RM51_MOUSE Reviewed; 128 AA.
AC Q9CPY1; Q9CWZ9;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=39S ribosomal protein L51, mitochondrial;
DE Short=L51mt;
DE Short=MRP-L51;
DE AltName: Full=bMRP-64;
DE Short=bMRP64;
DE Flags: Precursor;
GN Name=Mrpl51; Synonyms=Mrp64;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11402041; DOI=10.1074/jbc.m103236200;
RA Suzuki T., Terasaki M., Takemoto-Hori C., Hanada T., Ueda T., Wada A.,
RA Watanabe K.;
RT "Proteomic analysis of the mammalian mitochondrial ribosome. Identification
RT of protein components in the 28S small subunit.";
RL J. Biol. Chem. 276:33181-33195(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart, Mammary gland, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, and Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- SUBUNIT: Component of the mitochondrial ribosome large subunit (39S)
CC which comprises a 16S rRNA and about 50 distinct proteins (By
CC similarity). Interacts with OXA1L (By similarity).
CC {ECO:0000250|UniProtKB:P0C2B6, ECO:0000250|UniProtKB:Q4U2R6}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q4U2R6}.
CC -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein
CC mL51 family. {ECO:0000305}.
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DR EMBL; AB049960; BAB41013.1; -; mRNA.
DR EMBL; AK007256; BAB24918.1; -; mRNA.
DR EMBL; AK010268; BAB26808.1; -; mRNA.
DR EMBL; AK011966; BAB27944.1; -; mRNA.
DR EMBL; AK012126; BAB28048.1; -; mRNA.
DR EMBL; AK012524; BAB28295.1; -; mRNA.
DR EMBL; AK076130; BAC36207.1; -; mRNA.
DR EMBL; BC021535; AAH21535.1; -; mRNA.
DR EMBL; BC094621; AAH94621.1; -; mRNA.
DR EMBL; BC100602; AAI00603.1; -; mRNA.
DR CCDS; CCDS20545.1; -.
DR RefSeq; NP_079871.1; NM_025595.3.
DR AlphaFoldDB; Q9CPY1; -.
DR SMR; Q9CPY1; -.
DR ComplexPortal; CPX-5302; 39S mitochondrial large ribosomal subunit.
DR STRING; 10090.ENSMUSP00000032485; -.
DR EPD; Q9CPY1; -.
DR MaxQB; Q9CPY1; -.
DR PaxDb; Q9CPY1; -.
DR PeptideAtlas; Q9CPY1; -.
DR PRIDE; Q9CPY1; -.
DR ProteomicsDB; 300405; -.
DR Antibodypedia; 22416; 161 antibodies from 24 providers.
DR DNASU; 66493; -.
DR Ensembl; ENSMUST00000032485; ENSMUSP00000032485; ENSMUSG00000030335.
DR GeneID; 66493; -.
DR KEGG; mmu:66493; -.
DR UCSC; uc009dtw.1; mouse.
DR CTD; 51258; -.
DR MGI; MGI:1913743; Mrpl51.
DR VEuPathDB; HostDB:ENSMUSG00000030335; -.
DR eggNOG; KOG4045; Eukaryota.
DR GeneTree; ENSGT00390000018821; -.
DR HOGENOM; CLU_150741_0_0_1; -.
DR InParanoid; Q9CPY1; -.
DR OMA; LIIAPCW; -.
DR OrthoDB; 1197004at2759; -.
DR PhylomeDB; Q9CPY1; -.
DR TreeFam; TF106130; -.
DR Reactome; R-MMU-5389840; Mitochondrial translation elongation.
DR Reactome; R-MMU-5419276; Mitochondrial translation termination.
DR BioGRID-ORCS; 66493; 28 hits in 76 CRISPR screens.
DR ChiTaRS; Mrpl51; mouse.
DR PRO; PR:Q9CPY1; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9CPY1; protein.
DR Bgee; ENSMUSG00000030335; Expressed in hindlimb stylopod muscle and 188 other tissues.
DR Genevisible; Q9CPY1; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; IC:ComplexPortal.
DR GO; GO:0005762; C:mitochondrial large ribosomal subunit; ISS:UniProtKB.
DR GO; GO:0005761; C:mitochondrial ribosome; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:MGI.
DR GO; GO:0032543; P:mitochondrial translation; ISS:UniProtKB.
DR GO; GO:0006412; P:translation; IDA:MGI.
DR InterPro; IPR019373; Ribosomal_L51_mit.
DR PANTHER; PTHR13409; PTHR13409; 1.
DR Pfam; PF10244; MRP-L51; 1.
PE 1: Evidence at protein level;
KW Mitochondrion; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW Transit peptide.
FT TRANSIT 1..31
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 32..128
FT /note="39S ribosomal protein L51, mitochondrial"
FT /id="PRO_0000273083"
FT CONFLICT 8
FT /note="A -> E (in Ref. 2; BAB26808)"
FT /evidence="ECO:0000305"
FT CONFLICT 13
FT /note="L -> M (in Ref. 2; BAB26808)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 128 AA; 15103 MW; EA75B6F3D291D18C CRC64;
MAGSVPWAAS RRLWGWVPSA CRSFSLGVPR LAFVRLTLPP PKVVDRWNEK RALFGVYDNI
GILGNFEKHP KELIKGPVWL RGWRGNELQR CVRKKKFVGN RMFIEDLHNL NKRISYLYKH
FNRHGKYR
