RM12_MOUSE
ID RM12_MOUSE Reviewed; 201 AA.
AC Q9DB15; B1ATZ3; Q3TKJ3; Q99JS8;
DT 13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 13-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=39S ribosomal protein L12, mitochondrial;
DE Short=L12mt;
DE Short=MRP-L12;
DE Flags: Precursor;
GN Name=Mrpl12; Synonyms=Rpml12;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Liver, and Medulla oblongata;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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 PROTEIN SEQUENCE OF 154-165.
RC TISSUE=Brain;
RA Lubec G., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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).
RN [6]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-153; LYS-165 AND LYS-181, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-141, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: As a component of the mitochondrial large ribosomal subunit,
CC it plays a role in mitochondrial translation. Associates with
CC mitochondrial RNA polymerase to activate transcription.
CC {ECO:0000250|UniProtKB:P52815}.
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 NOA1. {ECO:0000250|UniProtKB:P52815}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P52815}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL12 family.
CC {ECO:0000305}.
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DR EMBL; AK005328; BAB23955.1; -; mRNA.
DR EMBL; AK028168; BAC25787.1; -; mRNA.
DR EMBL; AK134816; BAE22297.1; -; mRNA.
DR EMBL; AK166969; BAE39152.1; -; mRNA.
DR EMBL; AK168337; BAE40275.1; -; mRNA.
DR EMBL; AL669855; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005712; AAH05712.1; -; mRNA.
DR EMBL; BC019565; AAH19565.1; -; mRNA.
DR CCDS; CCDS25737.1; -.
DR RefSeq; NP_081480.2; NM_027204.2.
DR AlphaFoldDB; Q9DB15; -.
DR SMR; Q9DB15; -.
DR BioGRID; 207875; 26.
DR ComplexPortal; CPX-5302; 39S mitochondrial large ribosomal subunit.
DR IntAct; Q9DB15; 3.
DR MINT; Q9DB15; -.
DR STRING; 10090.ENSMUSP00000044417; -.
DR iPTMnet; Q9DB15; -.
DR PhosphoSitePlus; Q9DB15; -.
DR EPD; Q9DB15; -.
DR jPOST; Q9DB15; -.
DR MaxQB; Q9DB15; -.
DR PaxDb; Q9DB15; -.
DR PeptideAtlas; Q9DB15; -.
DR PRIDE; Q9DB15; -.
DR ProteomicsDB; 301602; -.
DR Antibodypedia; 60242; 242 antibodies from 30 providers.
DR DNASU; 56282; -.
DR Ensembl; ENSMUST00000043627; ENSMUSP00000044417; ENSMUSG00000039640.
DR GeneID; 56282; -.
DR KEGG; mmu:56282; -.
DR UCSC; uc007mta.1; mouse.
DR CTD; 6182; -.
DR MGI; MGI:1926273; Mrpl12.
DR VEuPathDB; HostDB:ENSMUSG00000039640; -.
DR eggNOG; KOG1715; Eukaryota.
DR GeneTree; ENSGT00390000000190; -.
DR HOGENOM; CLU_086499_0_2_1; -.
DR InParanoid; Q9DB15; -.
DR OMA; LEDKWGV; -.
DR OrthoDB; 1626139at2759; -.
DR PhylomeDB; Q9DB15; -.
DR TreeFam; TF105997; -.
DR Reactome; R-MMU-5389840; Mitochondrial translation elongation.
DR Reactome; R-MMU-5419276; Mitochondrial translation termination.
DR BioGRID-ORCS; 56282; 27 hits in 74 CRISPR screens.
DR ChiTaRS; Mrpl12; mouse.
DR PRO; PR:Q9DB15; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9DB15; protein.
DR Bgee; ENSMUSG00000039640; Expressed in floor plate of midbrain and 261 other tissues.
DR Genevisible; Q9DB15; 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; ISS:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0006390; P:mitochondrial transcription; ISO:MGI.
DR GO; GO:0032543; P:mitochondrial translation; IC:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
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 Acetylation; Direct protein sequencing; Mitochondrion; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; Transit peptide.
FT TRANSIT 1..46
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 47..201
FT /note="39S ribosomal protein L12, mitochondrial"
FT /id="PRO_0000030459"
FT REGION 37..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 109..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 141
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 153
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 165
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 181
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 8..18
FT /note="RCLWGPRLGLR -> AACGGHGLDSW (in Ref. 1; BAB23955)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 201 AA; 21708 MW; 893BEFB4F154076D CRC64;
MLPVAASRCL WGPRLGLRGA ALRLARQQMP SVCAARQLRS SSHRRSEALA GAPLDNAPKE
YPPKIQQLVQ DIASLTLLEI SDLNELLKKT LKIQDVGLMP MGGMVPGPVS AAAPASEAAE
EEDVPKQKER THFTVRLTEA KPVDKVKLIK EIKNYVQGIN LVQAKKLVES LPQEIKANVA
KAEAEKIKAA LEAVGGTVVL E
