RM39_MOUSE
ID RM39_MOUSE Reviewed; 336 AA.
AC Q9JKF7; A6X954; Q91YK5; Q9D8U5;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=39S ribosomal protein L39, mitochondrial;
DE Short=L39mt;
DE Short=MRP-L39;
GN Name=Mrpl39;
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].
RA Choi D.K., Taylor T.D., Hattori M., Sakaki Y.;
RT "Construction of a transcript map in the LL56-APP region of chromosome
RT 21q21.1-21.2.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pancreas;
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 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Pancreas, and
RC 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).
CC -!- SUBUNIT: Component of the mitochondrial ribosome large subunit (39S)
CC which comprises a 16S rRNA and about 50 distinct proteins.
CC {ECO:0000250|UniProtKB:Q9NYK5}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9NYK5}.
CC -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein
CC mL39 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF44697.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH12274.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH16561.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB25185.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF239728; AAF44697.1; ALT_SEQ; mRNA.
DR EMBL; AK007681; BAB25185.1; ALT_INIT; mRNA.
DR EMBL; CT027693; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466521; EDK98312.1; -; Genomic_DNA.
DR EMBL; BC012274; AAH12274.1; ALT_INIT; mRNA.
DR EMBL; BC016561; AAH16561.1; ALT_INIT; mRNA.
DR CCDS; CCDS57035.1; -.
DR RefSeq; NP_059100.3; NM_017404.4.
DR AlphaFoldDB; Q9JKF7; -.
DR SMR; Q9JKF7; -.
DR BioGRID; 205200; 31.
DR ComplexPortal; CPX-5302; 39S mitochondrial large ribosomal subunit.
DR IntAct; Q9JKF7; 1.
DR STRING; 10090.ENSMUSP00000112283; -.
DR iPTMnet; Q9JKF7; -.
DR PhosphoSitePlus; Q9JKF7; -.
DR EPD; Q9JKF7; -.
DR jPOST; Q9JKF7; -.
DR MaxQB; Q9JKF7; -.
DR PaxDb; Q9JKF7; -.
DR PeptideAtlas; Q9JKF7; -.
DR PRIDE; Q9JKF7; -.
DR ProteomicsDB; 299832; -.
DR Antibodypedia; 6007; 209 antibodies from 23 providers.
DR DNASU; 27393; -.
DR Ensembl; ENSMUST00000116584; ENSMUSP00000112283; ENSMUSG00000022889.
DR GeneID; 27393; -.
DR KEGG; mmu:27393; -.
DR UCSC; uc007zte.2; mouse.
DR CTD; 54148; -.
DR MGI; MGI:1351620; Mrpl39.
DR VEuPathDB; HostDB:ENSMUSG00000022889; -.
DR eggNOG; KOG1637; Eukaryota.
DR GeneTree; ENSGT00940000156271; -.
DR HOGENOM; CLU_071313_0_0_1; -.
DR InParanoid; Q9JKF7; -.
DR OMA; HLKAHHT; -.
DR OrthoDB; 1202682at2759; -.
DR PhylomeDB; Q9JKF7; -.
DR TreeFam; TF300858; -.
DR Reactome; R-MMU-5389840; Mitochondrial translation elongation.
DR Reactome; R-MMU-5419276; Mitochondrial translation termination.
DR BioGRID-ORCS; 27393; 22 hits in 74 CRISPR screens.
DR ChiTaRS; Mrpl39; mouse.
DR PRO; PR:Q9JKF7; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9JKF7; protein.
DR Bgee; ENSMUSG00000022889; Expressed in optic fissure and 259 other tissues.
DR Genevisible; Q9JKF7; 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:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0003735; F:structural constituent of ribosome; ISA:MGI.
DR GO; GO:0000002; P:mitochondrial genome maintenance; TAS:MGI.
DR GO; GO:0032543; P:mitochondrial translation; IC:ComplexPortal.
DR GO; GO:0006412; P:translation; ISA:MGI.
DR Gene3D; 3.10.20.30; -; 1.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR004095; TGS.
DR InterPro; IPR012676; TGS-like.
DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR SUPFAM; SSF55186; SSF55186; 1.
DR SUPFAM; SSF81271; SSF81271; 1.
DR PROSITE; PS51880; TGS; 1.
PE 1: Evidence at protein level;
KW Acetylation; Mitochondrion; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein.
FT CHAIN 1..336
FT /note="39S ribosomal protein L39, mitochondrial"
FT /id="PRO_0000087685"
FT DOMAIN 60..126
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT MOD_RES 123
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYK5"
FT CONFLICT 133
FT /note="K -> R (in Ref. 5; AAH16561)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="V -> L (in Ref. 5; AAH16561)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="L -> F (in Ref. 1; AAF44697)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="E -> G (in Ref. 5; AAH16561)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="S -> F (in Ref. 1; AAF44697)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 336 AA; 38549 MW; 20F03B4A8E874E5D CRC64;
MATAVGRLVL RRPGAGGGAR WRFIATSPAA ELSPTELTEM RNDLFNREKS RQLSLTPRTE
KIEVKHVGKT DPGTVFVMNK NISTPYSCAM HLSEWYCSKS ILALVDGQPW DMYKPLTKSC
EIKFLTFKDP DPKEVNKAYW RSCAMMLGCV IERAFKDDYV VSLVRAPEVP VIAGAFCYDV
TLDKRLDEWM PTKENLRSFT KDAHALIYRD LPFETLDVDA RVALEIFQHN KYKVDFIEEK
ASQNPERIVK LHRIGDFIDV SEGPLIPRTS VCFQYEVSAV HNLNPSQPNL IRRFQGLSLP
THLRAQFTIW DKLVERSRKM VTEDEVRQTE NTESTQ
