RM23_MOUSE
ID RM23_MOUSE Reviewed; 146 AA.
AC O35972; Q78E46;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=39S ribosomal protein L23, mitochondrial;
DE Short=L23mt;
DE Short=MRP-L23;
DE AltName: Full=L23 mitochondrial-related protein;
GN Name=Mrpl23; Synonyms=L23mrp;
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 [GENOMIC DNA / MRNA].
RC STRAIN=129/SvJ; TISSUE=Liver;
RX PubMed=9344651; DOI=10.1006/geno.1997.4961;
RA Zubair M., Hilton K., Saam J.R., Surani M.A., Tilghman S.M., Sasaki H.;
RT "Structure and expression of the mouse L23mrp gene downstream of the
RT imprinted H19 gene: biallelic expression and lack of interaction with the
RT H19 enhancers.";
RL Genomics 45:290-296(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11279069; DOI=10.1074/jbc.m100432200;
RA Suzuki T., Terasaki M., Takemoto-Hori C., Hanada T., Ueda T., Wada A.,
RA Watanabe K.;
RT "Structural compensation for the deficit of rRNA with proteins in the
RT mammalian mitochondrial ribosome. Systematic analysis of protein components
RT of the large ribosomal subunit from mammalian mitochondria.";
RL J. Biol. Chem. 276:21724-21736(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 8-44.
RC STRAIN=C57BL/6J;
RX PubMed=9337391; DOI=10.1007/s003359900583;
RA Greally J.M., Guinness M.E., McGrath J., Zemel S.;
RT "Matrix-attachment regions in the mouse chromosome 7F imprinted domain.";
RL Mamm. Genome 8:805-810(1997).
RN [6]
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).
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:Q16540}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q16540}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL23 family.
CC {ECO:0000305}.
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DR EMBL; U84902; AAC53392.1; -; mRNA.
DR EMBL; U84903; AAC53393.1; -; Genomic_DNA.
DR EMBL; AB049646; BAB40851.1; -; mRNA.
DR EMBL; AK086805; BAC39746.1; -; mRNA.
DR EMBL; BC081460; AAH81460.1; -; mRNA.
DR EMBL; U71209; AAB70459.1; -; Genomic_DNA.
DR CCDS; CCDS22032.1; -.
DR RefSeq; NP_035418.1; NM_011288.1.
DR AlphaFoldDB; O35972; -.
DR SMR; O35972; -.
DR BioGRID; 202972; 3.
DR ComplexPortal; CPX-5302; 39S mitochondrial large ribosomal subunit.
DR DIP; DIP-61654N; -.
DR IntAct; O35972; 1.
DR STRING; 10090.ENSMUSP00000039784; -.
DR iPTMnet; O35972; -.
DR PhosphoSitePlus; O35972; -.
DR SwissPalm; O35972; -.
DR EPD; O35972; -.
DR jPOST; O35972; -.
DR MaxQB; O35972; -.
DR PaxDb; O35972; -.
DR PeptideAtlas; O35972; -.
DR PRIDE; O35972; -.
DR ProteomicsDB; 300398; -.
DR DNASU; 19935; -.
DR Ensembl; ENSMUST00000038675; ENSMUSP00000039784; ENSMUSG00000037772.
DR GeneID; 19935; -.
DR KEGG; mmu:19935; -.
DR UCSC; uc009kny.1; mouse.
DR CTD; 6150; -.
DR MGI; MGI:1196612; Mrpl23.
DR VEuPathDB; HostDB:ENSMUSG00000037772; -.
DR eggNOG; KOG4089; Eukaryota.
DR GeneTree; ENSGT00390000007739; -.
DR HOGENOM; CLU_103097_1_0_1; -.
DR InParanoid; O35972; -.
DR OMA; PGTPGWF; -.
DR OrthoDB; 1495685at2759; -.
DR PhylomeDB; O35972; -.
DR TreeFam; TF105852; -.
DR Reactome; R-MMU-5389840; Mitochondrial translation elongation.
DR Reactome; R-MMU-5419276; Mitochondrial translation termination.
DR BioGRID-ORCS; 19935; 25 hits in 76 CRISPR screens.
DR ChiTaRS; Mrpl23; mouse.
DR PRO; PR:O35972; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; O35972; protein.
DR Bgee; ENSMUSG00000037772; Expressed in yolk sac and 70 other tissues.
DR ExpressionAtlas; O35972; baseline and differential.
DR Genevisible; O35972; MM.
DR GO; GO:0022626; C:cytosolic ribosome; IEA:UniProt.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
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:0003735; F:structural constituent of ribosome; ISO:MGI.
DR GO; GO:0032543; P:mitochondrial translation; IBA:GO_Central.
DR GO; GO:0006412; P:translation; ISO:MGI.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR012678; Ribosomal_L23/L15e_core_dom_sf.
DR InterPro; IPR013025; Ribosomal_L25/23.
DR PANTHER; PTHR12059; PTHR12059; 1.
DR Pfam; PF00276; Ribosomal_L23; 1.
DR SUPFAM; SSF54189; SSF54189; 1.
PE 1: Evidence at protein level;
KW Mitochondrion; Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..146
FT /note="39S ribosomal protein L23, mitochondrial"
FT /id="PRO_0000129485"
FT REGION 108..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 146 AA; 17122 MW; 0116ADE56C9B1553 CRC64;
MARNVLYPLY QLGGPQLRVF RTNFFIQLVR PGTAQPEDTV QFRIPMEMTR VDLRNYLEQI
YNVPVAAVRT RVQHGSNRRR DHKNVRIKKP DYKVAYVQLA HGQTFTFPDL FPEKDPRSPE
PLEEELPQQR QSSDLRCPGI PSWFGL
