ID   RL21_MOUSE              Reviewed;         160 AA.
AC   O09167; Q9CQM8;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2022, sequence version 4.
DT   24-JAN-2024, entry version 135.
DE   RecName: Full=Large ribosomal subunit protein eL21 {ECO:0000305};
DE   AltName: Full=60S ribosomal protein L21 {ECO:0000305};
GN   Name=Rpl21 {ECO:0000312|MGI:MGI:1278340};
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].
RC   STRAIN=C57BL/6J;
RA   Rocha D., Anderson E., Botcherby M., Jordan B.;
RL   Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain, Heart, Kidney, and Mammary gland;
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, 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] {ECO:0007744|PDB:7CPU, ECO:0007744|PDB:7CPV}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.03 ANGSTROMS) OF RIBOSOME, FUNCTION,
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=36517592; DOI=10.1038/s41586-022-05508-0;
RA   Li H., Huo Y., He X., Yao L., Zhang H., Cui Y., Xiao H., Xie W., Zhang D.,
RA   Wang Y., Zhang S., Tu H., Cheng Y., Guo Y., Cao X., Zhu Y., Jiang T.,
RA   Guo X., Qin Y., Sha J.;
RT   "A male germ-cell-specific ribosome controls male fertility.";
RL   Nature 0:0-0(2022).
CC   -!- FUNCTION: Component of the large ribosomal subunit (PubMed:36517592).
CC       The ribosome is a large ribonucleoprotein complex responsible for the
CC       synthesis of proteins in the cell (PubMed:36517592).
CC       {ECO:0000269|PubMed:36517592}.
CC   -!- SUBUNIT: Component of the large ribosomal subunit.
CC       {ECO:0000269|PubMed:36517592}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P46778}. Cytoplasm
CC       {ECO:0000269|PubMed:36517592}. Endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:P49666}. Note=Detected on cytosolic polysomes
CC       (By similarity). Detected in ribosomes that are associated with the
CC       rough endoplasmic reticulum (By similarity).
CC       {ECO:0000250|UniProtKB:P46778, ECO:0000250|UniProtKB:P49666}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL21 family.
CC       {ECO:0000305}.
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DR   EMBL; U93863; AAB52255.1; -; mRNA.
DR   EMBL; AK002940; BAB22470.1; -; mRNA.
DR   EMBL; AK008457; BAB25679.1; -; mRNA.
DR   EMBL; AK018480; BAB31230.1; -; mRNA.
DR   EMBL; AK146440; BAE27174.1; -; mRNA.
DR   EMBL; AK168998; BAE40797.1; -; mRNA.
DR   EMBL; AC124828; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC086904; AAH86904.1; -; mRNA.
DR   EMBL; BC086905; AAH86905.1; -; mRNA.
DR   EMBL; BC086935; AAH86935.1; -; mRNA.
DR   EMBL; BC089582; AAH89582.1; -; mRNA.
DR   EMBL; BC090256; AAH90256.1; -; mRNA.
DR   EMBL; BC094410; AAH94410.1; -; mRNA.
DR   EMBL; BC096404; AAH96404.1; -; mRNA.
DR   EMBL; BC106116; AAI06117.1; -; mRNA.
DR   EMBL; BC138299; AAI38300.1; -; mRNA.
DR   EMBL; BC138300; AAI38301.1; -; mRNA.
DR   CCDS; CCDS19872.1; -.
DR   RefSeq; NP_062621.2; NM_019647.6.
DR   PDB; 6SWA; EM; 3.10 A; R=1-160.
DR   PDB; 7CPU; EM; 2.82 A; LT=1-160.
DR   PDB; 7CPV; EM; 3.03 A; LT=1-160.
DR   PDB; 7LS1; EM; 3.30 A; N2=1-160.
DR   PDB; 7LS2; EM; 3.10 A; N2=1-160.
DR   PDBsum; 6SWA; -.
DR   PDBsum; 7CPU; -.
DR   PDBsum; 7CPV; -.
DR   PDBsum; 7LS1; -.
DR   PDBsum; 7LS2; -.
DR   AlphaFoldDB; O09167; -.
DR   EMDB; EMD-10321; -.
DR   EMDB; EMD-23500; -.
DR   EMDB; EMD-23501; -.
DR   EMDB; EMD-30432; -.
DR   EMDB; EMD-30433; -.
DR   SMR; O09167; -.
DR   ComplexPortal; CPX-5262; 60S cytosolic large ribosomal subunit.
DR   ComplexPortal; CPX-7662; 60S cytosolic large ribosomal subunit, testis-specific variant.
DR   ComplexPortal; CPX-7663; 60S cytosolic large ribosomal subunit, striated muscle variant.
DR   CORUM; O09167; -.
DR   IntAct; O09167; 4.
DR   MINT; O09167; -.
DR   STRING; 10090.ENSMUSP00000041652; -.
DR   GlyGen; O09167; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O09167; -.
DR   MetOSite; O09167; -.
DR   PhosphoSitePlus; O09167; -.
DR   SwissPalm; O09167; -.
DR   EPD; O09167; -.
DR   jPOST; O09167; -.
DR   MaxQB; O09167; -.
DR   PaxDb; 10090-ENSMUSP00000041652; -.
DR   PeptideAtlas; O09167; -.
DR   ProteomicsDB; 255157; -.
DR   ProteomicsDB; 340538; -.
DR   Pumba; O09167; -.
DR   TopDownProteomics; Q9CQM8; -.
DR   DNASU; 19933; -.
DR   Ensembl; ENSMUST00000035983.12; ENSMUSP00000041652.6; ENSMUSG00000041453.13.
DR   Ensembl; ENSMUST00000075453.9; ENSMUSP00000106213.2; ENSMUSG00000041453.13.
DR   Ensembl; ENSMUST00000099272.3; ENSMUSP00000106211.2; ENSMUSG00000041453.13.
DR   GeneID; 19933; -.
DR   KEGG; mmu:19933; -.
DR   AGR; MGI:1278340; -.
DR   CTD; 6144; -.
DR   MGI; MGI:1278340; Rpl21.
DR   VEuPathDB; HostDB:ENSMUSG00000041453; -.
DR   eggNOG; KOG1732; Eukaryota.
DR   GeneTree; ENSGT00950000182922; -.
DR   HOGENOM; CLU_103610_0_1_1; -.
DR   InParanoid; O09167; -.
DR   OMA; INYGDYV; -.
DR   OrthoDB; 2906608at2759; -.
DR   PhylomeDB; O09167; -.
DR   TreeFam; TF314640; -.
DR   Reactome; R-MMU-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR   Reactome; R-MMU-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR   Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   Reactome; R-MMU-72689; Formation of a pool of free 40S subunits.
DR   Reactome; R-MMU-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR   Reactome; R-MMU-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR   Reactome; R-MMU-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR   BioGRID-ORCS; 19933; 8 hits in 40 CRISPR screens.
DR   ChiTaRS; Rpl21; mouse.
DR   PRO; PR:O09167; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; O09167; Protein.
DR   Bgee; ENSMUSG00000041453; Expressed in ovary and 86 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
DR   GO; GO:0022626; C:cytosolic ribosome; ISO:MGI.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0098794; C:postsynapse; NAS:SynGO.
DR   GO; GO:0005840; C:ribosome; ISO:MGI.
DR   GO; GO:0045202; C:synapse; IDA:SynGO.
DR   GO; GO:0003735; F:structural constituent of ribosome; IDA:UniProtKB.
DR   GO; GO:0002181; P:cytoplasmic translation; NAS:ComplexPortal.
DR   Gene3D; 6.10.250.3260; -; 1.
DR   Gene3D; 2.30.30.70; Ribosomal protein L21; 1.
DR   InterPro; IPR001147; Ribosomal_eL21.
DR   InterPro; IPR018259; Ribosomal_eL21_CS.
DR   InterPro; IPR036948; Ribosomal_eL21_sf.
DR   InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR   PANTHER; PTHR20981; 60S RIBOSOMAL PROTEIN L21; 1.
DR   PANTHER; PTHR20981:SF8; 60S RIBOSOMAL PROTEIN L21; 1.
DR   Pfam; PF01157; Ribosomal_L21e; 1.
DR   SUPFAM; SSF50104; Translation proteins SH3-like domain; 1.
DR   PROSITE; PS01171; RIBOSOMAL_L21E; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Endoplasmic reticulum; Reference proteome;
KW   Ribonucleoprotein; Ribosomal protein.
FT   CHAIN           1..160
FT                   /note="Large ribosomal subunit protein eL21"
FT                   /id="PRO_0000149670"
FT   REGION          112..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        131..132
FT                   /note="QP -> HA (in Ref. 1; AAB52255)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   160 AA;  18579 MW;  74F215B18EAFAC22 CRC64;
     MTNTKGKRRG TRYMFSRPFR KHGVVPLATY MRIYKKGDIV DIKGMGTVQK GMPHKCYHGK
     TGRVYNVTQH AVGIIVNKQV KGKILAKRIN VRIEHIKHSK SRDSFLKRVK ENDQKKKEAK
     EKGTWVQLKR QPAPPREAHF VRTNGKEPEL LEPIPYEFMA
//