ID RL27_MOUSE Reviewed; 136 AA.
AC P61358;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 24-JAN-2024, entry version 171.
DE RecName: Full=Large ribosomal subunit protein eL27 {ECO:0000305};
DE AltName: Full=60S ribosomal protein L27;
GN Name=Rpl27;
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=BALB/cJ;
RA Jin C.G., Chen W.F., Li Y.;
RT "Cloning and characterization of cDNA encoding mouse ribosomal protein
RT L27.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Brain, Small intestine, and Thymus;
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 STRAIN=129, and FVB/N; TISSUE=Colon, 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 [4]
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 [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-27, 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).
RN [6]
RP INTERACTION WITH DHX33.
RX PubMed=26100019; DOI=10.1128/mcb.00315-15;
RA Zhang Y., You J., Wang X., Weber J.;
RT "The DHX33 RNA Helicase Promotes mRNA Translation Initiation.";
RL Mol. Cell. Biol. 35:2918-2931(2015).
RN [7] {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 Required for proper rRNA processing and maturation of 28S and 5.8S
CC rRNAs (By similarity). {ECO:0000250|UniProtKB:A1XQU5,
CC ECO:0000269|PubMed:36517592}.
CC -!- SUBUNIT: Component of the large ribosomal subunit (PubMed:36517592).
CC Interacts with RRP1B (By similarity). Interacts with DHX33
CC (PubMed:26100019). {ECO:0000250|UniProtKB:A1XQU5,
CC ECO:0000269|PubMed:26100019, ECO:0000269|PubMed:36517592}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P61353}. Cytoplasm
CC {ECO:0000269|PubMed:36517592}. Rough endoplasmic reticulum
CC {ECO:0000250|UniProtKB:A1XQU5}. 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:A1XQU5, ECO:0000250|UniProtKB:P61353}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL27 family.
CC {ECO:0000305}.
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DR EMBL; AF214527; AAF25951.1; -; mRNA.
DR EMBL; AK002945; BAB22471.1; -; mRNA.
DR EMBL; AK008120; BAB25475.1; -; mRNA.
DR EMBL; AK088211; BAC40213.1; -; mRNA.
DR EMBL; AK010627; BAB27073.1; -; mRNA.
DR EMBL; AK012566; BAB28321.1; -; mRNA.
DR EMBL; BC024366; AAH24366.1; -; mRNA.
DR EMBL; BC082284; AAH82284.1; -; mRNA.
DR CCDS; CCDS25470.1; -.
DR RefSeq; NP_035419.1; NM_011289.3.
DR RefSeq; XP_017170385.1; XM_017314896.1.
DR PDB; 6SWA; EM; 3.10 A; X=1-136.
DR PDB; 7CPU; EM; 2.82 A; LZ=1-136.
DR PDB; 7CPV; EM; 3.03 A; LZ=1-136.
DR PDB; 7LS1; EM; 3.30 A; T2=1-136.
DR PDB; 7LS2; EM; 3.10 A; T2=1-136.
DR PDBsum; 6SWA; -.
DR PDBsum; 7CPU; -.
DR PDBsum; 7CPV; -.
DR PDBsum; 7LS1; -.
DR PDBsum; 7LS2; -.
DR AlphaFoldDB; P61358; -.
DR EMDB; EMD-10321; -.
DR EMDB; EMD-23500; -.
DR EMDB; EMD-23501; -.
DR EMDB; EMD-30432; -.
DR EMDB; EMD-30433; -.
DR SMR; P61358; -.
DR BioGRID; 202974; 74.
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 IntAct; P61358; 5.
DR MINT; P61358; -.
DR STRING; 10090.ENSMUSP00000102870; -.
DR GlyGen; P61358; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P61358; -.
DR MetOSite; P61358; -.
DR PhosphoSitePlus; P61358; -.
DR SwissPalm; P61358; -.
DR EPD; P61358; -.
DR jPOST; P61358; -.
DR PaxDb; 10090-ENSMUSP00000090305; -.
DR PeptideAtlas; P61358; -.
DR ProteomicsDB; 253309; -.
DR Pumba; P61358; -.
DR TopDownProteomics; P61358; -.
DR DNASU; 19942; -.
DR Ensembl; ENSMUST00000077856.13; ENSMUSP00000090305.6; ENSMUSG00000063316.14.
DR Ensembl; ENSMUST00000107249.8; ENSMUSP00000102870.2; ENSMUSG00000063316.14.
DR GeneID; 19942; -.
DR KEGG; mmu:19942; -.
DR UCSC; uc007low.2; mouse.
DR AGR; MGI:98036; -.
DR CTD; 6155; -.
DR MGI; MGI:98036; Rpl27.
DR VEuPathDB; HostDB:ENSMUSG00000063316; -.
DR eggNOG; KOG3418; Eukaryota.
DR GeneTree; ENSGT00390000010721; -.
DR HOGENOM; CLU_067359_0_1_1; -.
DR InParanoid; P61358; -.
DR OMA; NQWFFTK; -.
DR OrthoDB; 4847090at2759; -.
DR PhylomeDB; P61358; -.
DR TreeFam; TF314648; -.
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; 19942; 26 hits in 72 CRISPR screens.
DR ChiTaRS; Rpl27; mouse.
DR PRO; PR:P61358; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P61358; Protein.
DR Bgee; ENSMUSG00000063316; Expressed in yolk sac and 68 other cell types or tissues.
DR ExpressionAtlas; P61358; baseline and differential.
DR Genevisible; P61358; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR GO; GO:0098556; C:cytoplasmic side of rough endoplasmic reticulum membrane; ISS:UniProtKB.
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:0015934; C:large ribosomal subunit; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0098794; C:postsynapse; NAS:SynGO.
DR GO; GO:0098793; C:presynapse; NAS:SynGO.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:MGI.
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 GO; GO:1904044; P:response to aldosterone; IEA:Ensembl.
DR GO; GO:0006364; P:rRNA processing; ISS:UniProtKB.
DR GO; GO:0140242; P:translation at postsynapse; NAS:SynGO.
DR GO; GO:0140236; P:translation at presynapse; NAS:SynGO.
DR CDD; cd06090; KOW_RPL27; 1.
DR Gene3D; 2.30.30.770; -; 1.
DR InterPro; IPR005824; KOW.
DR InterPro; IPR001141; Ribosomal_eL27.
DR InterPro; IPR018262; Ribosomal_eL27_CS.
DR InterPro; IPR041991; Ribosomal_eL27_KOW.
DR InterPro; IPR038655; Ribosomal_eL27_sf.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR10497; 60S RIBOSOMAL PROTEIN L27; 1.
DR PANTHER; PTHR10497:SF0; 60S RIBOSOMAL PROTEIN L27; 1.
DR Pfam; PF00467; KOW; 1.
DR Pfam; PF01777; Ribosomal_L27e; 1.
DR SMART; SM00739; KOW; 1.
DR SUPFAM; SSF50104; Translation proteins SH3-like domain; 1.
DR PROSITE; PS01107; RIBOSOMAL_L27E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Endoplasmic reticulum;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..136
FT /note="Large ribosomal subunit protein eL27"
FT /id="PRO_0000126078"
FT DOMAIN 5..40
FT /note="KOW"
FT MOD_RES 27
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 93
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P61353"
SQ SEQUENCE 136 AA; 15798 MW; 73F4151495029A32 CRC64;
MGKFMKPGKV VLVLAGRYSG RKAVIVKNID DGTSDRPYSH ALVAGIDRYP RKVTAAMGKK
KIAKRSKIKS FVKVYNYNHL MPTRYSVDIP LDKTVVNKDV FRDPALKRKA RREAKVKFEE
RYKTGKNKWF FQKLRF
//
