RL7_MOUSE
ID RL7_MOUSE Reviewed; 270 AA.
AC P14148; Q80UR0;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=60S ribosomal protein L7;
GN Name=Rpl7;
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].
RX PubMed=2365680; DOI=10.1016/s0021-9258(19)38420-0;
RA Meyuhas O., Klein A.;
RT "The mouse ribosomal protein L7 gene. Its primary structure and functional
RT analysis of the promoter region.";
RL J. Biol. Chem. 265:11465-11473(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=SWR/J;
RA Zheng Y.-M., Su P., Wang J.X., Basu A., Bhat K., Carter R., Avadhani N.G.;
RT "Immunochemical and structural similarity between a mouse cytochrome
RT oxidase subunit and ribosomal protein L7.";
RL Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Hematopoietic stem cell, 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 NUCLEOTIDE SEQUENCE [MRNA] OF 117-270.
RX PubMed=8441630; DOI=10.1093/nar/21.2.223;
RA Hemmerich P., von Mikecz A., Neumann F., Soezen O., Wolff-Vorbeck G.,
RA Zoebelein R., Krawinkel U.;
RT "Structural and functional properties of ribosomal protein L7 from humans
RT and rodents.";
RL Nucleic Acids Res. 21:223-231(1993).
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-149, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
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 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).
CC -!- FUNCTION: Component of the large ribosomal subunit. The ribosome is a
CC large ribonucleoprotein complex responsible for the synthesis of
CC proteins in the cell. Binds to G-rich structures in 28S rRNA and in
CC mRNAs. Plays a regulatory role in the translation apparatus; inhibits
CC cell-free translation of mRNAs. {ECO:0000250|UniProtKB:P18124}.
CC -!- SUBUNIT: Component of the large ribosomal subunit (By similarity).
CC Homodimer (By similarity). Interacts with DHX33 (PubMed:26100019).
CC {ECO:0000250|UniProtKB:P18124, ECO:0000269|PubMed:26100019}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P18124}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL30 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M29015; AAA40069.1; -; Genomic_DNA.
DR EMBL; M29016; AAA40070.1; -; mRNA.
DR EMBL; M85235; AAA40064.1; -; mRNA.
DR EMBL; BC025909; AAH25909.1; -; mRNA.
DR EMBL; BC051261; AAH51261.1; -; mRNA.
DR EMBL; X57960; CAA41028.1; -; mRNA.
DR EMBL; X57961; CAA41029.1; -; mRNA.
DR CCDS; CCDS14829.1; -.
DR PIR; A37055; A37055.
DR RefSeq; NP_035421.2; NM_011291.5.
DR PDB; 6SWA; EM; 3.10 A; F=1-270.
DR PDB; 7LS1; EM; 3.30 A; A1=1-270.
DR PDB; 7LS2; EM; 3.10 A; A1=1-270.
DR PDBsum; 6SWA; -.
DR PDBsum; 7LS1; -.
DR PDBsum; 7LS2; -.
DR AlphaFoldDB; P14148; -.
DR SMR; P14148; -.
DR BioGRID; 202988; 95.
DR ComplexPortal; CPX-5262; 60S cytosolic large ribosomal subunit.
DR CORUM; P14148; -.
DR IntAct; P14148; 7.
DR MINT; P14148; -.
DR STRING; 10090.ENSMUSP00000071616; -.
DR iPTMnet; P14148; -.
DR PhosphoSitePlus; P14148; -.
DR SwissPalm; P14148; -.
DR EPD; P14148; -.
DR jPOST; P14148; -.
DR PaxDb; P14148; -.
DR PeptideAtlas; P14148; -.
DR PRIDE; P14148; -.
DR ProteomicsDB; 299824; -.
DR TopDownProteomics; P14148; -.
DR Antibodypedia; 25169; 259 antibodies from 30 providers.
DR DNASU; 19989; -.
DR Ensembl; ENSMUST00000058437; ENSMUSP00000071616; ENSMUSG00000043716.
DR GeneID; 19989; -.
DR KEGG; mmu:19989; -.
DR UCSC; uc007ajl.3; mouse.
DR CTD; 6129; -.
DR MGI; MGI:98073; Rpl7.
DR VEuPathDB; HostDB:ENSMUSG00000043716; -.
DR eggNOG; KOG3184; Eukaryota.
DR GeneTree; ENSGT00950000182878; -.
DR HOGENOM; CLU_055156_0_2_1; -.
DR InParanoid; P14148; -.
DR OMA; TKKTNHF; -.
DR OrthoDB; 1544778at2759; -.
DR PhylomeDB; P14148; -.
DR TreeFam; TF300740; -.
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; 19989; 26 hits in 67 CRISPR screens.
DR ChiTaRS; Rpl7; mouse.
DR PRO; PR:P14148; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P14148; protein.
DR Bgee; ENSMUSG00000043716; Expressed in epiblast (generic) and 65 other tissues.
DR ExpressionAtlas; P14148; baseline and differential.
DR Genevisible; P14148; MM.
DR GO; GO:0031672; C:A band; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:MGI.
DR GO; GO:0022626; C:cytosolic ribosome; ISO:MGI.
DR GO; GO:0005844; C:polysome; IDA:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
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:0008097; F:5S rRNA binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0003729; F:mRNA binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:MGI.
DR GO; GO:0002181; P:cytoplasmic translation; IC:ComplexPortal.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; ISO:MGI.
DR GO; GO:0006364; P:rRNA processing; ISO:MGI.
DR GO; GO:0006412; P:translation; IC:MGI.
DR CDD; cd01657; Ribosomal_L7_archeal_euk; 1.
DR Gene3D; 3.30.1390.20; -; 1.
DR InterPro; IPR036919; L30_ferredoxin-like_sf.
DR InterPro; IPR018038; Ribosomal_L30_CS.
DR InterPro; IPR016082; Ribosomal_L30_ferredoxin-like.
DR InterPro; IPR012988; Ribosomal_L30_N.
DR InterPro; IPR039699; Ribosomal_L7/L30.
DR InterPro; IPR005998; Ribosomal_L7_euk.
DR InterPro; IPR035808; Ribosomal_L7_euk_arc.
DR PANTHER; PTHR11524; PTHR11524; 1.
DR Pfam; PF00327; Ribosomal_L30; 1.
DR Pfam; PF08079; Ribosomal_L30_N; 1.
DR SUPFAM; SSF55129; SSF55129; 1.
DR TIGRFAMs; TIGR01310; uL30_euk; 1.
DR PROSITE; PS00634; RIBOSOMAL_L30; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Phosphoprotein; Reference proteome;
KW Repeat; Ribonucleoprotein; Ribosomal protein; RNA-binding.
FT CHAIN 1..270
FT /note="60S ribosomal protein L7"
FT /id="PRO_0000104634"
FT REPEAT 7..18
FT /note="1"
FT REPEAT 19..29
FT /note="2"
FT REPEAT 30..40
FT /note="3"
FT REPEAT 41..52
FT /note="4"
FT REPEAT 53..64
FT /note="5"
FT REPEAT 65..76
FT /note="6"
FT REGION 7..76
FT /note="6 X 12 AA tandem repeats"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P18124"
FT MOD_RES 39
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P18124"
FT MOD_RES 146
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P18124"
FT MOD_RES 149
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 161
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P18124"
FT CONFLICT 25..29
FT /note="GPKTL -> WAKNS (in Ref. 2; AAA40064)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="L -> R (in Ref. 2; AAA40064)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="L -> V (in Ref. 2; AAA40064)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="R -> G (in Ref. 3; AAH51261)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="R -> Q (in Ref. 1; AAA40069)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 270 AA; 31420 MW; D006EDFB8CF95EFD CRC64;
MEAVPEKKKK VATVPGTLKK KVPAGPKTLK KKVPAVPETL KKKRRNFAEL KVKRLRKKFA
LKTLRKARRK LIYEKAKHYH KEYRQMYRTE IRMARMARKA GNFYVPAEPK LAFVIRIRGI
NGVSPKVRKV LQLLRLRQIF NGTFVKLNKA SINMLRIVEP YIAWGYPNLK SVNELIYKRG
YGKINKKRIA LTDNSLIARS LGKFGIICME DLIHEIYTVG KRFKEANNFL WPFKLSSPRG
GMKKKTTHFV EGGDAGNRED QINRLIRRMN
