RL6_RAT
ID RL6_RAT Reviewed; 298 AA.
AC P21533; Q4QRA9; Q64624; Q68G26;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 5.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=60S ribosomal protein L6;
DE AltName: Full=Neoplasm-related protein C140;
GN Name=Rpl6;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 71-89 AND 122-134.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=8828793; DOI=10.1080/15216549600201471;
RA Chan Y.-L., Wool I.G.;
RT "The primary structure of rat ribosomal protein L6.";
RL Biochem. Mol. Biol. Int. 39:431-438(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Placenta;
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 [3]
RP PROTEIN SEQUENCE OF 2-21.
RX PubMed=398910; DOI=10.1002/jss.400120403;
RA Wittmann-Liebold B., Geissler A.W., Lin A., Wool I.G.;
RT "Sequence of the amino-terminal region of rat liver ribosomal proteins S4,
RT S6, S8, L6, L7a, L18, L27, L30, L37, L37a, and L39.";
RL J. Supramol. Struct. 12:425-433(1979).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 71-298.
RX PubMed=8185817; DOI=10.1677/jme.0.0120085;
RA Ohta K., Endo T., Gunji K., Onaya T.;
RT "Isolation of a cDNA whose expression is markedly increased in malignantly
RT transformed FRTL cells and neoplastic human thyroid tissues.";
RL J. Mol. Endocrinol. 12:85-92(1994).
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. {ECO:0000250|UniProtKB:Q02878}.
CC -!- SUBUNIT: Component of the large ribosomal subunit (By similarity). May
CC bind IPO9 with low affinity (By similarity).
CC {ECO:0000250|UniProtKB:P47911, ECO:0000250|UniProtKB:Q02878}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q02878}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q02878}. Rough endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q2YGT9}. 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:Q02878, ECO:0000250|UniProtKB:Q2YGT9}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL6 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; X87107; CAA60588.1; -; mRNA.
DR EMBL; BC078761; AAH78761.1; -; mRNA.
DR EMBL; BC097295; AAH97295.1; -; mRNA.
DR EMBL; S71021; AAB30818.2; -; mRNA.
DR PIR; S11416; S11416.
DR PIR; T50782; T50782.
DR RefSeq; NP_446423.2; NM_053971.3.
DR RefSeq; XP_006249440.1; XM_006249378.3.
DR AlphaFoldDB; P21533; -.
DR SMR; P21533; -.
DR BioGRID; 250640; 4.
DR IntAct; P21533; 9.
DR MINT; P21533; -.
DR STRING; 10116.ENSRNOP00000038065; -.
DR iPTMnet; P21533; -.
DR PhosphoSitePlus; P21533; -.
DR SwissPalm; P21533; -.
DR jPOST; P21533; -.
DR PaxDb; P21533; -.
DR PRIDE; P21533; -.
DR GeneID; 117042; -.
DR KEGG; rno:117042; -.
DR UCSC; RGD:619826; rat.
DR CTD; 6128; -.
DR RGD; 619826; Rpl6.
DR VEuPathDB; HostDB:ENSRNOG00000025936; -.
DR eggNOG; KOG1694; Eukaryota.
DR HOGENOM; CLU_066767_0_0_1; -.
DR InParanoid; P21533; -.
DR OMA; WAREKKD; -.
DR OrthoDB; 1227453at2759; -.
DR PhylomeDB; P21533; -.
DR Reactome; R-RNO-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-RNO-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-RNO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-RNO-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-RNO-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-RNO-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-RNO-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR PRO; PR:P21533; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000025936; Expressed in ovary and 19 other tissues.
DR Genevisible; P21533; RN.
DR GO; GO:0031672; C:A band; IDA:RGD.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:RGD.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:RGD.
DR GO; GO:0022626; C:cytosolic ribosome; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0042788; C:polysomal ribosome; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:1990932; F:5.8S rRNA binding; IDA:RGD.
DR GO; GO:0003729; F:mRNA binding; IDA:RGD.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:RGD.
DR GO; GO:0000049; F:tRNA binding; IDA:RGD.
DR GO; GO:0002181; P:cytoplasmic translation; ISS:UniProtKB.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
DR CDD; cd13156; KOW_RPL6; 1.
DR Gene3D; 2.30.30.30; -; 1.
DR InterPro; IPR000915; 60S_ribosomal_L6E.
DR InterPro; IPR041997; KOW_RPL6.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR005568; Ribosomal_L6_N.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR10715; PTHR10715; 1.
DR Pfam; PF01159; Ribosomal_L6e; 1.
DR Pfam; PF03868; Ribosomal_L6e_N; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
DR PROSITE; PS01170; RIBOSOMAL_L6E; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Endoplasmic reticulum;
KW Isopeptide bond; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:398910"
FT CHAIN 2..298
FT /note="60S ribosomal protein L6"
FT /id="PRO_0000171012"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..54
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 104
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47911"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02878"
FT MOD_RES 217
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47911"
FT MOD_RES 249
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q02878"
FT CROSSLNK 5
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q02878"
FT CONFLICT 31..35
FT /note="LPAGA -> GAWC (in Ref. 1; CAA60588)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="L -> P (in Ref. 4; AAB30818)"
FT /evidence="ECO:0000305"
FT CONFLICT 191..220
FT /note="LNRVPLRRTHQKFVIATSTKVDISKVKIPK -> STEFLCVGHTRSLSSPPL
FT QKLISARLKFQ (in Ref. 4; AAB30818)"
FT /evidence="ECO:0000305"
FT CONFLICT 264..279
FT /note="DSQILPKIKAVPQLQG -> TRRFCQRSKLSPSSRA (in Ref. 4;
FT AAB30818)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 298 AA; 33562 MW; C92724D0F998503C CRC64;
MAGEKAEKPD KKEQKPAAKK AGGDATAPRA LPAGAVKKSS SKAKKLRKSK PHCSRNPVLV
RGIGRYSRSA MYSRKALYKR KYSAAKTKVE KKKKKEKVLA TVTKTVGGDK NGGTRVVKLR
KMPRYYPTED VPRKLLSHGK KPFSQHVRRL RSSITPGTVL IILTGRHRGK RVVFLKQLGS
GLLLVTGPLA LNRVPLRRTH QKFVIATSTK VDISKVKIPK HLTDAYFKKK PLRKPRHQEG
EIFDTEKEKY EITEQRKADQ KAVDSQILPK IKAVPQLQGY LRSQFSLTNG MYPHKLVF
