RL13_RAT
ID RL13_RAT Reviewed; 211 AA.
AC P41123;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=60S ribosomal protein L13;
GN Name=Rpl13;
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 PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=8198561; DOI=10.1006/bbrc.1994.1674;
RA Olvera J., Wool I.G.;
RT "The primary structure of rat ribosomal protein L13.";
RL Biochem. Biophys. Res. Commun. 201:102-107(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
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).
CC -!- FUNCTION: Component of the ribosome, a large ribonucleoprotein complex
CC responsible for the synthesis of proteins in the cell. The small
CC ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the
CC encoded message by selecting cognate aminoacyl-transfer RNA (tRNA)
CC molecules. The large subunit (LSU) contains the ribosomal catalytic
CC site termed the peptidyl transferase center (PTC), which catalyzes the
CC formation of peptide bonds, thereby polymerizing the amino acids
CC delivered by tRNAs into a polypeptide chain. The nascent polypeptides
CC leave the ribosome through a tunnel in the LSU and interact with
CC protein factors that function in enzymatic processing, targeting, and
CC the membrane insertion of nascent chains at the exit of the ribosomal
CC tunnel. As part of the LSU, it is probably required for its formation
CC and the maturation of rRNAs. Plays a role in bone development.
CC {ECO:0000250|UniProtKB:P26373}.
CC -!- SUBUNIT: Component of the 60S large ribosomal subunit (LSU).
CC {ECO:0000250|UniProtKB:P26373}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P26373}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL13 family.
CC {ECO:0000305}.
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DR EMBL; X78327; CAA55130.1; -; mRNA.
DR EMBL; BC058143; AAH58143.1; -; mRNA.
DR PIR; JC2368; JC2368.
DR RefSeq; NP_112363.1; NM_031101.1.
DR AlphaFoldDB; P41123; -.
DR SMR; P41123; -.
DR BioGRID; 249637; 4.
DR IntAct; P41123; 8.
DR MINT; P41123; -.
DR STRING; 10116.ENSRNOP00000020635; -.
DR iPTMnet; P41123; -.
DR PhosphoSitePlus; P41123; -.
DR jPOST; P41123; -.
DR PaxDb; P41123; -.
DR PRIDE; P41123; -.
DR Ensembl; ENSRNOT00000020635; ENSRNOP00000020635; ENSRNOG00000015335.
DR GeneID; 81765; -.
DR KEGG; rno:81765; -.
DR UCSC; RGD:621179; rat.
DR CTD; 6137; -.
DR RGD; 621179; Rpl13.
DR eggNOG; KOG3295; Eukaryota.
DR GeneTree; ENSGT00390000007818; -.
DR HOGENOM; CLU_075696_1_0_1; -.
DR InParanoid; P41123; -.
DR OMA; NQQIPHN; -.
DR OrthoDB; 1239434at2759; -.
DR PhylomeDB; P41123; -.
DR TreeFam; TF300073; -.
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:P41123; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000015335; Expressed in ovary and 9 other tissues.
DR Genevisible; P41123; RN.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:RGD.
DR GO; GO:0022626; C:cytosolic ribosome; ISO: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:0001824; P:blastocyst development; ISO:RGD.
DR GO; GO:0060348; P:bone development; ISO:RGD.
DR GO; GO:0097421; P:liver regeneration; IEP:RGD.
DR GO; GO:0006412; P:translation; NAS:UniProtKB.
DR HAMAP; MF_00499; Ribosomal_L13e; 1.
DR InterPro; IPR001380; Ribosomal_L13e.
DR InterPro; IPR018256; Ribosomal_L13e_CS.
DR PANTHER; PTHR11722; PTHR11722; 1.
DR Pfam; PF01294; Ribosomal_L13e; 1.
DR PROSITE; PS01104; RIBOSOMAL_L13E; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Isopeptide bond;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW Ubl conjugation.
FT CHAIN 1..211
FT /note="60S ribosomal protein L13"
FT /id="PRO_0000192921"
FT MOD_RES 16
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26373"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26373"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26373"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26373"
FT MOD_RES 177
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P26373"
FT CROSSLNK 123
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P26373"
FT CROSSLNK 145
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P26373"
FT CROSSLNK 174
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P26373"
FT CROSSLNK 174
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P26373"
FT CROSSLNK 177
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P26373"
FT CONFLICT 56
FT /note="R -> S (in Ref. 1; CAA55130)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 211 AA; 24309 MW; 27BE84B1D810206F CRC64;
MAPSRNGMIL KPHFHKDWQQ RVDTWFNQPA RKIRRRKARQ AKARRIAPRP ASGPIRPIVR
CPTVRYHTKV RAGRGFSLEE LRVAGIHKKM ARTIGISVDP RRRNKSTESL QANVQRLKEY
RSKLILFPRK PSAPKKGDSS AEELKLATQL TGPVMPIRNV YKKEKARAIT EEEKNFKAFA
SLRMARANAR LFGIRAKRAK EAAEQDVEKK K
