ID   RL10A_RAT               Reviewed;         217 AA.
AC   P62907; P52859; P53025;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 138.
DE   RecName: Full=Large ribosomal subunit protein uL1 {ECO:0000305};
DE   AltName: Full=60S ribosomal protein L10a;
GN   Name=Rpl10a;
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 199-213.
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RX   PubMed=8607874; DOI=10.1006/bbrc.1996.0513;
RA   Olvera J., Wool I.G.;
RT   "The primary structure of rat ribosomal protein L10a.";
RL   Biochem. Biophys. Res. Commun. 220:954-957(1996).
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 large ribosomal subunit. The ribosome is a
CC       large ribonucleoprotein complex responsible for the synthesis of
CC       proteins in the cell. {ECO:0000250|UniProtKB:P62906}.
CC   -!- SUBUNIT: Component of the large ribosomal subunit.
CC       {ECO:0000250|UniProtKB:P62906}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P62906}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL1 family.
CC       {ECO:0000305}.
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DR   EMBL; X93352; CAA63732.1; -; mRNA.
DR   EMBL; BC058468; AAH58468.1; -; mRNA.
DR   PIR; JC4677; JC4677.
DR   RefSeq; NP_112327.1; NM_031065.1.
DR   PDB; 7QGG; EM; 2.86 A; Cz=1-217.
DR   PDBsum; 7QGG; -.
DR   AlphaFoldDB; P62907; -.
DR   EMDB; EMD-13954; -.
DR   SMR; P62907; -.
DR   BioGRID; 249602; 4.
DR   IntAct; P62907; 3.
DR   STRING; 10116.ENSRNOP00000000603; -.
DR   iPTMnet; P62907; -.
DR   PhosphoSitePlus; P62907; -.
DR   jPOST; P62907; -.
DR   PaxDb; 10116-ENSRNOP00000000603; -.
DR   Ensembl; ENSRNOT00000000603.8; ENSRNOP00000000603.4; ENSRNOG00000000505.8.
DR   Ensembl; ENSRNOT00055011333; ENSRNOP00055008902; ENSRNOG00055006879.
DR   Ensembl; ENSRNOT00060009332; ENSRNOP00060007008; ENSRNOG00060005618.
DR   Ensembl; ENSRNOT00065051499; ENSRNOP00065042405; ENSRNOG00065029779.
DR   GeneID; 81729; -.
DR   KEGG; rno:81729; -.
DR   UCSC; RGD:620497; rat.
DR   AGR; RGD:620497; -.
DR   CTD; 4736; -.
DR   RGD; 620497; Rpl10a.
DR   eggNOG; KOG1570; Eukaryota.
DR   GeneTree; ENSGT00390000008767; -.
DR   HOGENOM; CLU_062853_3_0_1; -.
DR   InParanoid; P62907; -.
DR   OMA; KGPQNID; -.
DR   OrthoDB; 5095880at2759; -.
DR   PhylomeDB; P62907; -.
DR   TreeFam; TF300791; -.
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:P62907; -.
DR   Proteomes; UP000002494; Chromosome 20.
DR   Bgee; ENSRNOG00000000505; Expressed in thymus and 19 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; 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:0042788; C:polysomal ribosome; ISO:RGD.
DR   GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
DR   GO; GO:0045202; C:synapse; 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:0002181; P:cytoplasmic translation; ISO:RGD.
DR   GO; GO:0000470; P:maturation of LSU-rRNA; IBA:GO_Central.
DR   GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR   GO; GO:0006412; P:translation; IDA:RGD.
DR   CDD; cd00403; Ribosomal_L1; 1.
DR   Gene3D; 3.30.190.20; -; 1.
DR   Gene3D; 3.40.50.790; -; 1.
DR   InterPro; IPR002143; Ribosomal_uL1.
DR   InterPro; IPR023674; Ribosomal_uL1-like.
DR   InterPro; IPR028364; Ribosomal_uL1/biogenesis.
DR   InterPro; IPR016095; Ribosomal_uL1_3-a/b-sand.
DR   InterPro; IPR023673; Ribosomal_uL1_CS.
DR   PANTHER; PTHR23105:SF219; 60S RIBOSOMAL PROTEIN L10A; 1.
DR   PANTHER; PTHR23105; RIBOSOMAL PROTEIN L7AE FAMILY MEMBER; 1.
DR   Pfam; PF00687; Ribosomal_L1; 1.
DR   PIRSF; PIRSF002155; Ribosomal_L1; 1.
DR   SUPFAM; SSF56808; Ribosomal protein L1; 1.
DR   PROSITE; PS01199; RIBOSOMAL_L1; 1.
DR   Genevisible; P62907; RN.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW   Isopeptide bond; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P62906"
FT   CHAIN           2..217
FT                   /note="Large ribosomal subunit protein uL1"
FT                   /id="PRO_0000125822"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P62906"
FT   MOD_RES         11
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P53026"
FT   MOD_RES         91
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P53026"
FT   MOD_RES         106
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62906"
FT   MOD_RES         118
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62906"
FT   CROSSLNK        118
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62906"
FT   CROSSLNK        118
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62906"
FT   CROSSLNK        161
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P62906"
SQ   SEQUENCE   217 AA;  24831 MW;  38F1A31119A751D3 CRC64;
     MSSKVSRDTL YEAVREVLHG NQRKRRKFLE TVELQISLKN YDPQKDKRFS GTVRLKSTPR
     PKFSVCVLGD QQHCDEAKAV DIPHMDIEAL KKLNKNKKLV KKLAKKYDAF LASESLIKQI
     PRILGPGLNK AGKFPSLLTH NENMVAKVDE VKSTIKFQMK KVLCLAVAVG HVKMTDDELV
     YNIHLAVNFL VSLLKKNWQN VRALYIKSTM GKPQRLY
//