ID   RL27A_RAT               Reviewed;         148 AA.
AC   P18445;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=60S ribosomal protein L27a;
GN   Name=Rpl27a;
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 2-16.
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RX   PubMed=2207170; DOI=10.1016/0167-4781(90)90143-p;
RA   Wool I.G., Chan Y.-L., Paz V., Olvera J.;
RT   "The primary structure of rat ribosomal proteins: the amino acid sequences
RT   of L27a and L28 and corrections in the sequences of S4 and S12.";
RL   Biochim. Biophys. Acta 1050:69-73(1990).
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:P46776}.
CC   -!- SUBUNIT: Component of the large ribosomal subunit.
CC       {ECO:0000250|UniProtKB:P46776}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P46776}.
CC   -!- PTM: Hydroxylated on His-39 by MINA. {ECO:0000250|UniProtKB:P46776}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL15 family.
CC       {ECO:0000305}.
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DR   EMBL; X52733; CAA36947.1; -; mRNA.
DR   PIR; S13071; R5RTLA.
DR   RefSeq; NP_001099760.1; NM_001106290.1.
DR   AlphaFoldDB; P18445; -.
DR   SMR; P18445; -.
DR   BioGRID; 254258; 2.
DR   IntAct; P18445; 5.
DR   STRING; 10116.ENSRNOP00000019247; -.
DR   iPTMnet; P18445; -.
DR   PhosphoSitePlus; P18445; -.
DR   jPOST; P18445; -.
DR   PaxDb; P18445; -.
DR   PRIDE; P18445; -.
DR   GeneID; 293418; -.
DR   KEGG; rno:293418; -.
DR   UCSC; RGD:1309771; rat.
DR   CTD; 6157; -.
DR   RGD; 1309771; Rpl27a.
DR   eggNOG; KOG1742; Eukaryota.
DR   HOGENOM; CLU_109163_1_0_1; -.
DR   InParanoid; P18445; -.
DR   OMA; WGRVGQH; -.
DR   OrthoDB; 1445443at2759; -.
DR   PhylomeDB; P18445; -.
DR   TreeFam; TF313742; -.
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:P18445; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000014214; Expressed in spleen and 19 other tissues.
DR   Genevisible; P18445; RN.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:RGD.
DR   GO; GO:0022626; C:cytosolic ribosome; ISO:RGD.
DR   GO; GO:0003735; F:structural constituent of ribosome; ISO:RGD.
DR   GO; GO:0006412; P:translation; ISO:RGD.
DR   Gene3D; 4.10.990.10; -; 1.
DR   HAMAP; MF_01341; Ribosomal_L15; 1.
DR   InterPro; IPR036227; L18e/L15P_sf.
DR   InterPro; IPR027386; Rbsml_prot_L15/27a_N.
DR   InterPro; IPR030878; Ribosomal_L15.
DR   InterPro; IPR001196; Ribosomal_L15_CS.
DR   InterPro; IPR021131; Ribosomal_L18e/L15P.
DR   Pfam; PF00828; Ribosomal_L27A; 1.
DR   SUPFAM; SSF52080; SSF52080; 1.
DR   PROSITE; PS00475; RIBOSOMAL_L15; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; Hydroxylation;
KW   Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2207170"
FT   CHAIN           2..148
FT                   /note="60S ribosomal protein L27a"
FT                   /id="PRO_0000104884"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..35
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         39
FT                   /note="(3S)-3-hydroxyhistidine"
FT                   /evidence="ECO:0000250|UniProtKB:P46776"
FT   MOD_RES         47
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P46776"
FT   MOD_RES         55
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P46776"
FT   MOD_RES         68
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46776"
FT   MOD_RES         110
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P46776"
SQ   SEQUENCE   148 AA;  16618 MW;  9CFB1FA50E3504DD CRC64;
     MPSRLRKTRK LRGHVSHGHG RIGKHRKHPG GRGNAGGMHH HRINFDKYHP GYFGKVGMRH
     YHLKRNQSFC PTVNLDKLWT LVSEQTRVNA AKNKNGVAPI IDVVRSGYYK VLGKGKLPKQ
     PVIVKAKFFS RRAEEKIKGV GGACVLVA