RL15_BOVIN
ID RL15_BOVIN Reviewed; 204 AA.
AC Q5EAD6; Q5EA63;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=60S ribosomal protein L15;
GN Name=RPL15;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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:P61313}.
CC -!- SUBUNIT: Component of the large ribosomal subunit. Interacts with IFIT1
CC (via TPR repeats 1-4). {ECO:0000250|UniProtKB:P61313}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P61313}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL15 family.
CC {ECO:0000305}.
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DR EMBL; BT020633; AAX08650.1; -; mRNA.
DR EMBL; BT020706; AAX08723.1; -; mRNA.
DR EMBL; BC102404; AAI02405.1; -; mRNA.
DR RefSeq; NP_001071334.1; NM_001077866.1.
DR RefSeq; XP_005226233.1; XM_005226176.1.
DR AlphaFoldDB; Q5EAD6; -.
DR SMR; Q5EAD6; -.
DR STRING; 9913.ENSBTAP00000044213; -.
DR PaxDb; Q5EAD6; -.
DR PeptideAtlas; Q5EAD6; -.
DR PRIDE; Q5EAD6; -.
DR Ensembl; ENSBTAT00000020729; ENSBTAP00000044213; ENSBTAG00000033080.
DR GeneID; 507151; -.
DR KEGG; bta:507151; -.
DR CTD; 6138; -.
DR VEuPathDB; HostDB:ENSBTAG00000033080; -.
DR eggNOG; KOG1678; Eukaryota.
DR GeneTree; ENSGT00910000144184; -.
DR HOGENOM; CLU_080796_0_0_1; -.
DR InParanoid; Q5EAD6; -.
DR OMA; KYMQELY; -.
DR OrthoDB; 1181691at2759; -.
DR TreeFam; TF300050; -.
DR Reactome; R-BTA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-BTA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-BTA-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-BTA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-BTA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR Proteomes; UP000009136; Chromosome 27.
DR Bgee; ENSBTAG00000033080; Expressed in occipital lobe and 104 other tissues.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR Gene3D; 3.40.1120.10; -; 1.
DR InterPro; IPR024794; Rbsml_L15e_core_dom_sf.
DR InterPro; IPR000439; Ribosomal_L15e.
DR InterPro; IPR020925; Ribosomal_L15e_CS.
DR InterPro; IPR012678; Ribosomal_L23/L15e_core_dom_sf.
DR PANTHER; PTHR11847; PTHR11847; 1.
DR Pfam; PF00827; Ribosomal_L15e; 1.
DR SMART; SM01384; Ribosomal_L15e; 1.
DR SUPFAM; SSF54189; SSF54189; 1.
DR PROSITE; PS01194; RIBOSOMAL_L15E; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Isopeptide bond; Lipoprotein; Myristate; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P61313"
FT CHAIN 2..204
FT /note="60S ribosomal protein L15"
FT /id="PRO_0000240139"
FT REGION 165..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..186
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61314"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61313"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61313"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:P61313"
FT CROSSLNK 83
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P61313"
FT CONFLICT 94
FT /note="F -> L (in Ref. 1; AAX08723)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 204 AA; 24146 MW; A6E3AD1A76C9506F CRC64;
MGAYKYIQEL WRKKQSDVMR FLLRVRCWQY RQLSALHRAP RPTRPDKARR LGYKAKQGYV
IYRIRVRRGG RKRPVPKGAT YGKPVHHGVN QLKFARSLQS VAEERAGRHC GALRVLNSYW
VGEDSTYKFF EVILIDPFHK AIRRNPDTQW ITKPVHKHRE MRGLTSAGRK SRGLGKGHKF
HHTIGGSRRA AWRRRNTLQL HRYR
