RL15_CANLF
ID RL15_CANLF Reviewed; 204 AA.
AC E2QXF3;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=60S ribosomal protein L15;
GN Name=RPL15;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Boxer;
RX PubMed=16341006; DOI=10.1038/nature04338;
RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E.,
RA Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F.,
RA Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W.,
RA Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S.,
RA Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A.,
RA Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P.,
RA Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P.,
RA Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B.,
RA Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A.,
RA Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M.,
RA Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S.,
RA Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L.,
RA Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C.,
RA Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G.,
RA Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N.,
RA Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A.,
RA Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A.,
RA Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M.,
RA Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L.,
RA LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A.,
RA Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S.,
RA Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T.,
RA Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A.,
RA Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S.,
RA Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M.,
RA Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F.,
RA Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T.,
RA Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C.,
RA Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C.,
RA Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D.,
RA Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H.,
RA Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J.,
RA Zembek L., Zimmer A., Lander E.S.;
RT "Genome sequence, comparative analysis and haplotype structure of the
RT domestic dog.";
RL Nature 438:803-819(2005).
RN [2]
RP STRUCTURE BY ELECTRON MICROSCOPY (8.70 ANGSTROMS).
RX PubMed=18400176; DOI=10.1016/j.str.2008.01.007;
RA Chandramouli P., Topf M., Menetret J.F., Eswar N., Cannone J.J.,
RA Gutell R.R., Sali A., Akey C.W.;
RT "Structure of the mammalian 80S ribosome at 8.7 A resolution.";
RL Structure 16:535-548(2008).
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 RefSeq; NP_001300707.1; NM_001313778.1.
DR RefSeq; XP_862876.1; XM_857783.3.
DR PDB; 4V5Z; EM; 8.70 A; m=1-204.
DR PDBsum; 4V5Z; -.
DR AlphaFoldDB; E2QXF3; -.
DR SMR; E2QXF3; -.
DR STRING; 9615.ENSCAFP00000008630; -.
DR PaxDb; E2QXF3; -.
DR PRIDE; E2QXF3; -.
DR Ensembl; ENSCAFT00030042369; ENSCAFP00030036969; ENSCAFG00030022972.
DR Ensembl; ENSCAFT00040041226; ENSCAFP00040035951; ENSCAFG00040022162.
DR GeneID; 477046; -.
DR KEGG; cfa:477046; -.
DR CTD; 6138; -.
DR eggNOG; KOG1678; Eukaryota.
DR HOGENOM; CLU_080796_0_0_1; -.
DR InParanoid; E2QXF3; -.
DR OMA; KYMQELY; -.
DR OrthoDB; 1181691at2759; -.
DR TreeFam; TF300050; -.
DR Reactome; R-CFA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-CFA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-CFA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-CFA-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-CFA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-CFA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-CFA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR EvolutionaryTrace; E2QXF3; -.
DR Proteomes; UP000002254; Unplaced.
DR Bgee; ENSCAFG00000005764; Expressed in olfactory bulb and 47 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: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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Isopeptide bond; Lipoprotein; Myristate;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW 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_0000405588"
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"
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
