ID   RL18_CANLF              Reviewed;         188 AA.
AC   D0VWQ3; Q0QEV9;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   22-FEB-2012, sequence version 2.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=Large ribosomal subunit protein eL18 {ECO:0000305};
DE   AltName: Full=Ribosomal protein L18;
GN   Name=RPL18;
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   NUCLEOTIDE SEQUENCE [MRNA] OF 24-187.
RC   TISSUE=Liver;
RX   PubMed=16751257; DOI=10.1093/molbev/msl027;
RA   Kullberg M., Nilsson M.A., Arnason U., Harley E.H., Janke A.;
RT   "Housekeeping genes for phylogenetic analysis of eutherian relationships.";
RL   Mol. Biol. Evol. 23:1493-1503(2006).
RN   [3]
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:Q07020}.
CC   -!- SUBUNIT: Component of the large ribosomal subunit.
CC       {ECO:0000250|UniProtKB:Q07020}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q07020}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q07020}. Rough endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:Q95342}. Note=Detected on cytosolic polysomes
CC       (By similarity). Detected in ribosomes that are associated with the
CC       rough endoplasmic reticulum (By similarity).
CC       {ECO:0000250|UniProtKB:Q07020, ECO:0000250|UniProtKB:Q95342}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL18 family.
CC       {ECO:0000305}.
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DR   EMBL; DQ403035; ABD77168.1; -; mRNA.
DR   RefSeq; NP_001238887.1; NM_001251958.1.
DR   PDB; 4V5Z; EM; 8.70 A; o=1-188.
DR   PDBsum; 4V5Z; -.
DR   AlphaFoldDB; D0VWQ3; -.
DR   SMR; D0VWQ3; -.
DR   STRING; 9615.ENSCAFP00000048715; -.
DR   PaxDb; 9612-ENSCAFP00000005899; -.
DR   Ensembl; ENSCAFT00000006369.5; ENSCAFP00000005899.3; ENSCAFG00000003967.5.
DR   Ensembl; ENSCAFT00000080568.2; ENSCAFP00000056232.1; ENSCAFG00000003967.5.
DR   Ensembl; ENSCAFT00030023061.1; ENSCAFP00030020119.1; ENSCAFG00030012390.1.
DR   Ensembl; ENSCAFT00030023298.1; ENSCAFP00030020312.1; ENSCAFG00030012390.1.
DR   Ensembl; ENSCAFT00040002312.1; ENSCAFP00040001974.1; ENSCAFG00040001231.1.
DR   Ensembl; ENSCAFT00040002342.1; ENSCAFP00040002002.1; ENSCAFG00040001231.1.
DR   Ensembl; ENSCAFT00805001988; ENSCAFP00805001548; ENSCAFG00805001085.
DR   Ensembl; ENSCAFT00845001749.1; ENSCAFP00845001381.1; ENSCAFG00845001007.1.
DR   Ensembl; ENSCAFT00845001766.1; ENSCAFP00845001393.1; ENSCAFG00845001007.1.
DR   GeneID; 476422; -.
DR   KEGG; cfa:476422; -.
DR   CTD; 6141; -.
DR   VEuPathDB; HostDB:ENSCAFG00845001007; -.
DR   VGNC; VGNC:45714; RPL18.
DR   eggNOG; KOG1714; Eukaryota.
DR   GeneTree; ENSGT00390000012976; -.
DR   HOGENOM; CLU_080024_0_0_1; -.
DR   InParanoid; D0VWQ3; -.
DR   OMA; DHTTKQH; -.
DR   OrthoDB; 1122253at2759; -.
DR   TreeFam; TF300202; -.
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; D0VWQ3; -.
DR   Proteomes; UP000002254; Chromosome 1.
DR   Proteomes; UP000694429; Chromosome 1.
DR   Proteomes; UP000694542; Chromosome 1.
DR   Proteomes; UP000805418; Chromosome 1.
DR   Bgee; ENSCAFG00000003967; Expressed in ovary and 50 other cell types or tissues.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; ISS:UniProtKB.
DR   GO; GO:0005791; C:rough endoplasmic reticulum; 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; ISS:UniProtKB.
DR   Gene3D; 3.100.10.10; -; 1.
DR   InterPro; IPR000039; Ribosomal_eL18.
DR   InterPro; IPR021132; Ribosomal_eL18/eL18-A/B/_CS.
DR   InterPro; IPR021131; Ribosomal_uL15/eL18.
DR   InterPro; IPR036227; Ribosomal_uL15/eL18_sf.
DR   PANTHER; PTHR10934; 60S RIBOSOMAL PROTEIN L18; 1.
DR   PANTHER; PTHR10934:SF2; 60S RIBOSOMAL PROTEIN L18; 1.
DR   Pfam; PF17135; Ribosomal_L18; 1.
DR   SUPFAM; SSF52080; Ribosomal proteins L15p and L18e; 1.
DR   PROSITE; PS01106; RIBOSOMAL_L18E; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Endoplasmic reticulum; Isopeptide bond;
KW   Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW   Ubl conjugation.
FT   CHAIN           1..188
FT                   /note="Large ribosomal subunit protein eL18"
FT                   /id="PRO_0000405589"
FT   REGION          151..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        165..188
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         130
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q07020"
FT   MOD_RES         158
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q07020"
FT   CROSSLNK        119
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q07020"
FT   CROSSLNK        164
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q07020"
FT   CONFLICT        30
FT                   /note="K -> M (in Ref. 2; ABD77168)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   188 AA;  21592 MW;  B3FB31DFEA45A32C CRC64;
     MGVDIRHNKD RKVRRKEPKS QDIYLRLLVK LYRFLARRTN STFNQVVLKR LFMSRTNRPP
     LSLSRMIRKM KLPGRENKTA VVVGTITDDV RVQEVPKLKV CALRVSSRAR SRILKAGGKI
     LTFDQLALDS PKGCGTVLLS GPRKGREVYR HFGKAPGTPH SHTKPYVRSK GRKFERARGR
     RASRGYKN
//