ID   RL12_CANLF              Reviewed;         165 AA.
AC   E2RR58;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   RecName: Full=Large ribosomal subunit protein uL11 {ECO:0000305};
DE   AltName: Full=60S ribosomal protein L12;
GN   Name=RPL12;
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. Binds directly to 26S ribosomal RNA.
CC       {ECO:0000250|UniProtKB:P30050}.
CC   -!- SUBUNIT: Component of the large ribosomal subunit. Mature ribosomes
CC       consist of a small (40S) and a large (60S) subunit. The 40S subunit
CC       contains about 33 different proteins and 1 molecule of RNA (18S). The
CC       60S subunit contains about 49 different proteins and 3 molecules of RNA
CC       (28S, 5.8S and 5S). {ECO:0000250|UniProtKB:P30050}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P30050}.
CC   -!- PTM: Ubiquitinated at Lys-48 and Lys-83 by RNF14 and RNF25 in response
CC       to ribosome collisions (ribosome stalling).
CC       {ECO:0000250|UniProtKB:P30050}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL11 family.
CC       {ECO:0000305}.
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DR   RefSeq; NP_001238885.1; NM_001251956.1.
DR   PDB; 4V5Z; EM; 8.70 A; i=1-165.
DR   PDBsum; 4V5Z; -.
DR   AlphaFoldDB; E2RR58; -.
DR   SMR; E2RR58; -.
DR   STRING; 9615.ENSCAFP00000050907; -.
DR   PaxDb; 9612-ENSCAFP00000029847; -.
DR   Ensembl; ENSCAFT00000032052.6; ENSCAFP00000029847.4; ENSCAFG00000020136.6.
DR   Ensembl; ENSCAFT00000045165.3; ENSCAFP00000035849.1; ENSCAFG00000020136.6.
DR   Ensembl; ENSCAFT00030016990.1; ENSCAFP00030014847.1; ENSCAFG00030009173.1.
DR   Ensembl; ENSCAFT00030017076.1; ENSCAFP00030014922.1; ENSCAFG00030009173.1.
DR   Ensembl; ENSCAFT00040034270.1; ENSCAFP00040029833.1; ENSCAFG00040018547.1.
DR   Ensembl; ENSCAFT00040034370.1; ENSCAFP00040029926.1; ENSCAFG00040018547.1.
DR   Ensembl; ENSCAFT00805023904; ENSCAFP00805018789; ENSCAFG00805013124.
DR   Ensembl; ENSCAFT00845011528.1; ENSCAFP00845009006.1; ENSCAFG00845006492.1.
DR   Ensembl; ENSCAFT00845011582.1; ENSCAFP00845009049.1; ENSCAFG00845006492.1.
DR   GeneID; 480716; -.
DR   KEGG; cfa:480716; -.
DR   CTD; 6136; -.
DR   VEuPathDB; HostDB:ENSCAFG00845006492; -.
DR   VGNC; VGNC:111704; RPL12.
DR   eggNOG; KOG0886; Eukaryota.
DR   GeneTree; ENSGT00390000006922; -.
DR   HOGENOM; CLU_074237_5_0_1; -.
DR   InParanoid; E2RR58; -.
DR   OrthoDB; 5474609at2759; -.
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; E2RR58; -.
DR   Proteomes; UP000002254; Chromosome 9.
DR   Proteomes; UP000694429; Chromosome 9.
DR   Proteomes; UP000694542; Chromosome 9.
DR   Proteomes; UP000805418; Chromosome 9.
DR   Bgee; ENSCAFG00000020136; Expressed in lymph node and 48 other cell types or tissues.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR   GO; GO:0070180; F:large ribosomal subunit rRNA binding; IBA:GO_Central.
DR   GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR   GO; GO:0006412; P:translation; IBA:GO_Central.
DR   CDD; cd00349; Ribosomal_L11; 1.
DR   Gene3D; 1.10.10.250; Ribosomal protein L11, C-terminal domain; 1.
DR   Gene3D; 3.30.1550.10; Ribosomal protein L11/L12, N-terminal domain; 1.
DR   HAMAP; MF_00736; Ribosomal_uL11; 1.
DR   InterPro; IPR000911; Ribosomal_uL11.
DR   InterPro; IPR020783; Ribosomal_uL11_C.
DR   InterPro; IPR036769; Ribosomal_uL11_C_sf.
DR   InterPro; IPR020785; Ribosomal_uL11_CS.
DR   InterPro; IPR020784; Ribosomal_uL11_N.
DR   InterPro; IPR036796; Ribosomal_uL11_N_sf.
DR   PANTHER; PTHR11661; 60S RIBOSOMAL PROTEIN L12; 1.
DR   PANTHER; PTHR11661:SF38; 60S RIBOSOMAL PROTEIN L12; 1.
DR   Pfam; PF00298; Ribosomal_L11; 1.
DR   Pfam; PF03946; Ribosomal_L11_N; 1.
DR   SMART; SM00649; RL11; 1.
DR   SUPFAM; SSF54747; Ribosomal L11/L12e N-terminal domain; 1.
DR   SUPFAM; SSF46906; Ribosomal protein L11, C-terminal domain; 1.
DR   PROSITE; PS00359; RIBOSOMAL_L11; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Isopeptide bond; Phosphoprotein;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT   CHAIN           1..165
FT                   /note="Large ribosomal subunit protein uL11"
FT                   /id="PRO_0000405586"
FT   MOD_RES         38
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P30050"
FT   MOD_RES         54
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P30050"
FT   MOD_RES         165
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P30050"
FT   CROSSLNK        40
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P30050"
FT   CROSSLNK        48
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P30050"
FT   CROSSLNK        83
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P30050"
SQ   SEQUENCE   165 AA;  17819 MW;  7EFD783A8ED350F9 CRC64;
     MPPKFDPNEI KVVYLRCTGG EVGATSALAP KIGPLGLSPK KVGDDIAKAT GDWKGLRITV
     KLTIQNRQAQ IEVVPSASAL IIKALKEPPR DRKKQKNIKH SGNITFDEIV NIARQMRHRS
     LARELSGTIK EILGTAQSVG CNVDGRHPHD IIDDINSGAV ECPAS
//