RL19_CANLF
ID RL19_CANLF Reviewed; 196 AA.
AC D0VWQ5;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=60S ribosomal protein L19;
GN Name=RPL19;
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:P84098}.
CC -!- SUBUNIT: Component of the large ribosomal subunit.
CC {ECO:0000250|UniProtKB:P84098}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P84098}.
CC -!- PTM: Citrullinated by PADI4. {ECO:0000250|UniProtKB:P84099}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL19 family.
CC {ECO:0000305}.
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DR RefSeq; NP_001300711.1; NM_001313782.1.
DR PDB; 4V5Z; EM; 8.70 A; 7=98-110, p=1-196.
DR PDBsum; 4V5Z; -.
DR AlphaFoldDB; D0VWQ5; -.
DR SMR; D0VWQ5; -.
DR STRING; 9615.ENSCAFP00000024264; -.
DR PaxDb; D0VWQ5; -.
DR PRIDE; D0VWQ5; -.
DR Ensembl; ENSCAFT00030015754; ENSCAFP00030013737; ENSCAFG00030008501.
DR Ensembl; ENSCAFT00040005165; ENSCAFP00040004441; ENSCAFG00040002691.
DR Ensembl; ENSCAFT00845024224; ENSCAFP00845019031; ENSCAFG00845013552.
DR GeneID; 403682; -.
DR KEGG; cfa:403682; -.
DR CTD; 6143; -.
DR VEuPathDB; HostDB:ENSCAFG00845013552; -.
DR eggNOG; KOG1696; Eukaryota.
DR GeneTree; ENSGT00390000012628; -.
DR InParanoid; D0VWQ5; -.
DR OrthoDB; 1437042at2759; -.
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; D0VWQ5; -.
DR Proteomes; UP000002254; Chromosome 9.
DR Bgee; ENSCAFG00000016493; Expressed in mammary gland and 47 other tissues.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0042788; C:polysomal ribosome; IEA:Ensembl.
DR GO; GO:0045202; C:synapse; 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; IEA:Ensembl.
DR CDD; cd01417; Ribosomal_L19e_E; 1.
DR Gene3D; 1.10.1650.10; -; 1.
DR HAMAP; MF_01475; Ribosomal_L19e; 1.
DR InterPro; IPR035970; 60S_ribosomal_L19/L19e_sf.
DR InterPro; IPR000196; Ribosomal_L19/L19e.
DR InterPro; IPR023638; Ribosomal_L19/L19e_CS.
DR InterPro; IPR015972; Ribosomal_L19/L19e_dom1.
DR InterPro; IPR033935; Ribosomal_L19_euka.
DR InterPro; IPR039547; RPL19.
DR PANTHER; PTHR10722; PTHR10722; 1.
DR Pfam; PF01280; Ribosomal_L19e; 1.
DR SMART; SM01416; Ribosomal_L19e; 1.
DR SUPFAM; SSF48140; SSF48140; 1.
DR PROSITE; PS00526; RIBOSOMAL_L19E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Citrullination; Cytoplasm; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT CHAIN 1..196
FT /note="60S ribosomal protein L19"
FT /id="PRO_0000405590"
FT REGION 157..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 5
FT /note="Citrulline"
FT /evidence="ECO:0000250|UniProtKB:P84099"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P84098"
FT MOD_RES 16
FT /note="Citrulline"
FT /evidence="ECO:0000250|UniProtKB:P84099"
FT MOD_RES 38
FT /note="Citrulline"
FT /evidence="ECO:0000250|UniProtKB:P84099"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P84098"
FT MOD_RES 187
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P84098"
FT CROSSLNK 181
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:P84098"
SQ SEQUENCE 196 AA; 23466 MW; 4AF506393E526216 CRC64;
MSMLRLQKRL ASSVLRCGKK KVWLDPNETN EIANANSRQQ IRKLIKDGLI IRKPVTVHSR
ARCRKNTLAR RKGRHMGIGK RKGTANARMP EKVTWMRRMR ILRRLLRRYR ESKKIDRHMY
HSLYLKVKGN VFKNKRILME HIHKLKADKA RKKLLADQAE ARRSKTKEAR KRREERLQAK
KEEIIKTLSK EEETKK
