RL11_DICDI
ID RL11_DICDI Reviewed; 202 AA.
AC P16168; Q54X48;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=60S ribosomal protein L11;
DE AltName: Full=Vegetative-specific protein V18;
GN Name=rpl11; Synonyms=rpgC, V18; ORFNames=DDB_G0279189;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP PROTEIN SEQUENCE OF 13-27; 62-75 AND 180-202, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RA Bienvenut W.V., Veltman D.M., Insall R.H.;
RL Submitted (JAN-2010) to UniProtKB.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-113, AND DEVELOPMENTAL STAGE.
RC STRAIN=AX3;
RX PubMed=2602140; DOI=10.1093/nar/17.23.9679;
RA Singleton C.K., Manning S.S., Ken R.;
RT "Primary structure and regulation of vegetative specific genes of
RT Dictyostelium discoideum.";
RL Nucleic Acids Res. 17:9679-9692(1989).
CC -!- FUNCTION: Component of the ribosome, a large ribonucleoprotein complex
CC responsible for the synthesis of proteins in the cell. The small
CC ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the
CC encoded message by selecting cognate aminoacyl-transfer RNA (tRNA)
CC molecules. The large subunit (LSU) contains the ribosomal catalytic
CC site termed the peptidyl transferase center (PTC), which catalyzes the
CC formation of peptide bonds, thereby polymerizing the amino acids
CC delivered by tRNAs into a polypeptide chain. The nascent polypeptides
CC leave the ribosome through a tunnel in the LSU and interact with
CC protein factors that function in enzymatic processing, targeting, and
CC the membrane insertion of nascent chains at the exit of the ribosomal
CC tunnel. {ECO:0000250|UniProtKB:P0C0W9}.
CC -!- SUBUNIT: Component of the large ribosomal subunit.
CC {ECO:0000250|UniProtKB:P0C0W9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P0C0W9}. Cytoplasm
CC {ECO:0000250|UniProtKB:P0C0W9}.
CC -!- DEVELOPMENTAL STAGE: Expressed under normal growth conditions and is
CC deactivated upon initiation of development.
CC {ECO:0000269|PubMed:2602140}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL5 family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000030; EAL67743.1; -; Genomic_DNA.
DR EMBL; X15382; CAA33442.1; -; Genomic_DNA.
DR PIR; S07562; S07562.
DR RefSeq; XP_641729.1; XM_636637.1.
DR AlphaFoldDB; P16168; -.
DR SMR; P16168; -.
DR STRING; 44689.DDB0214853; -.
DR PaxDb; P16168; -.
DR EnsemblProtists; EAL67743; EAL67743; DDB_G0279189.
DR GeneID; 8621925; -.
DR KEGG; ddi:DDB_G0279189; -.
DR dictyBase; DDB_G0279189; rpl11.
DR eggNOG; KOG0397; Eukaryota.
DR HOGENOM; CLU_061015_3_0_1; -.
DR InParanoid; P16168; -.
DR OMA; QTETIKW; -.
DR PhylomeDB; P16168; -.
DR Reactome; R-DDI-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-DDI-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-DDI-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-DDI-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-DDI-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-DDI-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR PRO; PR:P16168; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0031012; C:extracellular matrix; HDA:dictyBase.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR Gene3D; 3.30.1440.10; -; 1.
DR InterPro; IPR002132; Ribosomal_L5.
DR InterPro; IPR031309; Ribosomal_L5_C.
DR InterPro; IPR020929; Ribosomal_L5_CS.
DR InterPro; IPR022803; Ribosomal_L5_dom_sf.
DR InterPro; IPR031310; Ribosomal_L5_N.
DR PANTHER; PTHR11994; PTHR11994; 1.
DR Pfam; PF00281; Ribosomal_L5; 1.
DR Pfam; PF00673; Ribosomal_L5_C; 1.
DR PIRSF; PIRSF002161; Ribosomal_L5; 1.
DR SUPFAM; SSF55282; SSF55282; 1.
DR PROSITE; PS00358; RIBOSOMAL_L5; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Nucleus; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT CHAIN 1..202
FT /note="60S ribosomal protein L11"
FT /id="PRO_0000125088"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 108
FT /note="K -> I (in Ref. 3; CAA33442)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="K -> N (in Ref. 3; CAA33442)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 202 AA; 22396 MW; 04222C631360A6AA CRC64;
MSAKAATKNA TKVAVKAPEA TTPVETKKSK KDNVMRGLRI EKLVLNICVG ESGDRLVRAA
KVLEQLTGQT PVYSKARYTV RSFNIRRNEQ IAAHVTVRGE KAAEILEKGL KVREFELRAR
NFSTQGSFGF GIQEHIDLGI KYDPSIGIYG MDFFVVLSRP GFRVAHKKRA GAKVGFQHKI
GKEDAVNWFK TTYDGIVIGG KK
