RL112_CAEBR
ID RL112_CAEBR Reviewed; 196 AA.
AC A8XJ93;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=60S ribosomal protein L11-2 {ECO:0000305};
GN Name=rpl-11.2 {ECO:0000312|WormBase:CBG14053};
GN ORFNames=CBG14053 {ECO:0000312|WormBase:CBG14053},
GN CBG_14053 {ECO:0000312|EMBL:CAP32718.1};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238 {ECO:0000312|Proteomes:UP000008549};
RN [1] {ECO:0000312|Proteomes:UP000008549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000312|Proteomes:UP000008549};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
RN [2] {ECO:0000305}
RP DISRUPTION PHENOTYPE.
RX PubMed=15687263; DOI=10.1534/genetics.104.040121;
RA Maciejowski J., Ahn J.H., Cipriani P.G., Killian D.J., Chaudhary A.L.,
RA Lee J.I., Voutev R., Johnsen R.C., Baillie D.L., Gunsalus K.C., Fitch D.H.,
RA Hubbard E.J.;
RT "Autosomal genes of autosomal/X-linked duplicated gene pairs and germ-line
RT proliferation in Caenorhabditis elegans.";
RL Genetics 169:1997-2011(2005).
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 -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in few viable
CC embryos and as a result few live progeny and defective growth.
CC {ECO:0000269|PubMed:15687263}.
CC -!- MISCELLANEOUS: There's a functional difference between the two L11-
CC encoding proteins in C.briggsae. rpl-11.1 plays a role in the germline
CC whereas rpl-11.2 has a somatic function. {ECO:0000305|PubMed:15687263}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL5 family.
CC {ECO:0000255|RuleBase:RU003930}.
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DR EMBL; HE600983; CAP32718.1; -; Genomic_DNA.
DR RefSeq; XP_002644280.1; XM_002644234.1.
DR AlphaFoldDB; A8XJ93; -.
DR SMR; A8XJ93; -.
DR STRING; 6238.CBG14053; -.
DR EnsemblMetazoa; CBG14053.1; CBG14053.1; WBGene00034687.
DR GeneID; 8586275; -.
DR KEGG; cbr:CBG_14053; -.
DR CTD; 8586275; -.
DR WormBase; CBG14053; CBP17996; WBGene00034687; Cbr-rpl-11.2.
DR eggNOG; KOG0397; Eukaryota.
DR HOGENOM; CLU_061015_3_0_1; -.
DR InParanoid; A8XJ93; -.
DR OMA; QTETIKW; -.
DR OrthoDB; 1340833at2759; -.
DR Proteomes; UP000008549; Chromosome X.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 3: Inferred from homology;
KW Cytoplasm; Nucleus; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA-binding.
FT CHAIN 1..196
FT /note="60S ribosomal protein L11-2"
FT /id="PRO_0000436902"
SQ SEQUENCE 196 AA; 22776 MW; A5B397B6254FBD92 CRC64;
MGDIEKQTEI REKKARNVMR ELKIQKLCLN ICVGESGDRL TRAAKVLEQL TGQTPVFSKA
RYTVRTFGIR RNEKIAVHCT VRGPKAEEIL EKGLKVKEYE LYKENFSDTG NFGFGVQEHI
DLGIKYDPSI GIYGMDFYVV LDRAGRRIAK RRRAPGRVGP SHRVEREESI KWFQQKYDGI
ILPPKPKVKR TFHRRR