RL10L_HUMAN
ID RL10L_HUMAN Reviewed; 214 AA.
AC Q96L21; Q8IUD1;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=60S ribosomal protein L10-like {ECO:0000303|PubMed:12490704};
DE AltName: Full=Large ribosomal subunit protein uL16-like;
GN Name=RPL10L {ECO:0000303|PubMed:12490704, ECO:0000312|HGNC:HGNC:17976};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12490704; DOI=10.1093/nar/gkf696;
RA Uechi T., Maeda N., Tanaka T., Kenmochi N.;
RT "Functional second genes generated by retrotransposition of the X-linked
RT ribosomal protein genes.";
RL Nucleic Acids Res. 30:5369-5375(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=19333399; DOI=10.1371/journal.pone.0005064;
RA Rohozinski J., Anderson M.L., Broaddus R.E., Edwards C.L., Bishop C.E.;
RT "Spermatogenesis associated retrogenes are expressed in the human ovary and
RT ovarian cancers.";
RL PLoS ONE 4:e5064-e5064(2009).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=28502657; DOI=10.1016/j.cub.2017.04.017;
RA Jiang L., Li T., Zhang X., Zhang B., Yu C., Li Y., Fan S., Jiang X.,
RA Khan T., Hao Q., Xu P., Nadano D., Huleihel M., Lunenfeld E., Wang P.J.,
RA Zhang Y., Shi Q.;
RT "RPL10L is required for male meiotic division by compensating for RPL10
RT during meiotic sex chromosome inactivation in mice.";
RL Curr. Biol. 27:1498-1505(2017).
RN [5]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME, FUNCTION,
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=23636399; DOI=10.1038/nature12104;
RA Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
RA Wilson D.N., Beckmann R.;
RT "Structures of the human and Drosophila 80S ribosome.";
RL Nature 497:80-85(2013).
RN [6] {ECO:0007744|PDB:4UG0}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RX PubMed=25901680; DOI=10.1038/nature14427;
RA Khatter H., Myasnikov A.G., Natchiar S.K., Klaholz B.P.;
RT "Structure of the human 80S ribosome.";
RL Nature 520:640-645(2015).
RN [7] {ECO:0007744|PDB:6LQM}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.09 ANGSTROMS), FUNCTION, AND SUBUNIT.
RX PubMed=32669547; DOI=10.1038/s41467-020-17237-x;
RA Liang X., Zuo M.Q., Zhang Y., Li N., Ma C., Dong M.Q., Gao N.;
RT "Structural snapshots of human pre-60S ribosomal particles before and after
RT nuclear export.";
RL Nat. Commun. 11:3542-3542(2020).
RN [8]
RP INVOLVEMENT IN SPGF63, AND VARIANT SPGF63 PRO-86.
RX PubMed=32111475; DOI=10.1016/j.fertnstert.2019.10.029;
RA Tu C., Meng L., Nie H., Yuan S., Wang W., Du J., Lu G., Lin G., Tan Y.Q.;
RT "A homozygous RPL10L missense mutation associated with male factor
RT infertility and severe oligozoospermia.";
RL Fertil. Steril. 113:561-568(2020).
CC -!- FUNCTION: Testis-specific component of the ribosome, which is required
CC for the transition from prophase to metaphase in male meiosis I (By
CC similarity). Compensates for the inactivated X-linked RPL10 paralog
CC during spermatogenesis (PubMed:12490704). The ribosome is a large
CC ribonucleoprotein complex responsible for the synthesis of proteins in
CC the cell (PubMed:23636399, PubMed:25901680, PubMed:32669547). 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 (PubMed:23636399, PubMed:25901680, PubMed:32669547). The
CC large subunit (LSU) contains the ribosomal catalytic site termed the
CC peptidyl transferase center (PTC), which catalyzes the formation of
CC peptide bonds, thereby polymerizing the amino acids delivered by tRNAs
CC into a polypeptide chain (PubMed:23636399, PubMed:25901680,
CC PubMed:32669547). The nascent polypeptides leave the ribosome through a
CC tunnel in the LSU and interact with protein factors that function in
CC enzymatic processing, targeting, and the membrane insertion of nascent
CC chains at the exit of the ribosomal tunnel (PubMed:23636399,
CC PubMed:25901680, PubMed:32669547). {ECO:0000250|UniProtKB:P86048,
CC ECO:0000269|PubMed:12490704, ECO:0000269|PubMed:23636399,
CC ECO:0000269|PubMed:25901680, ECO:0000269|PubMed:32669547}.
CC -!- SUBUNIT: Component of the 60S large ribosomal subunit (LSU).
CC {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:25901680,
CC ECO:0000269|PubMed:32669547}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:23636399,
CC ECO:0000305|PubMed:25901680, ECO:0000305|PubMed:32669547}.
CC -!- TISSUE SPECIFICITY: Almost testis-specific (PubMed:12490704,
CC PubMed:19333399, PubMed:28502657). Also expressed in pre- and
CC postmenopausal ovary (PubMed:19333399). {ECO:0000269|PubMed:12490704,
CC ECO:0000269|PubMed:19333399, ECO:0000269|PubMed:28502657}.
CC -!- DISEASE: Spermatogenic failure 63 (SPGF63) [MIM:619689]: An autosomal
CC recessive male infertility disorder characterized by severe
CC oligozoospermia and reduced progressive sperm motility.
CC {ECO:0000269|PubMed:32111475}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: This gene has no introns in its coding regions, and
CC therefore was most likely produced by retrotransposition of the
CC original X-linked gene during evolution. {ECO:0000269|PubMed:12490704}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL16 family.
CC {ECO:0000305}.
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DR EMBL; AB063605; BAC19833.1; -; Genomic_DNA.
DR EMBL; AB063608; BAC19835.1; -; mRNA.
DR EMBL; BC014310; AAH14310.1; -; mRNA.
DR EMBL; BC066312; AAH66312.1; -; mRNA.
DR CCDS; CCDS32071.1; -.
DR RefSeq; NP_542784.1; NM_080746.2.
DR PDB; 4UG0; EM; -; LI=1-214.
DR PDB; 4V6X; EM; 5.00 A; CI=1-214.
DR PDB; 5LKS; EM; 3.60 A; LI=1-214.
DR PDB; 5T2C; EM; 3.60 A; p=1-214.
DR PDB; 6IP5; EM; 3.90 A; 2D=1-214.
DR PDB; 6IP6; EM; 4.50 A; 2D=1-214.
DR PDB; 6IP8; EM; 3.90 A; 2D=1-214.
DR PDB; 6LQM; EM; 3.09 A; J=1-214.
DR PDB; 6QZP; EM; 2.90 A; LI=2-214.
DR PDB; 6XA1; EM; 2.80 A; LI=2-214.
DR PDB; 6Y0G; EM; 3.20 A; LI=1-214.
DR PDB; 6Y2L; EM; 3.00 A; LI=1-214.
DR PDB; 6Y57; EM; 3.50 A; LI=1-214.
DR PDB; 6Y6X; EM; 2.80 A; LI=2-214.
DR PDB; 6Z6L; EM; 3.00 A; LI=1-214.
DR PDB; 6Z6M; EM; 3.10 A; LI=1-214.
DR PDB; 6Z6N; EM; 2.90 A; LI=1-214.
DR PDB; 6ZM7; EM; 2.70 A; LI=1-214.
DR PDB; 6ZME; EM; 3.00 A; LI=1-214.
DR PDB; 6ZMI; EM; 2.60 A; LI=1-214.
DR PDB; 6ZMO; EM; 3.10 A; LI=1-214.
DR PDB; 7BHP; EM; 3.30 A; LI=1-214.
DR PDBsum; 4UG0; -.
DR PDBsum; 4V6X; -.
DR PDBsum; 5LKS; -.
DR PDBsum; 5T2C; -.
DR PDBsum; 6IP5; -.
DR PDBsum; 6IP6; -.
DR PDBsum; 6IP8; -.
DR PDBsum; 6LQM; -.
DR PDBsum; 6QZP; -.
DR PDBsum; 6XA1; -.
DR PDBsum; 6Y0G; -.
DR PDBsum; 6Y2L; -.
DR PDBsum; 6Y57; -.
DR PDBsum; 6Y6X; -.
DR PDBsum; 6Z6L; -.
DR PDBsum; 6Z6M; -.
DR PDBsum; 6Z6N; -.
DR PDBsum; 6ZM7; -.
DR PDBsum; 6ZME; -.
DR PDBsum; 6ZMI; -.
DR PDBsum; 6ZMO; -.
DR PDBsum; 7BHP; -.
DR AlphaFoldDB; Q96L21; -.
DR SMR; Q96L21; -.
DR BioGRID; 126711; 109.
DR IntAct; Q96L21; 16.
DR MINT; Q96L21; -.
DR STRING; 9606.ENSP00000298283; -.
DR DrugBank; DB02494; (S)-3-phenyllactic acid.
DR DrugBank; DB07374; Anisomycin.
DR DrugBank; DB08437; Puromycin.
DR iPTMnet; Q96L21; -.
DR PhosphoSitePlus; Q96L21; -.
DR SwissPalm; Q96L21; -.
DR BioMuta; RPL10L; -.
DR DMDM; 57013008; -.
DR EPD; Q96L21; -.
DR jPOST; Q96L21; -.
DR MassIVE; Q96L21; -.
DR MaxQB; Q96L21; -.
DR PaxDb; Q96L21; -.
DR PeptideAtlas; Q96L21; -.
DR PRIDE; Q96L21; -.
DR ProteomicsDB; 77142; -.
DR Antibodypedia; 23486; 143 antibodies from 23 providers.
DR DNASU; 140801; -.
DR Ensembl; ENST00000298283.5; ENSP00000298283.3; ENSG00000165496.5.
DR GeneID; 140801; -.
DR KEGG; hsa:140801; -.
DR MANE-Select; ENST00000298283.5; ENSP00000298283.3; NM_080746.3; NP_542784.1.
DR UCSC; uc001wwg.5; human.
DR CTD; 140801; -.
DR DisGeNET; 140801; -.
DR GeneCards; RPL10L; -.
DR HGNC; HGNC:17976; RPL10L.
DR HPA; ENSG00000165496; Tissue enriched (testis).
DR MIM; 619655; gene.
DR MIM; 619689; phenotype.
DR neXtProt; NX_Q96L21; -.
DR OpenTargets; ENSG00000165496; -.
DR PharmGKB; PA34662; -.
DR VEuPathDB; HostDB:ENSG00000165496; -.
DR eggNOG; KOG0857; Eukaryota.
DR GeneTree; ENSGT00390000003897; -.
DR HOGENOM; CLU_084051_0_0_1; -.
DR InParanoid; Q96L21; -.
DR OrthoDB; 1215841at2759; -.
DR PhylomeDB; Q96L21; -.
DR TreeFam; TF300082; -.
DR PathwayCommons; Q96L21; -.
DR Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-HSA-156902; Peptide chain elongation.
DR Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-HSA-192823; Viral mRNA Translation.
DR Reactome; R-HSA-2408557; Selenocysteine synthesis.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-HSA-72764; Eukaryotic Translation Termination.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-9633012; Response of EIF2AK4 (GCN2) to amino acid deficiency.
DR Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR SignaLink; Q96L21; -.
DR SIGNOR; Q96L21; -.
DR BioGRID-ORCS; 140801; 12 hits in 1065 CRISPR screens.
DR GeneWiki; RPL10L; -.
DR GenomeRNAi; 140801; -.
DR Pharos; Q96L21; Tbio.
DR PRO; PR:Q96L21; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q96L21; protein.
DR Bgee; ENSG00000165496; Expressed in left testis and 101 other tissues.
DR Genevisible; Q96L21; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:LIFEdb.
DR GO; GO:0005844; C:polysome; IEA:Ensembl.
DR GO; GO:0005840; C:ribosome; IDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007141; P:male meiosis I; ISS:UniProtKB.
DR GO; GO:0000027; P:ribosomal large subunit assembly; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd01433; Ribosomal_L16_L10e; 1.
DR Gene3D; 3.90.1170.10; -; 1.
DR InterPro; IPR001197; Ribosomal_L10e.
DR InterPro; IPR016180; Ribosomal_L10e/L16.
DR InterPro; IPR036920; Ribosomal_L10e/L16_sf.
DR InterPro; IPR018255; Ribosomal_L10e_CS.
DR PANTHER; PTHR11726; PTHR11726; 1.
DR Pfam; PF00252; Ribosomal_L16; 1.
DR PIRSF; PIRSF005590; Ribosomal_L10; 1.
DR SUPFAM; SSF54686; SSF54686; 1.
DR TIGRFAMs; TIGR00279; uL16_euk_arch; 1.
DR PROSITE; PS01257; RIBOSOMAL_L10E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Differentiation; Disease variant; Meiosis;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Spermatogenesis.
FT CHAIN 1..214
FT /note="60S ribosomal protein L10-like"
FT /id="PRO_0000147106"
FT VARIANT 86
FT /note="H -> P (in SPGF63; reduced protein expression)"
FT /evidence="ECO:0000269|PubMed:32111475"
FT /id="VAR_085860"
SQ SEQUENCE 214 AA; 24519 MW; 9119E2F8C40C2E37 CRC64;
MGRRPARCYR YCKNKPYPKS RFCRGVPDAK IRIFDLGRKK AKVDEFPLGG HMVSDEYEQL
SSEALEAARI CANKYMVKSC GRDGFHMRVR LHPFHVIRIN KMLSCAGADR LQTGMRGAFG
KPQGTVARVH IGQVIMSIRT KLQNEEHVIE ALRRAKFKFP GRQKIHISKK WGFTKFNADE
FEDMVAKKCL IPDGCGVKYV PSHGPLDKWR VLHS
