RL13A_MOUSE
ID RL13A_MOUSE Reviewed; 203 AA.
AC P19253;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=60S ribosomal protein L13a;
DE AltName: Full=Transplantation antigen P198;
DE AltName: Full=Tum-P198 antigen;
GN Name=Rpl13a; Synonyms=P198, Tstap198-7;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1694221; DOI=10.1084/jem.172.1.35;
RA Sibille C., Chomez P., Wildmann C., van Pel A., de Plaen E.,
RA Maryanski J.L., de Bergeyck V., Boon T.;
RT "Structure of the gene of tum- transplantation antigen P198: a point
RT mutation generates a new antigenic peptide.";
RL J. Exp. Med. 172:35-45(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; TISSUE=Mammary gland;
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 PROTEIN SEQUENCE OF 2-12; 54-59; 104-114; 135-140; 149-159 AND 192-197,
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Liver;
RA Kanor S., Bienvenut W.V.;
RL Submitted (OCT-2005) to UniProtKB.
RN [4]
RP SIMILARITY TO L13P.
RX PubMed=8188249; DOI=10.1006/geno.1994.1018;
RA Henikoff S., Henikoff J.G.;
RT "Protein family classification based on searching a database of blocks.";
RL Genomics 19:97-107(1994).
RN [5]
RP FUNCTION, PHOSPHORYLATION AT SER-77, SUBUNIT, RECONSTITUTION OF THE GAIT
RP COMPLEX, AND MUTAGENESIS OF SER-77.
RX PubMed=23071094; DOI=10.1128/mcb.01168-12;
RA Arif A., Chatterjee P., Moodt R.A., Fox P.L.;
RT "Heterotrimeric GAIT complex drives transcript-selective translation
RT inhibition in murine macrophages.";
RL Mol. Cell. Biol. 32:5046-5055(2012).
RN [6]
RP CITRULLINATION AT ARG-59 AND ARG-140.
RX PubMed=24463520; DOI=10.1038/nature12942;
RA Christophorou M.A., Castelo-Branco G., Halley-Stott R.P., Oliveira C.S.,
RA Loos R., Radzisheuskaya A., Mowen K.A., Bertone P., Silva J.C.,
RA Zernicka-Goetz M., Nielsen M.L., Gurdon J.B., Kouzarides T.;
RT "Citrullination regulates pluripotency and histone H1 binding to
RT chromatin.";
RL Nature 507:104-108(2014).
CC -!- FUNCTION: Associated with ribosomes but is not required for canonical
CC ribosome function and has extra-ribosomal functions (By similarity).
CC Component of the GAIT (gamma interferon-activated inhibitor of
CC translation) complex which mediates interferon-gamma-induced
CC transcript-selective translation inhibition in inflammation processes
CC (PubMed:23071094). Upon interferon-gamma activation and subsequent
CC phosphorylation dissociates from the ribosome and assembles into the
CC GAIT complex which binds to stem loop-containing GAIT elements in the
CC 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and
CC suppresses their translation (By similarity). In the GAIT complex
CC interacts with m7G cap-bound eIF4G at or near the eIF3-binding site and
CC blocks the recruitment of the 43S ribosomal complex (By similarity).
CC Involved in methylation of rRNA (By similarity).
CC {ECO:0000250|UniProtKB:P40429, ECO:0000269|PubMed:23071094}.
CC -!- SUBUNIT: Component of the 60S ribosome. Component of the GAIT complex.
CC Interacts with EIF4G1. {ECO:0000250|UniProtKB:P40429}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P40429}.
CC -!- PTM: Phosphorylation at Ser-77 upon interferon-gamma treatment in
CC macrophages involves a DAPK1-DAPK3 kinase cascade and is causing
CC release from the ribosome, association with the GAIT complex and
CC subsequent involvement in transcript-selective translation inhibition.
CC {ECO:0000269|PubMed:23071094}.
CC -!- PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}.
CC -!- POLYMORPHISM: The antigenic allele of P198 differs from the normal
CC allele by a single mutation. The TUM- mutation P198 generates a new
CC epitope recognized by syngeneic T-cells. {ECO:0000269|PubMed:1694221}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL13 family.
CC {ECO:0000305}.
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DR EMBL; X51528; CAA35908.1; -; Genomic_DNA.
DR EMBL; BC082289; AAH82289.1; -; mRNA.
DR CCDS; CCDS21230.1; -.
DR PIR; JL0149; JL0149.
DR RefSeq; NP_033464.2; NM_009438.5.
DR PDB; 6SWA; EM; 3.10 A; N=1-203.
DR PDB; 7LS1; EM; 3.30 A; I2=1-203.
DR PDB; 7LS2; EM; 3.10 A; I2=1-203.
DR PDBsum; 6SWA; -.
DR PDBsum; 7LS1; -.
DR PDBsum; 7LS2; -.
DR AlphaFoldDB; P19253; -.
DR SMR; P19253; -.
DR BioGRID; 204356; 106.
DR ComplexPortal; CPX-5262; 60S cytosolic large ribosomal subunit.
DR CORUM; P19253; -.
DR IntAct; P19253; 6.
DR MINT; P19253; -.
DR STRING; 10090.ENSMUSP00000115722; -.
DR iPTMnet; P19253; -.
DR PhosphoSitePlus; P19253; -.
DR SwissPalm; P19253; -.
DR EPD; P19253; -.
DR jPOST; P19253; -.
DR PaxDb; P19253; -.
DR PeptideAtlas; P19253; -.
DR PRIDE; P19253; -.
DR ProteomicsDB; 253297; -.
DR DNASU; 22121; -.
DR Ensembl; ENSMUST00000150350; ENSMUSP00000115722; ENSMUSG00000074129.
DR GeneID; 22121; -.
DR KEGG; mmu:22121; -.
DR UCSC; uc009gtj.2; mouse.
DR CTD; 23521; -.
DR MGI; MGI:1351455; Rpl13a.
DR VEuPathDB; HostDB:ENSMUSG00000074129; -.
DR eggNOG; KOG3204; Eukaryota.
DR GeneTree; ENSGT00390000010799; -.
DR HOGENOM; CLU_076922_0_0_1; -.
DR InParanoid; P19253; -.
DR OMA; GMLPWKT; -.
DR OrthoDB; 1312756at2759; -.
DR TreeFam; TF300159; -.
DR Reactome; R-MMU-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-MMU-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-MMU-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-MMU-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-MMU-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-MMU-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR BioGRID-ORCS; 22121; 41 hits in 95 CRISPR screens.
DR ChiTaRS; Rpl13a; mouse.
DR PRO; PR:P19253; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P19253; protein.
DR Bgee; ENSMUSG00000074129; Expressed in embryonic brain and 63 other tissues.
DR ExpressionAtlas; P19253; baseline and differential.
DR Genevisible; P19253; MM.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IPI:ComplexPortal.
DR GO; GO:0022626; C:cytosolic ribosome; ISO:MGI.
DR GO; GO:0097452; C:GAIT complex; IDA:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:MGI.
DR GO; GO:0005840; C:ribosome; ISO:MGI.
DR GO; GO:0003729; F:mRNA binding; IDA:MGI.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:MGI.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IDA:UniProtKB.
DR GO; GO:0002181; P:cytoplasmic translation; IC:ComplexPortal.
DR GO; GO:0042592; P:homeostatic process; IMP:MGI.
DR GO; GO:0060425; P:lung morphogenesis; IMP:MGI.
DR GO; GO:0048246; P:macrophage chemotaxis; IMP:MGI.
DR GO; GO:1901194; P:negative regulation of formation of translation preinitiation complex; ISO:MGI.
DR GO; GO:0017148; P:negative regulation of translation; IDA:UniProtKB.
DR GO; GO:0032496; P:response to lipopolysaccharide; IMP:MGI.
DR CDD; cd00392; Ribosomal_L13; 1.
DR Gene3D; 3.90.1180.10; -; 1.
DR HAMAP; MF_01366; Ribosomal_L13; 1.
DR InterPro; IPR005822; Ribosomal_L13.
DR InterPro; IPR023563; Ribosomal_L13_CS.
DR InterPro; IPR005755; Ribosomal_L13_euk/arc.
DR InterPro; IPR036899; Ribosomal_L13_sf.
DR PANTHER; PTHR11545; PTHR11545; 1.
DR Pfam; PF00572; Ribosomal_L13; 1.
DR SUPFAM; SSF52161; SSF52161; 1.
DR TIGRFAMs; TIGR01077; L13_A_E; 1.
DR PROSITE; PS00783; RIBOSOMAL_L13; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Citrullination; Cytoplasm;
KW Direct protein sequencing; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; Translation regulation;
KW Tumor antigen.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.3"
FT CHAIN 2..203
FT /note="60S ribosomal protein L13a"
FT /id="PRO_0000133770"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.3"
FT MOD_RES 59
FT /note="Citrulline"
FT /evidence="ECO:0000269|PubMed:24463520"
FT MOD_RES 77
FT /note="Phosphoserine; by ZIPK/DAPK3"
FT /evidence="ECO:0000269|PubMed:23071094"
FT MOD_RES 140
FT /note="Citrulline"
FT /evidence="ECO:0000269|PubMed:24463520"
FT MOD_RES 191
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P40429"
FT VARIANT 154
FT /note="A -> T (in allele TUM-)"
FT MUTAGEN 77
FT /note="S->A: Loss of interferon-gamma induced
FT phosphorylation."
FT /evidence="ECO:0000269|PubMed:23071094"
SQ SEQUENCE 203 AA; 23464 MW; 967AEAE3362E02CC CRC64;
MAEGQVLVLD GRGHLLGRLA AIVAKQVLLG RKVVVVRCEG INISGNFYRN KLKYLAFLRK
RMNTNPSRGP YHFRAPSRIF WRTVRGMLPH KTKRGQAALE RLKVLDGIPP PYDKKKRMVV
PAALKVVRLK PTRKFAYLGR LAHEVGWKYQ AVTATLEEKR KEKAKMHYRK KKQILRLRKQ
AEKNVEKKIC KFTEVLKTNG LLV
