RL13A_CANLF
ID RL13A_CANLF Reviewed; 203 AA.
AC Q9XSU0;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 2.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=60S ribosomal protein L13a;
GN Name=RPL13A;
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 [MRNA] OF 1-129.
RC STRAIN=Beagle; TISSUE=Pancreas;
RA Staten N.R.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-143.
RC TISSUE=Thyroid;
RX PubMed=10964405; DOI=10.1006/abio.2000.4674;
RA Pichon B., Mercan D., Pouillon V., Christophe-Hobertus C., Christophe D.;
RT "A method for the large-scale cloning of nuclear proteins and nuclear
RT targeting sequences on a functional basis.";
RL Anal. Biochem. 284:231-239(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 16-203.
RC STRAIN=Beagle; TISSUE=Jejunum;
RA Schlueter T., Hermanns J., Weindel M., Schuette D., Kranz H., Henrich J.,
RA Loebbert R.;
RT "Dog arrayTAG cDNA clone collection.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
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: Associated with ribosomes but is not required for canonical
CC ribosome function and has extra-ribosomal functions. Component of the
CC GAIT (gamma interferon-activated inhibitor of translation) complex
CC which mediates interferon-gamma-induced transcript-selective
CC translation inhibition in inflammation processes. Upon interferon-gamma
CC activation and subsequent phosphorylation dissociates from the ribosome
CC and assembles into the GAIT complex which binds to stem loop-containing
CC GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as
CC ceruplasmin) and suppresses their translation. 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. Involved in
CC methylation of rRNA. {ECO:0000250|UniProtKB:P40429}.
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:0000250|UniProtKB:P19253}.
CC -!- PTM: Citrullinated by PADI4. {ECO:0000250|UniProtKB:P19253}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL13 family.
CC {ECO:0000305}.
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DR EMBL; DN325227; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AJ388525; CAB46827.1; -; mRNA.
DR EMBL; CO660712; -; NOT_ANNOTATED_CDS; mRNA.
DR PDB; 4V5Z; EM; 8.70 A; j=1-203.
DR PDBsum; 4V5Z; -.
DR AlphaFoldDB; Q9XSU0; -.
DR SMR; Q9XSU0; -.
DR STRING; 9612.ENSCAFP00000005417; -.
DR PaxDb; Q9XSU0; -.
DR PRIDE; Q9XSU0; -.
DR eggNOG; KOG3204; Eukaryota.
DR InParanoid; Q9XSU0; -.
DR EvolutionaryTrace; Q9XSU0; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0097452; C:GAIT complex; ISS:UniProtKB.
DR GO; GO:0005840; C:ribosome; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:1901194; P:negative regulation of formation of translation preinitiation complex; ISS:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; ISS:UniProtKB.
DR GO; GO:0006412; P:translation; IEA:InterPro.
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; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW Translation regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P40429"
FT CHAIN 2..203
FT /note="60S ribosomal protein L13a"
FT /id="PRO_0000405587"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P40429"
FT MOD_RES 59
FT /note="Citrulline"
FT /evidence="ECO:0000250|UniProtKB:P19253"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40429"
FT MOD_RES 140
FT /note="Citrulline"
FT /evidence="ECO:0000250|UniProtKB:P19253"
FT MOD_RES 191
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P40429"
SQ SEQUENCE 203 AA; 23499 MW; 42C3DCBA129ED7FA CRC64;
MAEGQVLVLD GRGHLLGRLA AIVAKQVLLG RKVVVVRCEG INISGNFYRN KLNYLAFLRK
RMNTNPSRGP YDFRAPSRIF WRTVRGMLPH KTKRGQAALD RLKVFDGIPP PYDKKKRMVV
PAALKVVRLK PTRKFAYLGR LAHEVGWKYQ AVTATLEEKR KEKAKIHYRK KKQLMRLRKQ
AEKNVEKKID KYTEVLKTHG LLV
