ID   RL13A_MACFA             Reviewed;         203 AA.
AC   Q4R8Z2;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=60S ribosomal protein L13a;
GN   Name=RPL13A; ORFNames=QtsA-11103;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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; AB168305; BAE00429.1; -; mRNA.
DR   AlphaFoldDB; Q4R8Z2; -.
DR   SMR; Q4R8Z2; -.
DR   STRING; 9541.XP_005589973.1; -.
DR   PRIDE; Q4R8Z2; -.
DR   eggNOG; KOG3204; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0097452; C:GAIT complex; ISS:UniProtKB.
DR   GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Acetylation; Citrullination; Cytoplasm; Phosphoprotein; Reference proteome;
KW   Ribonucleoprotein; Ribosomal protein; 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_0000231001"
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;  23606 MW;  3E8B24AB6D10D406 CRC64;
     MAEVQVLVLD GRGHLLGRLA AIVAKQVLLG RKVVVVRCEG INISGNFYRN KLKYLAFLRK
     RMNTNPSRGP YHFRAPSRIF WRTVRGMLPH KTKRGQAALD RLKVFDGIPP PYDKKKRMVV
     PAALKVVRLK PTRKFAYLGR LAHEVGWKYQ AVTTTLEEKR KEKAKIHYRK KKQLMRLRKQ
     AEKNVEKKID KYTQVLKTHG LLV