ID   RL13A_RAT               Reviewed;         203 AA.
AC   P35427;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=60S ribosomal protein L13a;
GN   Name=Rpl13a;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-12.
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RX   PubMed=8119894; DOI=10.1016/s0021-9258(17)37502-6;
RA   Chan Y.-L., Olvera J., Glueck A., Wool I.G.;
RT   "A leucine zipper-like motif and a basic region-leucine zipper-like element
RT   in rat ribosomal protein L13a. Identification of the tum-transplantation
RT   antigen P198.";
RL   J. Biol. Chem. 269:5589-5594(1994).
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; X68282; CAA48343.1; -; mRNA.
DR   PIR; A53204; A53204.
DR   AlphaFoldDB; P35427; -.
DR   SMR; P35427; -.
DR   IntAct; P35427; 5.
DR   STRING; 10116.ENSRNOP00000027976; -.
DR   iPTMnet; P35427; -.
DR   PhosphoSitePlus; P35427; -.
DR   jPOST; P35427; -.
DR   PaxDb; P35427; -.
DR   PRIDE; P35427; -.
DR   UCSC; RGD:628697; rat.
DR   RGD; 628697; Rpl13a.
DR   eggNOG; KOG3204; Eukaryota.
DR   InParanoid; P35427; -.
DR   PhylomeDB; P35427; -.
DR   Reactome; R-RNO-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR   Reactome; R-RNO-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR   Reactome; R-RNO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   Reactome; R-RNO-72689; Formation of a pool of free 40S subunits.
DR   Reactome; R-RNO-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR   Reactome; R-RNO-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR   Reactome; R-RNO-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR   PRO; PR:P35427; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:RGD.
DR   GO; GO:0022626; C:cytosolic ribosome; ISO:RGD.
DR   GO; GO:0097452; C:GAIT complex; ISS:UniProtKB.
DR   GO; GO:1990904; C:ribonucleoprotein complex; ISO:RGD.
DR   GO; GO:0005840; C:ribosome; IDA:RGD.
DR   GO; GO:0003729; F:mRNA binding; ISO:RGD.
DR   GO; GO:0003735; F:structural constituent of ribosome; ISO:RGD.
DR   GO; GO:0071320; P:cellular response to cAMP; IEP:RGD.
DR   GO; GO:0071480; P:cellular response to gamma radiation; IEP:RGD.
DR   GO; GO:0071346; P:cellular response to interferon-gamma; ISO:RGD.
DR   GO; GO:0071493; P:cellular response to UV-B; IEP:RGD.
DR   GO; GO:0042592; P:homeostatic process; ISO:RGD.
DR   GO; GO:0060425; P:lung morphogenesis; ISO:RGD.
DR   GO; GO:0048246; P:macrophage chemotaxis; ISO:RGD.
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:0032496; P:response to lipopolysaccharide; ISO:RGD.
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   Acetylation; Citrullination; Cytoplasm; Direct protein sequencing;
KW   Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW   Translation regulation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P40429,
FT                   ECO:0000269|PubMed:8119894"
FT   CHAIN           2..203
FT                   /note="60S ribosomal protein L13a"
FT                   /id="PRO_0000133773"
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;  23476 MW;  2EEFA27AF6303727 CRC64;
     MAEGQVLVLD GRSHLLGRLA AIVAKQVLLG RKVVVVRCEG INISGNFYRN KLKYLAFLRK
     RMNTNPSRGP YHFRAPSRIF WRTVRGMLPH KTKRGQAALE RLKVLDGIPP PYDKKKRMVV
     PAALKVVRLK PTRKFAYLGR LAHEVGWKYQ AVTATLEEKR KEKAKIHYRK KKQLLRLRKQ
     AEKNVEKKIC KFTEVLKTNG LLV