RL13A_PONAB
ID RL13A_PONAB Reviewed; 203 AA.
AC Q5RA38;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=60S ribosomal protein L13a;
GN Name=RPL13A;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; CR859183; CAH91372.1; -; mRNA.
DR RefSeq; NP_001125810.1; NM_001132338.2.
DR AlphaFoldDB; Q5RA38; -.
DR SMR; Q5RA38; -.
DR STRING; 9601.ENSPPYP00000007711; -.
DR GeneID; 100172738; -.
DR KEGG; pon:100172738; -.
DR CTD; 23521; -.
DR eggNOG; KOG3204; Eukaryota.
DR InParanoid; Q5RA38; -.
DR OrthoDB; 1312756at2759; -.
DR Proteomes; UP000001595; 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_0000133772"
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; 23518 MW; 2B5AEF5847387F06 CRC64;
MAEVQVLVLD GRGHLLGRLA AIVAKQVLLG RKVVVVRCEG INISGNFYRN KLKYLAFLRK
RMNTSPSRGP YHFRAPSRIF WRTVRGMLPH KTKRGQAALD RLKVFDGIPP PYDKKKRMVV
PAALKVVRLK PTRKFAYLGR LAHEVGWKYQ AVTATLEEKR KEKAKIHYRK KKQLVRLRKQ
AEKNVEKKID KYTEVLKTHG LLV