ID   RL1D1_BOVIN             Reviewed;         482 AA.
AC   A4FV97;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Ribosomal L1 domain-containing protein 1;
GN   Name=RSL1D1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Basal ganglia;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Regulates cellular senescence through inhibition of PTEN
CC       translation. Acts as a pro-apoptotic regulator in response to DNA
CC       damage. {ECO:0000250|UniProtKB:O76021}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000250|UniProtKB:O76021}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL1 family.
CC       Highly divergent. {ECO:0000305}.
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DR   EMBL; BC123897; AAI23898.1; -; mRNA.
DR   AlphaFoldDB; A4FV97; -.
DR   SMR; A4FV97; -.
DR   STRING; 9913.ENSBTAP00000019422; -.
DR   PaxDb; A4FV97; -.
DR   PeptideAtlas; A4FV97; -.
DR   PRIDE; A4FV97; -.
DR   Ensembl; ENSBTAT00000019422; ENSBTAP00000019422; ENSBTAG00000014588.
DR   VEuPathDB; HostDB:ENSBTAG00000014588; -.
DR   VGNC; VGNC:34180; RSL1D1.
DR   eggNOG; KOG1685; Eukaryota.
DR   GeneTree; ENSGT00440000038603; -.
DR   HOGENOM; CLU_026457_0_0_1; -.
DR   InParanoid; A4FV97; -.
DR   OMA; KNEAIWL; -.
DR   TreeFam; TF354254; -.
DR   Proteomes; UP000009136; Chromosome 25.
DR   Bgee; ENSBTAG00000014588; Expressed in oocyte and 106 other tissues.
DR   ExpressionAtlas; A4FV97; baseline and differential.
DR   GO; GO:0030686; C:90S preribosome; IBA:GO_Central.
DR   GO; GO:0005694; C:chromosome; IEA:Ensembl.
DR   GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR   GO; GO:0003730; F:mRNA 3'-UTR binding; IEA:Ensembl.
DR   GO; GO:0048027; F:mRNA 5'-UTR binding; IEA:Ensembl.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0000470; P:maturation of LSU-rRNA; IBA:GO_Central.
DR   GO; GO:0042981; P:regulation of apoptotic process; ISS:UniProtKB.
DR   GO; GO:2000772; P:regulation of cellular senescence; ISS:UniProtKB.
DR   GO; GO:0032880; P:regulation of protein localization; IEA:Ensembl.
DR   CDD; cd00403; Ribosomal_L1; 1.
DR   Gene3D; 3.40.50.790; -; 1.
DR   InterPro; IPR023674; Ribosomal_L1-like.
DR   InterPro; IPR028364; Ribosomal_L1/biogenesis.
DR   InterPro; IPR016095; Ribosomal_L1_3-a/b-sand.
DR   Pfam; PF00687; Ribosomal_L1; 1.
DR   SUPFAM; SSF56808; SSF56808; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Coiled coil; Isopeptide bond; Nucleus; Phosphoprotein;
KW   Reference proteome; Ubl conjugation.
FT   CHAIN           1..482
FT                   /note="Ribosomal L1 domain-containing protein 1"
FT                   /id="PRO_0000319318"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          284..482
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          284..315
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..311
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        418..449
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        452..467
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:O76021"
FT   MOD_RES         354
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O76021"
FT   MOD_RES         367
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O76021"
FT   MOD_RES         384
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O76021"
FT   MOD_RES         388
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O76021"
FT   MOD_RES         407
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O76021"
FT   MOD_RES         415
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O76021"
FT   MOD_RES         457
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O76021"
FT   MOD_RES         461
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O76021"
FT   CROSSLNK        252
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:O76021"
FT   CROSSLNK        427
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:O76021"
FT   CROSSLNK        453
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:O76021"
SQ   SEQUENCE   482 AA;  53076 MW;  F98B32E3AD3E85D8 CRC64;
     MEASASNPPS TSPETSASTP ETPPGPEQLD EEQVKKAVEA LLAHSRSRKN ANGLLLNENE
     NFFLMVVLWK IPSKELRVRL SLPHGIRSDL ADVCLFTKDE PNLSSEQTER YYKKLLNNHG
     IKTISQIIPF RTLKKEYKAY EAKLRLLGSF DFFITDARIR RLLPSHLGRH FYNRKKVPVS
     VNLQSKTLSR EINDCIGGTV LNISKSGSCS TIRIGHTGMP IQHIVENVVA VAKSLSQKLP
     EKWESVKLLF VKTERSVSLP VFSSFVSSQG EAKGLRTRDL LKKVSKKSRK KTERALKRQQ
     EKKEKKLLKQ AAKAKPAPTT DAVAPKTGGV PTQDPAPQEE TGGVSALPKA QDDSEDEIPL
     LVPLKETPAA GSTKIQKAAI GKKSPKKSPG PNTARAKKRK ASPALETPIA AEPKTPGKGP
     GKKARVKEEV EKERNSSLGK KDPRQTPKKP EAKFFTTASS SVKKAPRTLT QRPKKPKVPQ
     ST