ID   G45IP_CHLAE             Reviewed;         222 AA.
AC   Q8SPE7;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 43.
DE   RecName: Full=Growth arrest and DNA damage-inducible proteins-interacting protein 1;
DE   AltName: Full=39S ribosomal protein L59, mitochondrial;
DE            Short=MRP-L59;
DE   AltName: Full=Papillomavirus L2-interacting nuclear protein 1;
DE            Short=PLINP-1;
GN   Name=GADD45GIP1; Synonyms=MRPL59, PLINP;
OS   Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Chlorocebus.
OX   NCBI_TaxID=9534;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Goernemann J.;
RT   "Cellular interaction partners of the HPV minor capsid protein L2.";
RL   Thesis (2002), University of Heidelberg, Germany.
CC   -!- FUNCTION: Acts as a negative regulator of G1 to S cell cycle phase
CC       progression by inhibiting cyclin-dependent kinases. Inhibitory effects
CC       are additive with GADD45 proteins but occurs also in the absence of
CC       GADD45 proteins. Acts as a repressor of the orphan nuclear receptor
CC       NR4A1 by inhibiting AB domain-mediated transcriptional activity. May be
CC       involved in the hormone-mediated regulation of NR4A1 transcriptional
CC       activity. May play a role in mitochondrial protein synthesis.
CC       {ECO:0000250|UniProtKB:Q8TAE8}.
CC   -!- SUBUNIT: Component of the mitochondrial ribosome large subunit (39S)
CC       which comprises a 16S rRNA and about 50 distinct proteins. Interacts
CC       with GADD45A, GADD45B and GADD45G. Interacts with NR4A1 via the NR4A1
CC       AB domain. Interacts with ATAD3A and ATAD3B.
CC       {ECO:0000250|UniProtKB:Q8TAE8}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q8TAE8}.
CC       Nucleus {ECO:0000250|UniProtKB:Q8TAE8}. Note=Using N-terminally tagged
CC       constructs, has been found in the nucleus. C-terminally tagged
CC       constructs are targeted exclusively to mitochondria. This discrepancy
CC       may be explained by masking of a potential N-terminal mitochondrial
CC       targeting signal by the tag. {ECO:0000250|UniProtKB:Q8TAE8}.
CC   -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein
CC       mL64 family. {ECO:0000305}.
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DR   EMBL; AJ437508; CAD26811.1; -; mRNA.
DR   AlphaFoldDB; Q8SPE7; -.
DR   SMR; Q8SPE7; -.
DR   IntAct; Q8SPE7; 3.
DR   PRIDE; Q8SPE7; -.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   Gene3D; 6.10.280.120; -; 1.
DR   InterPro; IPR043035; Damage-induce-interact_sf.
DR   InterPro; IPR018472; Damage-induce-interacting_prot.
DR   PANTHER; PTHR31761; PTHR31761; 1.
DR   Pfam; PF10147; CR6_interact; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Coiled coil; Mitochondrion; Nucleus; Ribonucleoprotein;
KW   Ribosomal protein.
FT   CHAIN           1..222
FT                   /note="Growth arrest and DNA damage-inducible proteins-
FT                   interacting protein 1"
FT                   /id="PRO_0000228619"
FT   REGION          14..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          188..222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          144..213
FT                   /evidence="ECO:0000255"
FT   MOTIF           184..200
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   222 AA;  25378 MW;  1DEDF23D388DAE04 CRC64;
     MAASVRKARS LLGLTATLAP GSRGYRAPPP PRREPGPWWP DPEDLLTHRW QLGPRYAAKQ
     FARYGAASGV APGSLWPSPE QLRELEAEER EWYPSLATMQ ESLRVKHLAE EQKRREREQH
     IAECMAKMPQ MIVNWQQQQR ERWEKAQADK ERRARLQAEA QELLGYQVNP KSARFQELLQ
     DLEKKERKRL KEEKQRQKQE ARAAALAAAA AQDPAASGAP SS