ID   C1D_PONAB               Reviewed;         141 AA.
AC   Q5RBU4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Nuclear nucleic acid-binding protein C1D;
GN   Name=C1D;
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=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays a role in the recruitment of the exosome to pre-rRNA to
CC       mediate the 3'-5' end processing of the 5.8S rRNA. Forms a multi-
CC       subunit complex with MPHOSPH6 and EXOSC10 and this complex along with
CC       MTR4 is required for the 3'-5' end processing of the 5.8S rRNA. Can
CC       activate PRKDC not only in the presence of linear DNA but also in the
CC       presence of supercoiled DNA. Can induce apoptosis in a p53/TP53
CC       dependent manner. May regulate the TRAX/TSN complex formation.
CC       Potentiates transcriptional repression by NR1D1 and THRB (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Monomer and homodimer. Interacts with NR1D1, THRA, THRB, NCOR1
CC       and NCOR2. Interacts with EXOSC10. Forms a heterotrimeric complex with
CC       EXOSC10 and MPHOSPH6 in vitro. The homodimeric form interacts with
CC       TSNAX following gamma-radiation. Interacts with RAC3 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13901}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q13901}. Nucleus, nucleolus
CC       {ECO:0000250|UniProtKB:Q13901}. Note=EXOSC10 is required for nucleolar
CC       localization. Colocalizes with TSNAX in the nucleus.
CC       {ECO:0000250|UniProtKB:Q13901}.
CC   -!- PTM: Phosphorylated by PRKDC. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the C1D family. {ECO:0000305}.
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DR   EMBL; CR858539; CAH90766.1; -; mRNA.
DR   RefSeq; NP_001125429.1; NM_001131957.1.
DR   RefSeq; XP_009235499.1; XM_009237224.1.
DR   AlphaFoldDB; Q5RBU4; -.
DR   SMR; Q5RBU4; -.
DR   STRING; 9601.ENSPPYP00000013776; -.
DR   Ensembl; ENSPPYT00000014335; ENSPPYP00000013776; ENSPPYG00000012354.
DR   GeneID; 100172337; -.
DR   KEGG; pon:100172337; -.
DR   CTD; 10438; -.
DR   eggNOG; KOG4835; Eukaryota.
DR   GeneTree; ENSGT00390000015405; -.
DR   HOGENOM; CLU_064339_4_1_1; -.
DR   InParanoid; Q5RBU4; -.
DR   Proteomes; UP000001595; Chromosome 2A.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   InterPro; IPR011082; Exosome-assoc_fac/DNA_repair.
DR   InterPro; IPR007146; Sas10/Utp3/C1D.
DR   PANTHER; PTHR15341; PTHR15341; 1.
DR   Pfam; PF04000; Sas10_Utp3; 1.
PE   2: Evidence at transcript level;
KW   Apoptosis; Cytoplasm; DNA-binding; Isopeptide bond; Nucleus;
KW   Phosphoprotein; Reference proteome; Repressor; RNA-binding;
KW   rRNA processing; Transcription; Transcription regulation; Ubl conjugation.
FT   CHAIN           1..141
FT                   /note="Nuclear nucleic acid-binding protein C1D"
FT                   /id="PRO_0000316302"
FT   REGION          1..100
FT                   /note="Required for transcriptional repression"
FT                   /evidence="ECO:0000250"
FT   REGION          50..100
FT                   /note="Interaction with NR1D1"
FT                   /evidence="ECO:0000250"
FT   REGION          100..141
FT                   /note="Interaction with NCOR1 and NCOR2"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        119
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13901"
FT   CROSSLNK        126
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13901"
FT   CROSSLNK        132
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13901"
SQ   SEQUENCE   141 AA;  16029 MW;  9976A3BBD5620EAC CRC64;
     MAGEEINEDY PVEIHEYLSA FENSIGAVDE MLKTMMSVSR NELLQKLDPL EQAKVDLVSA
     YTLNSMFWVY LATQGVNPKE HPVKQELERI RVYMNRVKEI TDKKKAGKLD RGAASRFVKN
     ALWEPKPKNA SKVANKGKSK S