CTBP1_XENLA
ID CTBP1_XENLA Reviewed; 440 AA.
AC Q9YHU0;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=C-terminal-binding protein 1;
DE Short=CtBP1;
DE EC=1.1.1.-;
DE AltName: Full=C-terminal-binding protein A;
GN Name=ctbp1; Synonyms=ctbp-a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9858600; DOI=10.1128/mcb.19.1.777;
RA Sewalt R.G.A.B., Gunster M.J., van der Vlag J., Satijn D.P.E., Otte A.P.;
RT "C-terminal binding protein is a transcriptional repressor that interacts
RT with a specific class of vertebrate polycomb proteins.";
RL Mol. Cell. Biol. 19:777-787(1999).
CC -!- FUNCTION: Corepressor targeting diverse transcription regulators. Has
CC dehydrogenase activity.
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; AF091554; AAD14596.1; -; mRNA.
DR RefSeq; NP_001079151.1; NM_001085682.1.
DR RefSeq; XP_018110260.1; XM_018254771.1.
DR AlphaFoldDB; Q9YHU0; -.
DR SMR; Q9YHU0; -.
DR GeneID; 373701; -.
DR KEGG; xla:373701; -.
DR CTD; 373701; -.
DR Xenbase; XB-GENE-864974; ctbp1.L.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 373701; Expressed in internal ear and 20 other tissues.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0003714; F:transcription corepressor activity; IEA:InterPro.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR CDD; cd05299; CtBP_dh; 1.
DR InterPro; IPR043322; CtBP.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 2: Evidence at transcript level;
KW NAD; Nucleus; Oxidoreductase; Reference proteome.
FT CHAIN 1..440
FT /note="C-terminal-binding protein 1"
FT /id="PRO_0000076046"
FT REGION 409..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 266
FT /evidence="ECO:0000250"
FT ACT_SITE 295
FT /evidence="ECO:0000250"
FT ACT_SITE 315
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 180..185
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 237..243
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 264..266
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 290
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 315..318
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 375..376
FT /note="Cleavage; by CAPN1"
FT /evidence="ECO:0000250|UniProtKB:Q13363"
FT SITE 387..388
FT /note="Cleavage; by CAPN1"
FT /evidence="ECO:0000250|UniProtKB:Q13363"
FT SITE 409..410
FT /note="Cleavage; by CAPN1 and CAPN3"
FT /evidence="ECO:0000250|UniProtKB:Q13363"
SQ SEQUENCE 440 AA; 47777 MW; E1AB044901A00116 CRC64;
MGSSHLLNKG LPLGIRPPIM NGPMHPRPLV ALLDGRDCTV EMPILKDVAT VAFCDAQSTQ
EIHEKVLNEA VGALMYHTIT LTREDLEKFK ALRIIVRIGS GFDNIDIKSA GDLGIAVCNV
PAASVEETAD STMCHILNLY RRTTWLHQAL REGTRVQSVE QIREVASGAA RIRGETLGII
GLGRVGQAVA LRAKTFGFNV FFYDPYLSDG IERALGLQRV STLQDLLFHS DCVTLHCGLN
EHNHHLINDF TIKQMRQGAF LVNTARGGLV DEKALAQALK EGRIRGAALD VHESEPFSFT
QGPLKDAPNL ICTPHAAWYS EQASIEMREE AAREIRRAIT GRIPDSLKNC VNKDHLTAAT
HWASMDPGVV HPELNGGAYR YPQGVVSVAP AGLPAAVEGI VPSAMSLSHA HPAVAHPPHA
PSPGQTIKPE ADRDHPSDQL