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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
 
 
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