CTBP2_XENLA
ID CTBP2_XENLA Reviewed; 437 AA.
AC Q9W758; Q6DFD9;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=C-terminal-binding protein 2;
DE Short=CtBP2;
DE AltName: Full=C-terminal-binding protein B;
DE AltName: Full=TCF-3 corepressor CtBP;
DE AltName: Full=XCtBP;
GN Name=ctbp2; Synonyms=ctbp-b;
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], FUNCTION, INTERACTION WITH TCF7L1-A, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=10375506; DOI=10.1242/dev.126.14.3159;
RA Brannon M., Brown J.D., Bates R., Kimelman D., Moon R.T.;
RT "XCtBP is a XTcf-3 co-repressor with roles throughout Xenopus
RT development.";
RL Development 126:3159-3170(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Corepressor targeting diverse transcription regulators.
CC {ECO:0000269|PubMed:10375506}.
CC -!- SUBUNIT: Interacts with the C-terminus of tcf7l1-a via the consensus
CC motifs P-X-[DNS]-L-[STVA]. {ECO:0000269|PubMed:10375506}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development. Localized to
CC discrete structures during neurulation. The pattern of expression is
CC increasingly refined to include the head, central nervous system and
CC tissues along the dorsal midline to the tailbud.
CC {ECO:0000269|PubMed:10375506}.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; AF152006; AAD41370.1; -; mRNA.
DR EMBL; BC076800; AAH76800.1; -; mRNA.
DR RefSeq; NP_001081966.1; NM_001088497.1.
DR RefSeq; XP_018109637.1; XM_018254148.1.
DR AlphaFoldDB; Q9W758; -.
DR SMR; Q9W758; -.
DR DNASU; 398147; -.
DR GeneID; 398147; -.
DR KEGG; xla:398147; -.
DR CTD; 398147; -.
DR Xenbase; XB-GENE-6251928; ctbp2l.S.
DR Proteomes; UP000186698; Chromosome 3S.
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 GO; GO:0050872; P:white fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Nucleus; Oxidoreductase; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Wnt signaling pathway.
FT CHAIN 1..437
FT /note="C-terminal-binding protein 2"
FT /id="PRO_0000076047"
FT REGION 410..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 269
FT /evidence="ECO:0000250"
FT ACT_SITE 298
FT /evidence="ECO:0000250"
FT ACT_SITE 318
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 183..188
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 207
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 240..246
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 267..269
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 293
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 318..321
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 437 AA; 47776 MW; 49D2FEFD82E2B010 CRC64;
MDKHKVKRQR LDRICDGIRP PILNGPMPVR PLVALLDGRD CTIEMPILKD VATVAFCDAQ
STQEIHEKVL SEAVGALMYH TITLSREDLE KFKALRIIIK IGSGYDNIDI KSAAELGIAV
CNIPSASVEE TADSTLCHIL NLYRRVTWLH QAMREGNRPA SVEQIREVAG GAARIRGETL
GIIGLGRIGQ AVALRAKAFN FTVIFYDPYL ADGVERSLGL QRMATLQELL MHSDCITLHC
NLNEHNHHLI NDFTIKQMRQ GCFLVNTARG GLVDEKALAQ ALKDGRIRGA ALDVHESEPF
SFSQGPLKDA PNLICTPHTA WYSEHASIEA REEAAKEIRR AIAGPIPDSL RNCVNKDYLL
AAVQWSGMEQ AAVHPELNGA SSYRFPPGVV GVTSAGHPSA IEGLVASSHP LIPSVSHTPS
PGQTTKPDPD REIPTDQ
