CTBP1_CAEEL
ID CTBP1_CAEEL Reviewed; 727 AA.
AC Q20595; H8W3Z5; Q20596;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 3.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=C-terminal-binding protein 1 {ECO:0000303|PubMed:18005989};
GN Name=ctbp-1 {ECO:0000312|EMBL:CCD71569.1, ECO:0000312|WormBase:F49E10.5a};
GN ORFNames=F49E10.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000312|EMBL:CCD71569.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CCD71569.1};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, SUBUNIT, AND DOMAIN.
RX PubMed=18005989; DOI=10.1016/j.jmb.2007.10.041;
RA Nicholas H.R., Lowry J.A., Wu T., Crossley M.;
RT "The Caenorhabditis elegans protein CTBP-1 defines a new group of THAP
RT domain-containing CtBP corepressors.";
RL J. Mol. Biol. 375:1-11(2008).
RN [3] {ECO:0000305}
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-332; GLY-334 AND
RP HIS-467.
RX PubMed=19164523; DOI=10.1073/pnas.0802674106;
RA Chen S., Whetstine J.R., Ghosh S., Hanover J.A., Gali R.R., Grosu P.,
RA Shi Y.;
RT "The conserved NAD(H)-dependent corepressor CTBP-1 regulates Caenorhabditis
RT elegans life span.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:1496-1501(2009).
RN [4] {ECO:0000305, ECO:0000312|PDB:2JM3}
RP STRUCTURE BY NMR OF 1-89 IN COMPLEX WITH ZINC, DOMAIN, AND DNA-BINDING.
RX PubMed=17174978; DOI=10.1016/j.jmb.2006.11.058;
RA Liew C.K., Crossley M., Mackay J.P., Nicholas H.R.;
RT "Solution structure of the THAP domain from Caenorhabditis elegans C-
RT terminal binding protein (CtBP).";
RL J. Mol. Biol. 366:382-390(2007).
CC -!- FUNCTION: Binds DNA and represses gene expression. Plays a role in
CC regulation of life span, possibly by regulating transcription of genes
CC important for lipid metabolism. {ECO:0000269|PubMed:18005989,
CC ECO:0000269|PubMed:19164523}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17174978,
CC ECO:0000269|PubMed:18005989}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000269|PubMed:9851916};
CC IsoId=Q20595-1; Sequence=Displayed;
CC Name=b {ECO:0000269|PubMed:9851916};
CC IsoId=Q20595-2; Sequence=VSP_053308, VSP_053309;
CC -!- DOMAIN: The THAP-type zinc finger mediates DNA-binding but is not
CC required for repression of gene expression.
CC {ECO:0000269|PubMed:17174978, ECO:0000269|PubMed:18005989}.
CC -!- DISRUPTION PHENOTYPE: Adult life span extension and increased
CC resistance to oxidative and heat stress but not to DNA damage,
CC starvation or pathogen stress. {ECO:0000269|PubMed:19164523}.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000255}.
CC -!- CAUTION: In contrast to other members of the family, lacks the
CC conserved Arg and Glu active sites at positions 417 and 446
CC respectively, suggesting that it lacks dehydrogenase activity.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FO081427; CCD71569.1; -; Genomic_DNA.
DR EMBL; FO081427; CCG28183.1; -; Genomic_DNA.
DR PIR; T34289; T34289.
DR RefSeq; NP_001257030.1; NM_001270101.1. [Q20595-1]
DR RefSeq; NP_001257031.1; NM_001270102.1. [Q20595-2]
DR PDB; 2JM3; NMR; -; A=1-89.
DR PDBsum; 2JM3; -.
DR AlphaFoldDB; Q20595; -.
DR SMR; Q20595; -.
DR BioGRID; 45786; 1.
DR STRING; 6239.F49E10.5a; -.
DR EPD; Q20595; -.
DR PaxDb; Q20595; -.
DR PeptideAtlas; Q20595; -.
DR PRIDE; Q20595; -.
DR EnsemblMetazoa; F49E10.5a.1; F49E10.5a.1; WBGene00006424. [Q20595-1]
DR EnsemblMetazoa; F49E10.5b.1; F49E10.5b.1; WBGene00006424. [Q20595-2]
DR GeneID; 180853; -.
DR KEGG; cel:CELE_F49E10.5; -.
DR UCSC; F49E10.5; c. elegans. [Q20595-1]
DR CTD; 180853; -.
DR WormBase; F49E10.5a; CE29966; WBGene00006424; ctbp-1. [Q20595-1]
DR WormBase; F49E10.5b; CE47412; WBGene00006424; ctbp-1. [Q20595-2]
DR eggNOG; KOG0067; Eukaryota.
DR GeneTree; ENSGT00940000171573; -.
DR HOGENOM; CLU_016243_0_0_1; -.
DR InParanoid; Q20595; -.
DR OMA; IAVCHAP; -.
DR OrthoDB; 911009at2759; -.
DR PhylomeDB; Q20595; -.
DR Reactome; R-CEL-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-CEL-4641265; Repression of WNT target genes.
DR EvolutionaryTrace; Q20595; -.
DR PRO; PR:Q20595; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00006424; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:WormBase.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0001221; F:transcription coregulator binding; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:WormBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:WormBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd05299; CtBP_dh; 1.
DR InterPro; IPR043322; CtBP.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR006612; THAP_Znf.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR Pfam; PF05485; THAP; 1.
DR SMART; SM00980; THAP; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR PROSITE; PS50950; ZF_THAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; DNA-binding; Metal-binding; NAD;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Zinc; Zinc-finger.
FT CHAIN 1..727
FT /note="C-terminal-binding protein 1"
FT /id="PRO_0000424056"
FT ZN_FING 5..60
FT /note="THAP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00309"
FT REGION 64..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..680
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 251
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P56545"
FT BINDING 331..336
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P56545"
FT BINDING 355
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P56545"
FT BINDING 388..394
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P56545"
FT BINDING 415..417
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P56545"
FT BINDING 441
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P56545"
FT BINDING 467..470
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P56545"
FT VAR_SEQ 1..121
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_053308"
FT VAR_SEQ 122..140
FT /note="KSRSFRDFYPSLSSTPSFD -> MGGEANGTKPTGSQKRKRN (in
FT isoform b)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_053309"
FT MUTAGEN 332
FT /note="G->V: Does not rescue the extended lifespan
FT phenotype observed in ctbp-1 deletion mutants."
FT /evidence="ECO:0000269|PubMed:19164523"
FT MUTAGEN 334
FT /note="G->V: Does not rescue the extended lifespan
FT phenotype observed in ctbp-1 deletion mutants."
FT /evidence="ECO:0000269|PubMed:19164523"
FT MUTAGEN 467
FT /note="H->A: Rescues the extended lifespan phenotype
FT observed in ctbp-1 deletion mutants."
FT /evidence="ECO:0000269|PubMed:19164523"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:2JM3"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:2JM3"
FT HELIX 33..43
FT /evidence="ECO:0007829|PDB:2JM3"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:2JM3"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:2JM3"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:2JM3"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:2JM3"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:2JM3"
SQ SEQUENCE 727 AA; 79598 MW; 33D6FC34EE01A371 CRC64;
MPTTCGFPNC KFRSRYRGLE DNRHFYRIPK RPLILRQRWL TAIGRTEETV VSQLRICSAH
FEGGEKKEGD IPVPDPTVDK QIKIELPPKE SKNSDRRRKQ NIPARFPRPE SPSGDSPSYS
KKSRSFRDFY PSLSSTPSFD PAQSPHTPHP PVLPDPQQAL NDILSMTSTR MNGPSSSRPL
VALLDGRDCS VEMPILKDVA TVAFCDAQST QEIHEKVLNE AVAALMYHSI KLEKEDLEKF
KVLKVVFRIG YGIDNIDVKA ATELGIAVCH APGDYVEDVA DSTLSLILDL FRRTYWHAKS
YSETRKTIGA DQVRENAVGS KKVRGSVLGI LGCGRVGTAV GLRARAFGLH IIFYDPFVRE
GHDKALGFER VYTMDEFMSR SDCISLHCNL GDETRGIINA DSLRQCKSGV YIVNTSHAGL
INENDLAAAL KNGHVKGAAL DVHDSVRFDP NCLNPLVGCP NIINTPHSAW MTEASCKDLR
INAAKEIRKA INGRCPQDLT HCINKEAVMR NSNPINRRTS SAHPLLNMGF PTLPNFPPMS
MSPHFPYPNP LLAMGAQMGA LNPFMGNGAL PFNPAAALSS LAAAQAANAQ RGSPANRSSR
SSPSPHTNKS SVSPGNNGHV KTEPSSPAAK IEVDIAENDK HSMMTFLQRL IAPNGDSGAS
TADSGIEGGD KEKVQSDGDE NMEDMEVIDA EKLKEELNIG QLEEPEEISV GLNNGNRINI
DEQPLAT
