GenomeNet

Database: UniProt
Entry: Q20595
LinkDB: Q20595
Original site: Q20595 
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   16-JAN-2019, entry version 140.
DE   RecName: Full=C-terminal-binding protein 1 {ECO:0000303|PubMed:18005989};
GN   Name=ctbp-1 {ECO:0000312|EMBL:CCD71569.1,
GN   ECO:0000312|WormBase:F49E10.5a}; 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
RT   investigating 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
RP   AND 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
RT   Caenorhabditis 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
RP   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
CC       genes important for lipid metabolism.
CC       {ECO:0000269|PubMed:18005989, 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}.
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   UniGene; Cel.17039; -.
DR   PDB; 2JM3; NMR; -; A=1-89.
DR   PDBsum; 2JM3; -.
DR   ProteinModelPortal; Q20595; -.
DR   SMR; Q20595; -.
DR   STRING; 6239.F49E10.5; -.
DR   EPD; Q20595; -.
DR   PaxDb; Q20595; -.
DR   PeptideAtlas; Q20595; -.
DR   PRIDE; Q20595; -.
DR   EnsemblMetazoa; F49E10.5a; F49E10.5a; WBGene00006424. [Q20595-1]
DR   EnsemblMetazoa; F49E10.5b; F49E10.5b; 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   eggNOG; COG0111; LUCA.
DR   GeneTree; ENSGT00940000171573; -.
DR   HOGENOM; HOG000020404; -.
DR   InParanoid; Q20595; -.
DR   KO; K04496; -.
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 4 organ(s), highest expression level in pharyngeal muscle cell (C elegans).
DR   GO; GO:0005634; C:nucleus; IDA:WormBase.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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   Gene3D; 3.30.40.180; -; 1.
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   InterPro; IPR038441; THAP_Znf_sf.
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; Complete proteome; DNA-binding;
KW   Metal-binding; NAD; Reference proteome; Repressor; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1    727       C-terminal-binding protein 1.
FT                                /FTId=PRO_0000424056.
FT   ZN_FING       5     60       THAP-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00309}.
FT   NP_BIND     331    336       NAD. {ECO:0000250|UniProtKB:P56545}.
FT   NP_BIND     388    394       NAD. {ECO:0000250|UniProtKB:P56545}.
FT   NP_BIND     415    417       NAD. {ECO:0000250|UniProtKB:P56545}.
FT   NP_BIND     467    470       NAD. {ECO:0000250|UniProtKB:P56545}.
FT   BINDING     251    251       NAD. {ECO:0000250|UniProtKB:P56545}.
FT   BINDING     355    355       NAD. {ECO:0000250|UniProtKB:P56545}.
FT   BINDING     441    441       NAD. {ECO:0000250|UniProtKB:P56545}.
FT   VAR_SEQ       1    121       Missing (in isoform b).
FT                                {ECO:0000303|PubMed:9851916}.
FT                                /FTId=VSP_053308.
FT   VAR_SEQ     122    140       KSRSFRDFYPSLSSTPSFD -> MGGEANGTKPTGSQKRKR
FT                                N (in isoform b).
FT                                {ECO:0000303|PubMed:9851916}.
FT                                /FTId=VSP_053309.
FT   MUTAGEN     332    332       G->V: Does not rescue the extended
FT                                lifespan phenotype observed in ctbp-1
FT                                deletion mutants.
FT                                {ECO:0000269|PubMed:19164523}.
FT   MUTAGEN     334    334       G->V: Does not rescue the extended
FT                                lifespan phenotype observed in ctbp-1
FT                                deletion mutants.
FT                                {ECO:0000269|PubMed:19164523}.
FT   MUTAGEN     467    467       H->A: Rescues the extended lifespan
FT                                phenotype observed in ctbp-1 deletion
FT                                mutants. {ECO:0000269|PubMed:19164523}.
FT   TURN         13     15       {ECO:0000244|PDB:2JM3}.
FT   STRAND       16     18       {ECO:0000244|PDB:2JM3}.
FT   HELIX        33     43       {ECO:0000244|PDB:2JM3}.
FT   HELIX        47     49       {ECO:0000244|PDB:2JM3}.
FT   STRAND       50     53       {ECO:0000244|PDB:2JM3}.
FT   HELIX        58     60       {ECO:0000244|PDB:2JM3}.
FT   STRAND       67     70       {ECO:0000244|PDB:2JM3}.
FT   TURN         76     78       {ECO:0000244|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
//
DBGET integrated database retrieval system