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Database: UniProt
Entry: Q9Z2F5
LinkDB: Q9Z2F5
Original site: Q9Z2F5 
ID   CTBP1_RAT               Reviewed;         430 AA.
AC   Q9Z2F5;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 3.
DT   16-JAN-2019, entry version 167.
DE   RecName: Full=C-terminal-binding protein 1;
DE            Short=CtBP1;
DE            EC=1.1.1.-;
DE   AltName: Full=50 kDa BFA-dependent ADP-ribosylation substrate;
DE   AltName: Full=BARS-50;
DE   AltName: Full=C-terminal-binding protein 3;
DE            Short=CtBP3;
GN   Name=Ctbp1; Synonyms=Bars, Ctbp3;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RX   PubMed=10364211; DOI=10.1074/jbc.274.25.17705;
RA   Spano S., Silletta M.G., Colanzi A., Alberti S., Fiucci G.,
RA   Valente C., Fusella A., Salmona M., Mironov A., Luini A., Corda D.;
RT   "Molecular cloning and functional characterization of brefeldin A-ADP-
RT   ribosylated substrate. A novel protein involved in the maintenance of
RT   the Golgi structure.";
RL   J. Biol. Chem. 274:17705-17710(1999).
RN   [2]
RP   ERRATUM.
RA   Spano S., Silletta M.G., Colanzi A., Alberti S., Fiucci G.,
RA   Valente C., Fusella A., Salmona M., Mironov A., Luini A., Corda D.;
RL   J. Biol. Chem. 274:25188-25188(1999).
RN   [3]
RP   SEQUENCE REVISION TO 259.
RA   Spano S., Silletta M.G., Colanzi A., Alberti S., Fiucci G.,
RA   Valente C., Fusella A., Salmona M., Mironov A., Luini A., Corda D.;
RL   Submitted (MAY-2001) to UniProtKB.
RN   [4]
RP   PROTEIN SEQUENCE OF 275-294, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA   Lubec G., Diao W.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
RP   FUNCTION, ADP-RIBOSYLATION, AND SUBCELLULAR LOCATION.
RX   PubMed=7624370; DOI=10.1073/pnas.92.15.7065;
RA   Di Girolamo M., Silletta M.G., De Matteis M.A., Braca A., Colanzi A.,
RA   Pawlak D., Rasenick M.M., Luini A., Corda D.;
RT   "Evidence that the 50-kDa substrate of brefeldin A-dependent ADP-
RT   ribosylation binds GTP and is modulated by the G-protein beta gamma
RT   subunit complex.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:7065-7069(1995).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-349 IN COMPLEX WITH NADH,
RP   FUNCTION, AND MUTAGENESIS OF ALA-41 AND VAL-55.
RX   PubMed=12805226; DOI=10.1093/emboj/cdg283;
RA   Nardini M., Spano S., Cericola C., Pesce A., Massaro A., Millo E.,
RA   Luini A., Corda D., Bolognesi M.;
RT   "CtBP/BARS: a dual-function protein involved in transcription co-
RT   repression and Golgi membrane fission.";
RL   EMBO J. 22:3122-3130(2003).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 1-350 IN COMPLEX WITH NAD
RP   AND ZNF217, AND INTERACTION WITH ZNF217.
RX   PubMed=16940172; DOI=10.1128/MCB.00680-06;
RA   Quinlan K.G.R., Nardini M., Verger A., Francescato P., Yaswen P.,
RA   Corda D., Bolognesi M., Crossley M.;
RT   "Specific recognition of ZNF217 and other zinc finger proteins at a
RT   surface groove of C-terminal binding proteins.";
RL   Mol. Cell. Biol. 26:8159-8172(2006).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 1-350 OF MUTANT GLU-172, NAD
RP   BINDING, SUBUNIT, AND MUTAGENESIS OF GLY-172.
RX   PubMed=19351597; DOI=10.1016/j.bbrc.2009.02.010;
RA   Nardini M., Valente C., Ricagno S., Luini A., Corda D., Bolognesi M.;
RT   "CtBP1/BARS Gly172-->Glu mutant structure: impairing NAD(H)-binding
RT   and dimerization.";
RL   Biochem. Biophys. Res. Commun. 381:70-74(2009).
CC   -!- FUNCTION: Corepressor targeting diverse transcription regulators
CC       such as GLIS2 or BCL6. Has dehydrogenase activity. Involved in
CC       controlling the equilibrium between tubular and stacked structures
CC       in the Golgi complex. Functions in brown adipose tissue (BAT)
CC       differentiation. {ECO:0000269|PubMed:10364211,
CC       ECO:0000269|PubMed:12805226, ECO:0000269|PubMed:7624370}.
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC       Note=Cofactor binding induces a conformational change.;
CC   -!- SUBUNIT: Homo- or heterodimer. Heterodimer with CTBP2. Interacts
CC       with ELK3 (via its PXDLS motif). Interacts with RBBP8 (via its
CC       PXDLS motif); the interaction is disrupted by binding to
CC       adenovirus E1A. Interacts with PNN, MECOM and ZFHX1B. Interacts
CC       with ZNF366 (via PXDLS motif) (By similarity). Interaction with
CC       SATB1 (non-acetylated form); the interaction stabilizes its
CC       attachment to DNA and promotes transcription repression. Interacts
CC       with PRDM16; the interaction represses white adipose tissue (WAT)-
CC       specific genes expression. Interacts with GLIS2, HIPK2, FOXP1,
CC       FOXP2, HDAC4, HDAC5, HDAC9, NRIP1 and WIZ. Interacts with ZNF217.
CC       Interacts with BCL6; the interaction is required for BCL6
CC       transcriptional autoinhibition and inhibition of some BCL6 target
CC       genes. Interacts with IKZF4 (By similarity). Interacts with MCRIP1
CC       (unphosphorylated form, via the PXDLS motif); competitively
CC       inhibiting CTBP-ZEB1 interaction (By similarity).
CC       {ECO:0000250|UniProtKB:O88712, ECO:0000250|UniProtKB:Q13363,
CC       ECO:0000269|PubMed:12805226, ECO:0000269|PubMed:16940172,
CC       ECO:0000269|PubMed:19351597}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13363}.
CC       Nucleus {ECO:0000250|UniProtKB:Q13363}.
CC   -!- PTM: The level of phosphorylation appears to be regulated during
CC       the cell cycle. Phosphorylation by HIPK2 on Ser-412 induces
CC       proteasomal degradation (By similarity). {ECO:0000250}.
CC   -!- PTM: ADP-ribosylated; when cells are exposed to brefeldin A.
CC   -!- PTM: Sumoylation on Lys-418 is promoted by the E3 SUMO-protein
CC       ligase CBX4. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
DR   EMBL; AF067795; AAC79427.2; -; mRNA.
DR   RefSeq; NP_062074.2; NM_019201.3.
DR   RefSeq; XP_017454636.1; XM_017599147.1.
DR   UniGene; Rn.3946; -.
DR   PDB; 1HKU; X-ray; 2.30 A; A=1-350.
DR   PDB; 1HL3; X-ray; 3.10 A; A=1-350.
DR   PDB; 2HU2; X-ray; 2.85 A; A=1-350.
DR   PDB; 3GA0; X-ray; 3.40 A; A=1-350.
DR   PDBsum; 1HKU; -.
DR   PDBsum; 1HL3; -.
DR   PDBsum; 2HU2; -.
DR   PDBsum; 3GA0; -.
DR   DisProt; DP00499; -.
DR   ProteinModelPortal; Q9Z2F5; -.
DR   SMR; Q9Z2F5; -.
DR   BioGrid; 248034; 4.
DR   IntAct; Q9Z2F5; 2.
DR   MINT; Q9Z2F5; -.
DR   STRING; 10116.ENSRNOP00000062945; -.
DR   iPTMnet; Q9Z2F5; -.
DR   PhosphoSitePlus; Q9Z2F5; -.
DR   jPOST; Q9Z2F5; -.
DR   PaxDb; Q9Z2F5; -.
DR   PRIDE; Q9Z2F5; -.
DR   GeneID; 29382; -.
DR   KEGG; rno:29382; -.
DR   UCSC; RGD:2441; rat.
DR   CTD; 1487; -.
DR   RGD; 2441; Ctbp1.
DR   eggNOG; KOG0067; Eukaryota.
DR   eggNOG; COG0111; LUCA.
DR   HOGENOM; HOG000136701; -.
DR   HOVERGEN; HBG001898; -.
DR   InParanoid; Q9Z2F5; -.
DR   KO; K04496; -.
DR   OrthoDB; 700058at2759; -.
DR   PhylomeDB; Q9Z2F5; -.
DR   EvolutionaryTrace; Q9Z2F5; -.
DR   PRO; PR:Q9Z2F5; -.
DR   Proteomes; UP000002494; Unplaced.
DR   Genevisible; Q9Z2F5; RN.
DR   GO; GO:0005737; C:cytoplasm; IMP:CAFA.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0005634; C:nucleus; IDA:SynGO.
DR   GO; GO:0098793; C:presynapse; IDA:SynGO.
DR   GO; GO:0017053; C:transcriptional repressor complex; ISS:UniProtKB.
DR   GO; GO:0051287; F:NAD binding; IDA:UniProtKB.
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:0030165; F:PDZ domain binding; IPI:CAFA.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR   GO; GO:0003714; F:transcription corepressor activity; TAS:RGD.
DR   GO; GO:0016746; F:transferase activity, transferring acyl groups; TAS:RGD.
DR   GO; GO:0061025; P:membrane fusion; TAS:RGD.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0099526; P:presynapse to nucleus signaling pathway; IDA:SynGO.
DR   GO; GO:0050872; P:white fat cell differentiation; ISS:UniProtKB.
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   3D-structure; ADP-ribosylation; Complete proteome; Cytoplasm;
KW   Differentiation; Direct protein sequencing; Isopeptide bond; NAD;
KW   Nucleus; Oxidoreductase; Phosphoprotein; Reference proteome;
KW   Repressor; Transcription; Transcription regulation; Ubl conjugation.
FT   CHAIN         1    430       C-terminal-binding protein 1.
FT                                /FTId=PRO_0000076043.
FT   NP_BIND     169    174       NAD. {ECO:0000269|PubMed:12805226,
FT                                ECO:0000269|PubMed:16940172}.
FT   NP_BIND     226    232       NAD. {ECO:0000269|PubMed:12805226,
FT                                ECO:0000269|PubMed:16940172}.
FT   NP_BIND     253    255       NAD. {ECO:0000269|PubMed:12805226,
FT                                ECO:0000269|PubMed:16940172}.
FT   REGION        1     59       Interaction with GLIS2 1. {ECO:0000250}.
FT   REGION      277    349       Interaction with GLIS2 2. {ECO:0000250}.
FT   ACT_SITE    255    255       {ECO:0000250}.
FT   ACT_SITE    284    284       {ECO:0000250}.
FT   ACT_SITE    304    304       Proton donor. {ECO:0000250}.
FT   BINDING      89     89       NAD. {ECO:0000269|PubMed:12805226,
FT                                ECO:0000269|PubMed:16940172}.
FT   BINDING     193    193       NAD. {ECO:0000269|PubMed:12805226,
FT                                ECO:0000269|PubMed:16940172}.
FT   BINDING     279    279       NAD. {ECO:0000269|PubMed:12805226,
FT                                ECO:0000269|PubMed:16940172}.
FT   MOD_RES     289    289       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q13363}.
FT   MOD_RES     412    412       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q13363}.
FT   CROSSLNK    418    418       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT                                {ECO:0000250}.
FT   MUTAGEN      41     41       A->E: Strongly reduces interaction with
FT                                E1A. {ECO:0000269|PubMed:12805226}.
FT   MUTAGEN      55     55       V->R: Strongly reduces interaction with
FT                                E1A. {ECO:0000269|PubMed:12805226}.
FT   MUTAGEN     172    172       G->E: Loss dimerization and of NAD
FT                                binding. {ECO:0000269|PubMed:19351597}.
FT   CONFLICT    175    175       G -> S (in Ref. 1; AA sequence).
FT                                {ECO:0000305}.
FT   STRAND       18     23       {ECO:0000244|PDB:1HKU}.
FT   TURN         28     30       {ECO:0000244|PDB:1HKU}.
FT   HELIX        31     34       {ECO:0000244|PDB:1HKU}.
FT   TURN         35     37       {ECO:0000244|PDB:1HKU}.
FT   STRAND       39     42       {ECO:0000244|PDB:1HKU}.
FT   HELIX        48     50       {ECO:0000244|PDB:1HKU}.
FT   HELIX        53     58       {ECO:0000244|PDB:1HKU}.
FT   STRAND       59     64       {ECO:0000244|PDB:1HKU}.
FT   STRAND       66     68       {ECO:0000244|PDB:1HKU}.
FT   HELIX        72     76       {ECO:0000244|PDB:1HKU}.
FT   STRAND       83     89       {ECO:0000244|PDB:1HKU}.
FT   STRAND       92     94       {ECO:0000244|PDB:1HL3}.
FT   HELIX        96    101       {ECO:0000244|PDB:1HKU}.
FT   STRAND      105    107       {ECO:0000244|PDB:1HKU}.
FT   STRAND      111    113       {ECO:0000244|PDB:1HKU}.
FT   HELIX       114    130       {ECO:0000244|PDB:1HKU}.
FT   HELIX       132    140       {ECO:0000244|PDB:1HKU}.
FT   HELIX       148    154       {ECO:0000244|PDB:1HKU}.
FT   TURN        155    157       {ECO:0000244|PDB:1HKU}.
FT   STRAND      165    169       {ECO:0000244|PDB:1HKU}.
FT   HELIX       173    183       {ECO:0000244|PDB:1HKU}.
FT   TURN        184    186       {ECO:0000244|PDB:1HKU}.
FT   STRAND      188    192       {ECO:0000244|PDB:1HKU}.
FT   STRAND      194    196       {ECO:0000244|PDB:3GA0}.
FT   HELIX       200    203       {ECO:0000244|PDB:1HKU}.
FT   HELIX       212    218       {ECO:0000244|PDB:1HKU}.
FT   STRAND      220    224       {ECO:0000244|PDB:1HKU}.
FT   STRAND      230    232       {ECO:0000244|PDB:1HL3}.
FT   HELIX       238    243       {ECO:0000244|PDB:1HKU}.
FT   STRAND      248    252       {ECO:0000244|PDB:1HKU}.
FT   HELIX       256    258       {ECO:0000244|PDB:1HKU}.
FT   HELIX       261    269       {ECO:0000244|PDB:1HKU}.
FT   STRAND      272    279       {ECO:0000244|PDB:1HKU}.
FT   STRAND      282    285       {ECO:0000244|PDB:1HKU}.
FT   STRAND      288    291       {ECO:0000244|PDB:1HL3}.
FT   TURN        292    295       {ECO:0000244|PDB:1HKU}.
FT   STRAND      297    301       {ECO:0000244|PDB:1HKU}.
FT   HELIX       310    329       {ECO:0000244|PDB:1HKU}.
FT   TURN        332    334       {ECO:0000244|PDB:1HKU}.
FT   STRAND      337    340       {ECO:0000244|PDB:1HKU}.
FT   HELIX       342    344       {ECO:0000244|PDB:3GA0}.
SQ   SEQUENCE   430 AA;  46628 MW;  0A36DBF27E6A8605 CRC64;
     MSGVRPPIMN GPMHPRPLVA LLDGRDCTVE MPILKDVATV AFCDAQSTQE IHEKVLNEAV
     GALMYHTITL TREDLEKFKA LRIIVRIGSG FDNIDIKSAG DLGIAVCNVP AASVEETADS
     TLCHILNLYR RTTWLHQALR EGTRVQSVEQ IREVASGAAR IRGETLGIIG LGRVGQAVAL
     RAKAFGFNVL FYDPYLSDGI ERALGLQRVS TLQDLLFHSD CVTLHCGLNE HNHHLINDFT
     VKQMRQGAFL VNTARGGLVD EKALAQALKE GRIRGAALDV HESEPFSFSQ GPLKDAPNLI
     CTPHAAWYSE QASIEMREEA AREIRRAITG RIPDSLKNCV NKDHLTAATH WASMDPAVVH
     PELNGAAYSR YPPGVVSVAP TGIPAAVEGI VPSAMSLSHG LPPVAHPPHA PSPGQTVKPE
     ADRDHTTDQL
//
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