CTBP1_RAT
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 03-AUG-2022, entry version 184.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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., Valente C.,
RA 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 the
RT Golgi structure.";
RL J. Biol. Chem. 274:17705-17710(1999).
RN [2]
RP ERRATUM OF PUBMED:10364211.
RA Spano S., Silletta M.G., Colanzi A., Alberti S., Fiucci G., Valente C.,
RA 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., Valente C.,
RA 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 subunit
RT complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:7065-7069(1995).
RN [6]
RP INTERACTION WITH CTBP1, AND SUBCELLULAR LOCATION.
RX PubMed=25652077; DOI=10.15252/embj.201488796;
RA Ivanova D., Dirks A., Montenegro-Venegas C., Schoene C., Altrock W.D.,
RA Marini C., Frischknecht R., Schanze D., Zenker M., Gundelfinger E.D.,
RA Fejtova A.;
RT "Synaptic activity controls localization and function of CtBP1 via binding
RT to Bassoon and Piccolo.";
RL EMBO J. 34:1056-1077(2015).
RN [7]
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-repression
RT and Golgi membrane fission.";
RL EMBO J. 22:3122-3130(2003).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 1-350 IN COMPLEX WITH NAD AND
RP 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., Corda D.,
RA Bolognesi M., Crossley M.;
RT "Specific recognition of ZNF217 and other zinc finger proteins at a surface
RT groove of C-terminal binding proteins.";
RL Mol. Cell. Biol. 26:8159-8172(2006).
RN [9]
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 and
RT dimerization.";
RL Biochem. Biophys. Res. Commun. 381:70-74(2009).
CC -!- FUNCTION: Corepressor targeting diverse transcription regulators such
CC as GLIS2 or BCL6. Has dehydrogenase activity. Involved in controlling
CC the equilibrium between tubular and stacked structures in the Golgi
CC complex. Functions in brown adipose tissue (BAT) differentiation.
CC {ECO:0000269|PubMed:10364211, ECO:0000269|PubMed:12805226,
CC 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 with
CC ELK3 (via its PXDLS motif). Interacts with RBBP8 (via its PXDLS motif);
CC the interaction is disrupted by binding to adenovirus E1A. Interacts
CC with PNN, MECOM and ZFHX1B. Interacts with ZNF366 (via PXDLS motif) (By
CC similarity). Interaction with SATB1 (non-acetylated form); the
CC interaction stabilizes its attachment to DNA and promotes transcription
CC repression. Interacts with PRDM16; the interaction represses white
CC adipose tissue (WAT)-specific genes expression. Interacts with GLIS2,
CC HIPK2, FOXP1, FOXP2, HDAC4, HDAC5, HDAC9, NRIP1 and WIZ. Interacts with
CC ZNF217. 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 inhibiting
CC CTBP-ZEB1 interaction (By similarity). Interacts with Bassoon/BSN; this
CC interaction targets and anchors CTBP1 to presynapses (PubMed:25652077).
CC Interacts with SIMC1 (By similarity). {ECO:0000250|UniProtKB:O88712,
CC ECO:0000250|UniProtKB:Q13363, ECO:0000269|PubMed:12805226,
CC ECO:0000269|PubMed:16940172, ECO:0000269|PubMed:19351597,
CC ECO:0000269|PubMed:25652077}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13363}. Nucleus
CC {ECO:0000269|PubMed:25652077}. Synapse, synaptosome
CC {ECO:0000269|PubMed:25652077}.
CC -!- PTM: The level of phosphorylation appears to be regulated during the
CC cell cycle. Phosphorylation by HIPK2 on Ser-412 induces proteasomal
CC 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 ligase
CC CBX4. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; AF067795; AAC79427.2; -; mRNA.
DR RefSeq; NP_062074.2; NM_019201.3.
DR RefSeq; XP_017454636.1; XM_017599147.1.
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 AlphaFoldDB; Q9Z2F5; -.
DR SMR; Q9Z2F5; -.
DR BioGRID; 248034; 4.
DR IntAct; Q9Z2F5; 4.
DR MINT; Q9Z2F5; -.
DR STRING; 10116.ENSRNOP00000062945; -.
DR iPTMnet; Q9Z2F5; -.
DR PhosphoSitePlus; Q9Z2F5; -.
DR jPOST; Q9Z2F5; -.
DR PaxDb; Q9Z2F5; -.
DR PRIDE; Q9Z2F5; -.
DR Ensembl; ENSRNOT00000112665; ENSRNOP00000080240; ENSRNOG00000005428.
DR GeneID; 29382; -.
DR KEGG; rno:29382; -.
DR UCSC; RGD:2441; rat.
DR CTD; 1487; -.
DR RGD; 2441; Ctbp1.
DR eggNOG; KOG0067; Eukaryota.
DR GeneTree; ENSGT00940000157061; -.
DR HOGENOM; CLU_019796_1_3_1; -.
DR InParanoid; Q9Z2F5; -.
DR OrthoDB; 700058at2759; -.
DR PhylomeDB; Q9Z2F5; -.
DR Reactome; R-RNO-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-RNO-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-RNO-4641265; Repression of WNT target genes.
DR EvolutionaryTrace; Q9Z2F5; -.
DR PRO; PR:Q9Z2F5; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Genevisible; Q9Z2F5; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IMP:CAFA.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:SynGO.
DR GO; GO:0098793; C:presynapse; IDA:SynGO.
DR GO; GO:0098831; C:presynaptic active zone cytoplasmic component; ISO:RGD.
DR GO; GO:0017053; C:transcription repressor complex; ISS:UniProtKB.
DR GO; GO:0016746; F:acyltransferase activity; TAS:RGD.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
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:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0001222; F:transcription corepressor binding; ISO:RGD.
DR GO; GO:0031507; P:heterochromatin assembly; ISO:RGD.
DR GO; GO:0061025; P:membrane fusion; TAS:RGD.
DR GO; GO:0035067; P:negative regulation of histone acetylation; ISO:RGD.
DR GO; GO:0090241; P:negative regulation of histone H4 acetylation; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0031065; P:positive regulation of histone deacetylation; ISO:RGD.
DR GO; GO:0099526; P:presynapse to nucleus signaling pathway; IDA:SynGO.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0050872; P:white fat cell differentiation; 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 1: Evidence at protein level;
KW 3D-structure; ADP-ribosylation; Cytoplasm; Differentiation;
KW Direct protein sequencing; Isopeptide bond; NAD; Nucleus; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Repressor; Synapse; Synaptosome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..430
FT /note="C-terminal-binding protein 1"
FT /id="PRO_0000076043"
FT REGION 1..59
FT /note="Interaction with GLIS2 1"
FT /evidence="ECO:0000250"
FT REGION 277..349
FT /note="Interaction with GLIS2 2"
FT /evidence="ECO:0000250"
FT REGION 398..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 255
FT /evidence="ECO:0000250"
FT ACT_SITE 284
FT /evidence="ECO:0000250"
FT ACT_SITE 304
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12805226,
FT ECO:0000269|PubMed:16940172"
FT BINDING 169..174
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12805226,
FT ECO:0000269|PubMed:16940172"
FT BINDING 193
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12805226,
FT ECO:0000269|PubMed:16940172"
FT BINDING 226..232
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12805226,
FT ECO:0000269|PubMed:16940172"
FT BINDING 253..255
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12805226,
FT ECO:0000269|PubMed:16940172"
FT BINDING 279
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12805226,
FT ECO:0000269|PubMed:16940172"
FT SITE 364..365
FT /note="Cleavage; by CAPN1"
FT /evidence="ECO:0000250|UniProtKB:Q13363"
FT SITE 377..378
FT /note="Cleavage; by CAPN1"
FT /evidence="ECO:0000250|UniProtKB:Q13363"
FT SITE 399..400
FT /note="Cleavage; by CAPN1 and CAPN3"
FT /evidence="ECO:0000250|UniProtKB:Q13363"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13363"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13363"
FT CROSSLNK 418
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT MUTAGEN 41
FT /note="A->E: Strongly reduces interaction with E1A."
FT /evidence="ECO:0000269|PubMed:12805226"
FT MUTAGEN 55
FT /note="V->R: Strongly reduces interaction with E1A."
FT /evidence="ECO:0000269|PubMed:12805226"
FT MUTAGEN 172
FT /note="G->E: Loss dimerization and of NAD binding."
FT /evidence="ECO:0000269|PubMed:19351597"
FT CONFLICT 175
FT /note="G -> S (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 18..23
FT /evidence="ECO:0007829|PDB:1HKU"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:1HKU"
FT HELIX 31..34
FT /evidence="ECO:0007829|PDB:1HKU"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:1HKU"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:1HKU"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:1HKU"
FT HELIX 53..58
FT /evidence="ECO:0007829|PDB:1HKU"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:1HKU"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:1HKU"
FT HELIX 72..76
FT /evidence="ECO:0007829|PDB:1HKU"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:1HKU"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:1HL3"
FT HELIX 96..101
FT /evidence="ECO:0007829|PDB:1HKU"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:1HKU"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:1HKU"
FT HELIX 114..130
FT /evidence="ECO:0007829|PDB:1HKU"
FT HELIX 132..140
FT /evidence="ECO:0007829|PDB:1HKU"
FT HELIX 148..154
FT /evidence="ECO:0007829|PDB:1HKU"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:1HKU"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:1HKU"
FT HELIX 173..183
FT /evidence="ECO:0007829|PDB:1HKU"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:1HKU"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:1HKU"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:3GA0"
FT HELIX 200..203
FT /evidence="ECO:0007829|PDB:1HKU"
FT HELIX 212..218
FT /evidence="ECO:0007829|PDB:1HKU"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:1HKU"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:1HL3"
FT HELIX 238..243
FT /evidence="ECO:0007829|PDB:1HKU"
FT STRAND 248..252
FT /evidence="ECO:0007829|PDB:1HKU"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:1HKU"
FT HELIX 261..269
FT /evidence="ECO:0007829|PDB:1HKU"
FT STRAND 272..279
FT /evidence="ECO:0007829|PDB:1HKU"
FT STRAND 282..285
FT /evidence="ECO:0007829|PDB:1HKU"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:1HL3"
FT TURN 292..295
FT /evidence="ECO:0007829|PDB:1HKU"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:1HKU"
FT HELIX 310..329
FT /evidence="ECO:0007829|PDB:1HKU"
FT TURN 332..334
FT /evidence="ECO:0007829|PDB:1HKU"
FT STRAND 337..340
FT /evidence="ECO:0007829|PDB:1HKU"
FT HELIX 342..344
FT /evidence="ECO:0007829|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
