CTBP2_BOVIN
ID CTBP2_BOVIN Reviewed; 445 AA.
AC Q0VCQ1; Q9GKK1;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=C-terminal-binding protein 2;
DE Short=CtBP2;
GN Name=CTBP2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PARTIAL PROTEIN SEQUENCE (ISOFORM
RP 2), AND TISSUE SPECIFICITY.
RX PubMed=11163272; DOI=10.1016/s0896-6273(00)00159-8;
RA Schmitz F., Koenigstorfer A., Suedhof T.C.;
RT "RIBEYE, a component of synaptic ribbons: a protein's journey through
RT evolution provides insight into synaptic ribbon function.";
RL Neuron 28:857-872(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Corepressor targeting diverse transcription regulators.
CC Functions in brown adipose tissue (BAT) differentiation (By
CC similarity). Isoform 2 probably acts as a scaffold for specialized
CC synapses. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the C-terminus of adenovirus E1A protein. Can
CC form homodimers or heterodimers of CTBP1 and CTBP2. Interacts with
CC HIPK2. Interacts with ZNF217, PNN, NRIP1 and WIZ. Interacts with
CC PRDM16; represses white adipose tissue (WAT)-specific genes expression
CC (By similarity). Interacts with MCRIP1 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P56545}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Synapse {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q0VCQ1-1; Sequence=Displayed;
CC Name=2; Synonyms=Ribeye;
CC IsoId=Q0VCQ1-2; Sequence=VSP_027614;
CC -!- TISSUE SPECIFICITY: Isoform 2 is specifically localized in synaptic
CC ribbon (at protein level). {ECO:0000269|PubMed:11163272}.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; AF222713; AAG45953.1; -; mRNA.
DR EMBL; BC120058; AAI20059.1; -; mRNA.
DR RefSeq; NP_783643.1; NM_175712.1. [Q0VCQ1-2]
DR RefSeq; XP_005225890.1; XM_005225833.2. [Q0VCQ1-1]
DR RefSeq; XP_005225892.1; XM_005225835.3.
DR AlphaFoldDB; Q0VCQ1; -.
DR SMR; Q0VCQ1; -.
DR STRING; 9913.ENSBTAP00000004405; -.
DR PaxDb; Q0VCQ1; -.
DR PRIDE; Q0VCQ1; -.
DR Ensembl; ENSBTAT00000004404; ENSBTAP00000004404; ENSBTAG00000003397. [Q0VCQ1-1]
DR Ensembl; ENSBTAT00000083896; ENSBTAP00000072639; ENSBTAG00000003397. [Q0VCQ1-1]
DR Ensembl; ENSBTAT00000084737; ENSBTAP00000072614; ENSBTAG00000003397. [Q0VCQ1-1]
DR GeneID; 281730; -.
DR KEGG; bta:281730; -.
DR CTD; 1488; -.
DR VEuPathDB; HostDB:ENSBTAG00000003397; -.
DR eggNOG; KOG0067; Eukaryota.
DR GeneTree; ENSGT00940000154430; -.
DR HOGENOM; CLU_019796_1_3_1; -.
DR InParanoid; Q0VCQ1; -.
DR OMA; TCHTAFY; -.
DR OrthoDB; 700058at2759; -.
DR Reactome; R-BTA-4641265; Repression of WNT target genes.
DR Proteomes; UP000009136; Chromosome 26.
DR Bgee; ENSBTAG00000003397; Expressed in retina and 103 other tissues.
DR ExpressionAtlas; Q0VCQ1; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0098684; C:photoreceptor ribbon synapse; IDA:SynGO.
DR GO; GO:0098831; C:presynaptic active zone cytoplasmic component; IDA:SynGO.
DR GO; GO:0017053; C:transcription repressor complex; ISS:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IBA:GO_Central.
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: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; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
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; 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; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Differentiation; Direct protein sequencing;
KW Methylation; NAD; Nucleus; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Repressor; Synapse; Transcription;
KW Transcription regulation.
FT CHAIN 1..445
FT /note="C-terminal-binding protein 2"
FT /id="PRO_0000284890"
FT REGION 414..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 272
FT /evidence="ECO:0000250"
FT ACT_SITE 301
FT /evidence="ECO:0000250"
FT ACT_SITE 321
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 186..191
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 210
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 243..249
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 270..272
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 296
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 321..324
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT MOD_RES 22
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P56545"
FT MOD_RES 428
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P56545"
FT VAR_SEQ 1..20
FT /note="MALVDKHKVKRQRLDRICEG -> MPVPSRHINIGRSQSWDAAGWYEGPWEV
FT AEAPGRRSSLTDGGGEGLWYPGLRDVAMPGAAEPCLYREAFYSTAAGRKSSVPDFAFYD
FT SRQAVMSARGALLPGDYYSDPAGAARAPGEPLHHRHPGAGQPLPGYGAPGGRMTWEPVA
FT ARAPALQDTGHLYRDPGGKMIPQGQRSHSRAPSPAQYIGEPADSRYGAEAPAYPTGQVY
FT NNASERPVDSAASRQAAPTCLVVDPGAAAASGIGVGTAPSAPPRGYGPAREGVHPRMAY
FT ERCESDPSAFQGPGGSKRSVMPEFLALLRAEGVSEATPVALLQQGFDSPAVLATMEDAD
FT IKCVAPNLGQARVLSRLASGCRTEMQLRRQGRGPPLPRTRSSSFSHRSELQGDQVGLGA
FT AALQPQPQPQAGPLQAASPRAVDPAHRRPSSAPSQHLLETAATYSGPRVGAQAAHFPSN
FT SGYSSPTPCALTARPSPAYPLQPGVPLTHPGPRTAYSTAYTVPMELLKRERGAAVSPVP
FT SPHGSPQLLRKPGAPLEPPALPPASQSLHTPHSPYQKVARRTGAPIIVSTMLAPEPS
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11163272"
FT /id="VSP_027614"
SQ SEQUENCE 445 AA; 48947 MW; 413399EE65099A09 CRC64;
MALVDKHKVK RQRLDRICEG IRPQIMNGPL HPRPLVALLD GRDCTVEMPI LKDLATVAFC
DAQSTQEIHE KVLNEAVGAM MYHTITLTRE DLEKFKALRV IVRIGSGYDN VDIKAAGELG
IAVCNIPSAA VEETADSTIC HILNLYRRNT WLYQALREGT RVQSVEQIRE VASGAARIRG
ETLGLIGFGR TGQAVAVRAK AFGFSVLFYD PYLQDGTERS LGVQRVYTLQ DLLYQSDCVS
LHCNLNEHNH HLINDFTIKQ MRQGAFLVNA ARGGLVDEKA LAQALKEGRI RGAALDVHES
EPFSFAQGPL KDAPNLICTP HTAWYSEQAS LEMREAAATE IRRAITGRIP ESLRNCVNKE
FFVTTAPWSV IDQQAIHPEL NGATYRYPPG IVGVAPGGLP AAMEGIIPGG IPVTHNLPTV
AHPSQAPSPN QPTKHGDNRE HPNEQ
