ID CTBP2_RAT Reviewed; 445 AA. AC Q9EQH5; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 2. DT 19-MAR-2014, entry version 88. DE RecName: Full=C-terminal-binding protein 2; DE Short=CtBP2; GN Name=Ctbp2; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 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 GENOMIC DNA]. RC STRAIN=Brown Norway; RX PubMed=15057822; DOI=10.1038/nature02426; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., RA Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., RA Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., RA Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., RA Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., RA Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., RA Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., RA Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., RA Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., RA D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., RA Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., RA Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., RA Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., RA Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., RA Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., RA Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., RA Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., RA Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., RA Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., RA Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., RA Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., RA Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., RA Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., RA Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., RA Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., RA Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., RA Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., RA Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., RA Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., RA Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., RA Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., RA Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., RA Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., RA Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., RA Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into RT mammalian evolution."; RL Nature 428:493-521(2004). CC -!- FUNCTION: Corepressor targeting diverse transcription regulators. CC Functions in brown adipose tissue (BAT) differentiation. Isoform 2 CC probably acts as a scaffold for specialized synapses (By CC similarity). CC -!- SUBUNIT: Interacts with HIPK2, ZNF217 and PNN (By similarity). CC Interacts with the transcription factors BKLF, delta CC EF1/AREB6/ZEB, EVI-1 and Friend of GATA (FOG) via the consensus CC motif P-X-[DNS]-L-[STVA]. Can form a complex with BKLF on a CACCC- CC box oligonucleotide. Can form homodimers or heterodimers of CTBP1 CC and CTBP2. Interacts with NRIP1 and WIZ. Interacts with PRDM16; CC represses white adipose tissue (WAT)-specific genes expression (By CC similarity). CC -!- SUBCELLULAR LOCATION: Nucleus (Potential). Cell junction, synapse CC (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9EQH5-1; Sequence=Displayed; CC Name=2; Synonyms=Ribeye; CC IsoId=Q9EQH5-2; Sequence=VSP_027611; CC -!- TISSUE SPECIFICITY: Isoform 2 is specifically localized in CC synaptic ribbon (at protein level). CC -!- PTM: Phosphorylation by HIPK2 on Ser-428 induces proteasomal CC degradation (By similarity). CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid CC dehydrogenase family. 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; AF222712; AAG45952.1; -; mRNA. DR EMBL; AABR03001613; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AABR03000195; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; NP_445787.1; NM_053335.1. DR UniGene; Rn.138124; -. DR ProteinModelPortal; Q9EQH5; -. DR SMR; Q9EQH5; 33-362. DR BioGrid; 249593; 1. DR STRING; 10116.ENSRNOP00000023404; -. DR PaxDb; Q9EQH5; -. DR PRIDE; Q9EQH5; -. DR Ensembl; ENSRNOT00000023404; ENSRNOP00000023404; ENSRNOG00000017326. [Q9EQH5-2] DR Ensembl; ENSRNOT00000023574; ENSRNOP00000023574; ENSRNOG00000017326. [Q9EQH5-1] DR GeneID; 81717; -. DR KEGG; rno:81717; -. DR UCSC; RGD:68372; rat. [Q9EQH5-1] DR CTD; 1488; -. DR RGD; 68372; Ctbp2. DR eggNOG; COG0111; -. DR GeneTree; ENSGT00530000063021; -. DR HOGENOM; HOG000136701; -. DR HOVERGEN; HBG001898; -. DR KO; K04496; -. DR OMA; MEDADIK; -. DR OrthoDB; EOG761BT9; -. DR TreeFam; TF313593; -. DR NextBio; 615359; -. DR PRO; PR:Q9EQH5; -. DR Genevestigator; Q9EQH5; -. DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW. DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell. DR GO; GO:0017053; C:transcriptional repressor complex; ISS:UniProtKB. 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:0003714; F:transcription corepressor activity; IEA:Ensembl. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0050872; P:white fat cell differentiation; ISS:UniProtKB. DR Gene3D; 3.40.50.720; -; 2. DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom. DR InterPro; IPR006140; D-isomer_2_OHA_DH_NAD-bd. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00389; 2-Hacid_dh; 1. DR Pfam; PF02826; 2-Hacid_dh_C; 1. DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cell junction; Complete proteome; KW Differentiation; NAD; Nucleus; Oxidoreductase; Phosphoprotein; KW Reference proteome; Repressor; Synapse; Transcription; KW Transcription regulation. FT CHAIN 1 445 C-terminal-binding protein 2. FT /FTId=PRO_0000299356. FT NP_BIND 186 191 NAD (By similarity). FT NP_BIND 243 249 NAD (By similarity). FT NP_BIND 270 272 NAD (By similarity). FT NP_BIND 321 324 NAD (By similarity). FT ACT_SITE 272 272 By similarity. FT ACT_SITE 301 301 By similarity. FT ACT_SITE 321 321 Proton donor (By similarity). FT BINDING 106 106 NAD (By similarity). FT BINDING 210 210 NAD (By similarity). FT BINDING 296 296 NAD (By similarity). FT MOD_RES 428 428 Phosphoserine; by HIPK2 (By similarity). FT VAR_SEQ 1 20 MALVDKHKVKRQRLDRICEG -> MPVPSRHINIGRSQSWD FT AAGWYEGPWENAGPPGRRSSLTYGPGEGVWCELVNHRAQDT FT ESCLSREAFYNSLASRKGSVPDFTFYDSRQAVMSGRGSVLP FT QDYYGDPSRGTRVPKEPPFYRDPGTSRPVPSYGVLGSRIPW FT EQVQGQLPALQDAGHLYRESGSKTVLHGQRTHCRAPSPGRY FT GREQPDSRLGIEVPTYSPNSSQVYNDICERPVDSTHARQVA FT PTCLVVDPSSTAPTENSTGVAPGSLNRGYGPTRESIHSKLA FT YENYEADLSTFQGPGGKRTVYPEFLALLRAEGVAEATLAAL FT LQQGFDSPAVLATLEDADIKSVAPNLGQARVLSRLVSSCRT FT EMQFRRQDRTGPPPRHRSSSFSHRSELLPNDTASLGTTALQ FT FHPAGPLQTPSPRGGDLGRRPSSAPSQHLLETAATYSAPVV FT GSQTPHLPSNSGYSSPTPCALTARLASSYPSQAGVALTANP FT GPSVPLHSSPRTAYSTSYTVPMELLKRERSVTASPLPSPHA FT SPQLLRKPGAAPVEPAALPPVRQSLHTPHPPYQKVARRTGA FT PIIVSTMLTPEPS (in isoform 2). FT /FTId=VSP_027611. SQ SEQUENCE 445 AA; 48987 MW; 403012CDEB2E492B CRC64; MALVDKHKVK RQRLDRICEG IRPQIMNGPL HPRPLVALLD GRDCTVEMPI LKDLATVAFC DAQSTQEIHE KVLNEAVGAM MYHTITLTRE DLEKFKALRV IVRIGSGYDN VDIKAAGELG IAVCNIPSAA VEETADSTVC HILNLYRRNT WLYQALREGT RVQSVEQIRE VASGAARIRG ETLGLIGFGR TGQAVAVRAK AFGFSVIFYD PYLQDGIERS LGVQRVYTLQ DLLYQSDCVS LHCNLNEHNH HLINDFTIKQ MRQGAFLVNA ARGGLVDEKA LAQALKEGRI RGAALDVHES EPFSFAQGPL KDAPNLICTP HTAWYSEQAS LEMREAAATE IRRAITGRIP ESLRNCVNKE FFVTSTPWSV IDQQAIHPEL NGATYRYPPG IVGVAPGGLP PAMEGIIPGG IPVTHNLPTV AHPSQAPSPN QPTKHGDNRE HPNEQ //