10         20         30         40         50         60
         |          |          |          |          |          |
MSGVRPPIMN GPMHPRPLVA LLDGRDCTVE MPILKDVATV AFCDAQSTQE IHEKVLNEAV - 60
GALMYHTITL TREDLEKFKA LRIIVRIGSG FDNIDIKSAG DLGIAVCNVP AASVEETADS - 120
TLCHILNLYR RTTWLHQALR EGTRVQSVEQ IREVASGAAR IRGETLGIIG LGRVGQAVAL - 180
RAKAFGFNVL FYDPYLSDGI ERALGLQRVS TLQDLLFHSD CVTLHCGLNE HNHHLINDFT - 240
VKQMRQGAFL VNTARGGLVD EKALAQALKE GRIRGAALDV HESEPFSFSQ GPLKDAPNLI - 300
CTPHAAWYSE QASIEMREEA AREIRRAITG RIPDSLKNCV NKDHLTAATH WASMDPAVVH - 360
PELNGAAYSR YPPGVVSVAP TGIPAAVEGI VPSAMSLSHG LPPVAHPPHA PSPGQTVKPE - 420
ADRDHTTDQL

C-terminal binding proteins (CtBPs) belong to a recently discovered protein family, hosting isoforms CtBP1, 2, and 3, that show distinct functions according to their cellular localization. In the nucleus, CtBPs act as transcriptional corepressors, targeting DNA-binding proteins. Two-hybrid screens have been identified in Drosophila and mammals about three dozen CtBP-interacting transcription factors. CtBP corepressor activity has been proposed to rely on its ability to oligomerize, thus acting as a scaffold in the formation of a multiprotein complex that hosts the essential components of both gene targeting and coordinated histone modifications, thus allowing repression of the targeted genes. In isolated Golgi apparatus the CtBP3 isoform (previously known as BARS [Brefeldin A-ADP Ribosylated Substrate] and recently renamed as short-CtBP1 or CtBP1-S) has been shown to be a key component of the machinery controlling Golgi tubule fission. The CtBP fission inducing activity was shown to participate in the fragmentation of the Golgi complex during mitosis and in intracellular membrane traffic. Thus, based on its ability to fulfill different functions depending on cellular localization, CtBP has been described as a moonlighting protein. Involved in controlling the equilibrium between tubular and stacked structures in the Golgi complex. Corepressor targeting diverse transcription regulators such as GLIS2. Has dehydrogenase activity. Functions in brown adipose tissue (BAT) differentiation.