CTBP1_HUMAN
ID CTBP1_HUMAN Reviewed; 440 AA.
AC Q13363; Q4W5N3; Q7Z2Q5;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 229.
DE RecName: Full=C-terminal-binding protein 1;
DE Short=CtBP1;
DE EC=1.1.1.-;
GN Name=CTBP1; Synonyms=CTBP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 98-108, AND
RP INTERACTION WITH RBBP8 AND ADENOVIRUS E1A.
RC TISSUE=B-cell, and Cervix carcinoma;
RX PubMed=7479821; DOI=10.1073/pnas.92.23.10467;
RA Schaeper U., Boyd J.M., Verma S., Uhlmann E., Subramanian T.,
RA Chinnadurai G.;
RT "Molecular cloning and characterization of a cellular phosphoprotein that
RT interacts with a conserved C-terminal domain of adenovirus E1A involved in
RT negative modulation of oncogenic transformation.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:10467-10471(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SEQUENCE REVISION, AND FUNCTION.
RX PubMed=9858600; DOI=10.1128/mcb.19.1.777;
RA Sewalt R.G.A.B., Gunster M.J., van der Vlag J., Satijn D.P.E., Otte A.P.;
RT "C-terminal binding protein is a transcriptional repressor that interacts
RT with a specific class of vertebrate polycomb proteins.";
RL Mol. Cell. Biol. 19:777-787(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 410-415, INTERACTION WITH SIMC1, PROTEOLYTIC CLEAVAGE
RP SITES, AND MUTAGENESIS OF ALA-52; VAL-66; GLY-183; GLY-186 AND ASP-204.
RX PubMed=23707407; DOI=10.1016/j.jmb.2013.05.009;
RA Ono Y., Iemura S., Novak S.M., Doi N., Kitamura F., Natsume T.,
RA Gregorio C.C., Sorimachi H.;
RT "PLEIAD/SIMC1/C5orf25, a novel autolysis regulator for a skeletal-muscle-
RT specific calpain, CAPN3, scaffolds a CAPN3 substrate, CTBP1.";
RL J. Mol. Biol. 425:2955-2972(2013).
RN [7]
RP INTERACTION WITH ADENOVIRUS E1A (MICROBIAL INFECTION), AND PHOSPHORYLATION.
RX PubMed=8440238; DOI=10.1002/j.1460-2075.1993.tb05679.x;
RA Boyd J.M., Subramanian T., Schaeper U., la Regina M., Bayley S.,
RA Chinnadurai G.;
RT "A region in the C-terminus of adenovirus 2/5 E1a protein is required for
RT association with a cellular phosphoprotein and important for the negative
RT modulation of T24-ras mediated transformation, tumorigenesis and
RT metastasis.";
RL EMBO J. 12:469-478(1993).
RN [8]
RP INTERACTION WITH MECOM.
RX PubMed=11568182; DOI=10.1074/jbc.m106733200;
RA Chakraborty S., Senyuk V., Sitailo S., Chi Y., Nucifora G.;
RT "Interaction of EVI1 with cAMP-responsive element-binding protein-binding
RT protein (CBP) and p300/CBP-associated factor (P/CAF) results in reversible
RT acetylation of EVI1 and in co-localization in nuclear speckles.";
RL J. Biol. Chem. 276:44936-44943(2001).
RN [9]
RP INTERACTION WITH EPSTEIN-BARR VIRUS/EBV PROTEIN EBNA6 (MICROBIAL
RP INFECTION).
RX PubMed=11462050; DOI=10.1128/jvi.75.16.7749-7755.2001;
RA Touitou R., Hickabottom M., Parker G., Crook T., Allday M.J.;
RT "Physical and functional interactions between the corepressor CtBP and the
RT Epstein-Barr virus nuclear antigen EBNA3C.";
RL J. Virol. 75:7749-7755(2001).
RN [10]
RP INTERACTION WITH NRIP1.
RX PubMed=11509661; DOI=10.1128/mcb.21.18.6181-6188.2001;
RA Vo N., Fjeld C., Goodman R.H.;
RT "Acetylation of nuclear hormone receptor-interacting protein RIP140
RT regulates binding of the transcriptional corepressor CtBP.";
RL Mol. Cell. Biol. 21:6181-6188(2001).
RN [11]
RP INTERACTION WITH EPSTEIN-BARR VIRUS/EBV PROTEIN EBNA3 (MICROBIAL
RP INFECTION).
RX PubMed=12372828; DOI=10.1074/jbc.m208116200;
RA Hickabottom M., Parker G.A., Freemont P., Crook T., Allday M.J.;
RT "Two nonconsensus sites in the Epstein-Barr virus oncoprotein EBNA3A
RT cooperate to bind the co-repressor carboxyl-terminal-binding protein
RT (CtBP).";
RL J. Biol. Chem. 277:47197-47204(2002).
RN [12]
RP SUMOYLATION AT LYS-428, AND SUBCELLULAR LOCATION.
RX PubMed=12679040; DOI=10.1016/s0092-8674(03)00159-4;
RA Kagey M.H., Melhuish T.A., Wotton D.;
RT "The polycomb protein Pc2 is a SUMO E3.";
RL Cell 113:127-137(2003).
RN [13]
RP INTERACTION WITH HIPK2, PHOSPHORYLATION AT SER-422, AND MUTAGENESIS OF
RP SER-422.
RX PubMed=14567915; DOI=10.1016/s0092-8674(03)00802-x;
RA Zhang Q., Yoshimatsu Y., Hildebrand J., Frisch S.M., Goodman R.H.;
RT "Homeodomain interacting protein kinase 2 promotes apoptosis by
RT downregulating the transcriptional corepressor CtBP.";
RL Cell 115:177-186(2003).
RN [14]
RP FUNCTION IN TRANSCRIPTIONAL REPRESSION, AND INTERACTION WITH PNN.
RX PubMed=15542832; DOI=10.1128/mcb.24.23.10223-10235.2004;
RA Alpatov R., Munguba G.C., Caton P., Joo J.H., Shi Y., Shi Y., Hunt M.E.,
RA Sugrue S.P.;
RT "Nuclear speckle-associated protein Pnn/DRS binds to the transcriptional
RT corepressor CtBP and relieves CtBP-mediated repression of the E-cadherin
RT gene.";
RL Mol. Cell. Biol. 24:10223-10235(2004).
RN [15]
RP INTERACTION WITH NRIP1.
RX PubMed=15060175; DOI=10.1093/nar/gkh524;
RA Castet A., Boulahtouf A., Versini G., Bonnet S., Augereau P., Vignon F.,
RA Khochbin S., Jalaguier S., Cavailles V.;
RT "Multiple domains of the receptor-interacting protein 140 contribute to
RT transcription inhibition.";
RL Nucleic Acids Res. 32:1957-1966(2004).
RN [16]
RP INTERACTION WITH ZFHX1B.
RX PubMed=16061479; DOI=10.1074/jbc.m504477200;
RA Long J., Zuo D., Park M.;
RT "Pc2-mediated sumoylation of Smad-interacting protein 1 attenuates
RT transcriptional repression of E-cadherin.";
RL J. Biol. Chem. 280:35477-35489(2005).
RN [17]
RP INTERACTION WITH MECOM.
RX PubMed=15897867; DOI=10.1038/sj.onc.1208754;
RA Nitta E., Izutsu K., Yamaguchi Y., Imai Y., Ogawa S., Chiba S.,
RA Kurokawa M., Hirai H.;
RT "Oligomerization of Evi-1 regulated by the PR domain contributes to
RT recruitment of corepressor CtBP.";
RL Oncogene 24:6165-6173(2005).
RN [18]
RP INTERACTION WITH FOXP1.
RX PubMed=16609867; DOI=10.1007/s00427-006-0073-8;
RA Schoen C., Wochnik A., Roessner A., Donow C., Knoechel W.;
RT "The FoxP subclass in Xenopus laevis development.";
RL Dev. Genes Evol. 216:641-646(2006).
RN [19]
RP INTERACTION WITH WIZ.
RX PubMed=16702210; DOI=10.1074/jbc.m603087200;
RA Ueda J., Tachibana M., Ikura T., Shinkai Y.;
RT "Zinc finger protein Wiz links G9a/GLP histone methyltransferases to the
RT co-repressor molecule CtBP.";
RL J. Biol. Chem. 281:20120-20128(2006).
RN [20]
RP INTERACTION WITH ZNF366.
RX PubMed=16393996; DOI=10.4049/jimmunol.176.2.1081;
RA Triantis V., Trancikova D.E., Looman M.W., Hartgers F.C., Janssen R.A.,
RA Adema G.J.;
RT "Identification and characterization of DC-SCRIPT, a novel dendritic cell-
RT expressed member of the zinc finger family of transcriptional regulators.";
RL J. Immunol. 176:1081-1089(2006).
RN [21]
RP INTERACTION WITH ZNF366.
RX PubMed=17085477; DOI=10.1093/nar/gkl875;
RA Lopez-Garcia J., Periyasamy M., Thomas R.S., Christian M., Leao M., Jat P.,
RA Kindle K.B., Heery D.M., Parker M.G., Buluwela L., Kamalati T., Ali S.;
RT "ZNF366 is an estrogen receptor corepressor that acts through CtBP and
RT histone deacetylases.";
RL Nucleic Acids Res. 34:6126-6136(2006).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [23]
RP FUNCTION AS COREPRESSOR, INTERACTION WITH BCL6, AND TISSUE SPECIFICITY.
RX PubMed=18212045; DOI=10.1128/mcb.01400-07;
RA Mendez L.M., Polo J.M., Yu J.J., Krupski M., Ding B.B., Melnick A.,
RA Ye B.H.;
RT "CtBP is an essential corepressor for BCL6 autoregulation.";
RL Mol. Cell. Biol. 28:2175-2186(2008).
RN [24]
RP FUNCTION, AND INTERACTION WITH SATB1.
RX PubMed=19103759; DOI=10.1128/mcb.00822-08;
RA Purbey P.K., Singh S., Notani D., Kumar P.P., Limaye A.S., Galande S.;
RT "Acetylation-dependent interaction of SATB1 and CtBP1 mediates
RT transcriptional repression by SATB1.";
RL Mol. Cell. Biol. 29:1321-1337(2009).
RN [25]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [27]
RP INTERACTION WITH HADV5 E1A (MICROBIAL INFECTION).
RX PubMed=23747199; DOI=10.1016/j.virol.2013.05.018;
RA Subramanian T., Zhao L.J., Chinnadurai G.;
RT "Interaction of CtBP with adenovirus E1A suppresses immortalization of
RT primary epithelial cells and enhances virus replication during productive
RT infection.";
RL Virology 443:313-320(2013).
RN [28]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [29]
RP INTERACTION WITH MCRIP1.
RX PubMed=25728771; DOI=10.1016/j.molcel.2015.01.023;
RA Ichikawa K., Kubota Y., Nakamura T., Weng J.S., Tomida T., Saito H.,
RA Takekawa M.;
RT "MCRIP1, an ERK substrate, mediates ERK-induced gene silencing during
RT epithelial-mesenchymal transition by regulating the co-repressor CtBP.";
RL Mol. Cell 58:35-46(2015).
RN [30]
RP INVOLVEMENT IN HADDTS, AND VARIANT HADDTS TRP-342.
RX PubMed=27094857; DOI=10.1007/s10048-016-0482-4;
RA Beck D.B., Cho M.T., Millan F., Yates C., Hannibal M., O'Connor B.,
RA Shinawi M., Connolly A.M., Waggoner D., Halbach S., Angle B., Sanders V.,
RA Shen Y., Retterer K., Begtrup A., Bai R., Chung W.K.;
RT "A recurrent de novo CTBP1 mutation is associated with developmental delay,
RT hypotonia, ataxia, and tooth enamel defects.";
RL Neurogenetics 17:173-178(2016).
RN [31]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 28-353 IN COMPLEX WITH NAD,
RP FUNCTION, COFACTOR, MUTAGENESIS OF CYS-134; ASN-138; ARG-141;
RP 141-ARG-ARG-142; LEU-150; ARG-163; ARG-171; GLY-181; GLY-183; ASP-204;
RP ARG-266; ASP-290; GLU-295 AND HIS-315, AND DIMERIZATION.
RX PubMed=12419229; DOI=10.1016/s1097-2765(02)00650-0;
RA Kumar V., Carlson J.E., Ohgi K.A., Edwards T.A., Rose D.W., Escalante C.R.,
RA Rosenfeld M.G., Aggarwal A.K.;
RT "Transcription corepressor CtBP is an NAD(+)-regulated dehydrogenase.";
RL Mol. Cell 10:857-869(2002).
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:12419229, ECO:0000269|PubMed:15542832,
CC ECO:0000269|PubMed:18212045, ECO:0000269|PubMed:19103759,
CC ECO:0000269|PubMed:9858600}.
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000269|PubMed:12419229};
CC Note=NAD is required for efficient interaction with E1A. Cofactor
CC binding induces a conformation change. {ECO:0000269|PubMed:12419229};
CC -!- SUBUNIT: Homo- or heterodimer. Heterodimer with CTBP2. Interacts with
CC PRDM16; the interaction represses white adipose tissue (WAT)-specific
CC genes expression. Interacts with GLIS2, FOXP2, HDAC4, HDAC5, HDAC9 and
CC ZNF217. Interacts with ELK3 (via its PXDLS motif). Interacts with RBBP8
CC (via its PXDLS motif); the interaction is disrupted by binding to
CC adenovirus E1A. Interacts with FOXP1, HIPK2, PNN, NRIP1, MECOM, ZFHX1B
CC and WIZ. Interacts with ZNF366 (via PXDLS motif) (PubMed:16393996,
CC PubMed:17085477). Interaction with SATB1 (non-acetylated form); the
CC interaction stabilizes its attachment to DNA and promotes transcription
CC repression. 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 (PubMed:25728771). Interacts with Bassoon/BSN;
CC this interaction targets and anchors CTBP1 to presynapses (By
CC similarity). Interacts with SIMC1 (PubMed:23707407).
CC {ECO:0000250|UniProtKB:O88712, ECO:0000269|PubMed:11509661,
CC ECO:0000269|PubMed:11568182, ECO:0000269|PubMed:12419229,
CC ECO:0000269|PubMed:14567915, ECO:0000269|PubMed:15060175,
CC ECO:0000269|PubMed:15542832, ECO:0000269|PubMed:15897867,
CC ECO:0000269|PubMed:16061479, ECO:0000269|PubMed:16393996,
CC ECO:0000269|PubMed:16609867, ECO:0000269|PubMed:16702210,
CC ECO:0000269|PubMed:17085477, ECO:0000269|PubMed:18212045,
CC ECO:0000269|PubMed:19103759, ECO:0000269|PubMed:23707407,
CC ECO:0000269|PubMed:25728771, ECO:0000269|PubMed:7479821}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus EBNA3
CC and EBNA6. {ECO:0000269|PubMed:11462050, ECO:0000269|PubMed:12372828}.
CC -!- SUBUNIT: (Microbial infection) Interacts with adenovirus E1A protein
CC (via its C-terminus); the interaction disrupts the interaction of CTBP1
CC with RBBP8. {ECO:0000269|PubMed:8440238}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human adenovirus 5 E1A
CC protein; this interaction seems to potentiate viral replication.
CC {ECO:0000269|PubMed:23747199}.
CC -!- INTERACTION:
CC Q13363; O00257: CBX4; NbExp=4; IntAct=EBI-908846, EBI-722425;
CC Q13363; Q13363: CTBP1; NbExp=8; IntAct=EBI-908846, EBI-908846;
CC Q13363; P56545: CTBP2; NbExp=13; IntAct=EBI-908846, EBI-741533;
CC Q13363; Q9BXL5: HEMGN; NbExp=2; IntAct=EBI-908846, EBI-3916399;
CC Q13363; Q14526: HIC1; NbExp=2; IntAct=EBI-908846, EBI-2507362;
CC Q13363; O43474: KLF4; NbExp=4; IntAct=EBI-908846, EBI-7232405;
CC Q13363; Q96JN0: LCOR; NbExp=8; IntAct=EBI-908846, EBI-746045;
CC Q13363; Q8N3X6: LCORL; NbExp=6; IntAct=EBI-908846, EBI-7138654;
CC Q13363; P48552: NRIP1; NbExp=3; IntAct=EBI-908846, EBI-746484;
CC Q13363; Q9Y5P3: RAI2; NbExp=3; IntAct=EBI-908846, EBI-746228;
CC Q13363; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-908846, EBI-750109;
CC Q13363; Q96EK4: THAP11; NbExp=3; IntAct=EBI-908846, EBI-1790529;
CC Q13363; Q8N895: ZNF366; NbExp=5; IntAct=EBI-908846, EBI-2813661;
CC Q13363; Q92618: ZNF516; NbExp=14; IntAct=EBI-908846, EBI-2799490;
CC Q13363; A2APF7: Zbp1; Xeno; NbExp=2; IntAct=EBI-908846, EBI-6115394;
CC Q13363-2; Q9H6U6: BCAS3; NbExp=3; IntAct=EBI-10171858, EBI-6083685;
CC Q13363-2; P55273: CDKN2D; NbExp=3; IntAct=EBI-10171858, EBI-745859;
CC Q13363-2; Q76N32: CEP68; NbExp=3; IntAct=EBI-10171858, EBI-9051024;
CC Q13363-2; Q49AN0: CRY2; NbExp=3; IntAct=EBI-10171858, EBI-2212355;
CC Q13363-2; Q13363-2: CTBP1; NbExp=5; IntAct=EBI-10171858, EBI-10171858;
CC Q13363-2; P56545: CTBP2; NbExp=5; IntAct=EBI-10171858, EBI-741533;
CC Q13363-2; P56545-3: CTBP2; NbExp=4; IntAct=EBI-10171858, EBI-10171902;
CC Q13363-2; A0A0S2Z5I3: DMRTB1; NbExp=3; IntAct=EBI-10171858, EBI-16431245;
CC Q13363-2; I6L9A0: DMRTB1; NbExp=3; IntAct=EBI-10171858, EBI-10178554;
CC Q13363-2; O15409: FOXP2; NbExp=7; IntAct=EBI-10171858, EBI-983612;
CC Q13363-2; P09067: HOXB5; NbExp=3; IntAct=EBI-10171858, EBI-3893317;
CC Q13363-2; Q13422: IKZF1; NbExp=3; IntAct=EBI-10171858, EBI-745305;
CC Q13363-2; Q13422-7: IKZF1; NbExp=5; IntAct=EBI-10171858, EBI-11522367;
CC Q13363-2; Q9Y4X4: KLF12; NbExp=6; IntAct=EBI-10171858, EBI-750750;
CC Q13363-2; P57682: KLF3; NbExp=3; IntAct=EBI-10171858, EBI-8472267;
CC Q13363-2; P45984: MAPK9; NbExp=3; IntAct=EBI-10171858, EBI-713568;
CC Q13363-2; O94818-2: NOL4; NbExp=4; IntAct=EBI-10171858, EBI-10190763;
CC Q13363-2; Q96MY1: NOL4L; NbExp=3; IntAct=EBI-10171858, EBI-6660790;
CC Q13363-2; Q9NQ66: PLCB1; NbExp=3; IntAct=EBI-10171858, EBI-3396023;
CC Q13363-2; Q13131: PRKAA1; NbExp=3; IntAct=EBI-10171858, EBI-1181405;
CC Q13363-2; Q15583: TGIF1; NbExp=3; IntAct=EBI-10171858, EBI-714215;
CC Q13363-2; Q15583-2: TGIF1; NbExp=3; IntAct=EBI-10171858, EBI-12691451;
CC Q13363-2; Q63HK5: TSHZ3; NbExp=3; IntAct=EBI-10171858, EBI-9053916;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12679040}. Nucleus
CC {ECO:0000269|PubMed:12679040}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q13363-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13363-2; Sequence=VSP_043305;
CC -!- TISSUE SPECIFICITY: Expressed in germinal center B-cells.
CC {ECO:0000269|PubMed:18212045}.
CC -!- PTM: The level of phosphorylation appears to be regulated during the
CC cell cycle. Phosphorylation by HIPK2 on Ser-422 induces proteasomal
CC degradation. {ECO:0000269|PubMed:14567915, ECO:0000269|PubMed:8440238}.
CC -!- PTM: ADP-ribosylated; when cells are exposed to brefeldin A.
CC {ECO:0000250}.
CC -!- PTM: Sumoylation on Lys-428 is promoted by the E3 SUMO-protein ligase
CC CBX4. {ECO:0000269|PubMed:12679040}.
CC -!- DISEASE: Hypotonia, ataxia, developmental delay, and tooth enamel
CC defect syndrome (HADDTS) [MIM:617915]: An autosomal dominant disorder
CC characterized by delayed motor development, intellectual disability,
CC failure to thrive, hypotonia, ataxia, and tooth enamel defects.
CC {ECO:0000269|PubMed:27094857}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000305}.
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; U37408; AAC62822.1; -; mRNA.
DR EMBL; AF091555; AAD14597.1; -; mRNA.
DR EMBL; AC092535; AAY40989.1; -; Genomic_DNA.
DR EMBL; CH471131; EAW82599.1; -; Genomic_DNA.
DR EMBL; CH471131; EAW82600.1; -; Genomic_DNA.
DR EMBL; CH471131; EAW82601.1; -; Genomic_DNA.
DR EMBL; BC011655; AAH11655.1; -; mRNA.
DR EMBL; BC053320; AAH53320.1; -; mRNA.
DR CCDS; CCDS3348.1; -. [Q13363-1]
DR CCDS; CCDS43203.1; -. [Q13363-2]
DR RefSeq; NP_001012632.1; NM_001012614.1. [Q13363-2]
DR RefSeq; NP_001319.1; NM_001328.2. [Q13363-1]
DR RefSeq; XP_016863253.1; XM_017007764.1. [Q13363-2]
DR RefSeq; XP_016863254.1; XM_017007765.1.
DR RefSeq; XP_016863255.1; XM_017007766.1.
DR RefSeq; XP_016863256.1; XM_017007767.1.
DR PDB; 1MX3; X-ray; 1.95 A; A=28-353.
DR PDB; 4LCE; X-ray; 2.38 A; A=28-353.
DR PDB; 4U6Q; X-ray; 2.30 A; A=28-353.
DR PDB; 4U6S; X-ray; 2.10 A; A=28-353.
DR PDB; 6CDF; X-ray; 2.60 A; A=28-379.
DR PDB; 6CDR; X-ray; 2.40 A; A=28-379.
DR PDB; 6V89; X-ray; 2.45 A; A=28-375.
DR PDB; 6V8A; X-ray; 2.35 A; A=28-375.
DR PDB; 7KWM; X-ray; 2.30 A; A=28-356.
DR PDBsum; 1MX3; -.
DR PDBsum; 4LCE; -.
DR PDBsum; 4U6Q; -.
DR PDBsum; 4U6S; -.
DR PDBsum; 6CDF; -.
DR PDBsum; 6CDR; -.
DR PDBsum; 6V89; -.
DR PDBsum; 6V8A; -.
DR PDBsum; 7KWM; -.
DR AlphaFoldDB; Q13363; -.
DR SMR; Q13363; -.
DR BioGRID; 107869; 334.
DR CORUM; Q13363; -.
DR DIP; DIP-24245N; -.
DR ELM; Q13363; -.
DR IntAct; Q13363; 688.
DR MINT; Q13363; -.
DR STRING; 9606.ENSP00000290921; -.
DR BindingDB; Q13363; -.
DR DrugBank; DB01942; Formic acid.
DR iPTMnet; Q13363; -.
DR PhosphoSitePlus; Q13363; -.
DR SwissPalm; Q13363; -.
DR BioMuta; CTBP1; -.
DR DMDM; 6014741; -.
DR EPD; Q13363; -.
DR jPOST; Q13363; -.
DR MassIVE; Q13363; -.
DR PaxDb; Q13363; -.
DR PeptideAtlas; Q13363; -.
DR PRIDE; Q13363; -.
DR ProteomicsDB; 59349; -. [Q13363-1]
DR ProteomicsDB; 59350; -. [Q13363-2]
DR Antibodypedia; 3783; 700 antibodies from 43 providers.
DR DNASU; 1487; -.
DR Ensembl; ENST00000290921.10; ENSP00000290921.6; ENSG00000159692.16. [Q13363-1]
DR Ensembl; ENST00000382952.8; ENSP00000372411.3; ENSG00000159692.16. [Q13363-2]
DR GeneID; 1487; -.
DR KEGG; hsa:1487; -.
DR MANE-Select; ENST00000382952.8; ENSP00000372411.3; NM_001012614.2; NP_001012632.1. [Q13363-2]
DR UCSC; uc003gcu.2; human. [Q13363-1]
DR CTD; 1487; -.
DR DisGeNET; 1487; -.
DR GeneCards; CTBP1; -.
DR HGNC; HGNC:2494; CTBP1.
DR HPA; ENSG00000159692; Low tissue specificity.
DR MalaCards; CTBP1; -.
DR MIM; 602618; gene.
DR MIM; 617915; phenotype.
DR neXtProt; NX_Q13363; -.
DR OpenTargets; ENSG00000159692; -.
DR Orphanet; 280; Wolf-Hirschhorn syndrome.
DR PharmGKB; PA26995; -.
DR VEuPathDB; HostDB:ENSG00000159692; -.
DR eggNOG; KOG0067; Eukaryota.
DR GeneTree; ENSGT00940000157061; -.
DR HOGENOM; CLU_019796_1_3_1; -.
DR InParanoid; Q13363; -.
DR OMA; HTITLMK; -.
DR OrthoDB; 700058at2759; -.
DR PhylomeDB; Q13363; -.
DR TreeFam; TF313593; -.
DR BioCyc; MetaCyc:ENSG00000159692-MON; -.
DR PathwayCommons; Q13363; -.
DR Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-HSA-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-HSA-4641265; Repression of WNT target genes.
DR Reactome; R-HSA-5339700; Signaling by TCF7L2 mutants.
DR SignaLink; Q13363; -.
DR SIGNOR; Q13363; -.
DR BioGRID-ORCS; 1487; 29 hits in 1087 CRISPR screens.
DR ChiTaRS; CTBP1; human.
DR EvolutionaryTrace; Q13363; -.
DR GeneWiki; CTBP1; -.
DR GenomeRNAi; 1487; -.
DR Pharos; Q13363; Tbio.
DR PRO; PR:Q13363; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q13363; protein.
DR Bgee; ENSG00000159692; Expressed in tendon of biceps brachii and 206 other tissues.
DR ExpressionAtlas; Q13363; baseline and differential.
DR Genevisible; Q13363; HS.
DR GO; GO:0098982; C:GABA-ergic synapse; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0098831; C:presynaptic active zone cytoplasmic component; IEA:Ensembl.
DR GO; GO:0017053; C:transcription repressor complex; IDA:BHF-UCL.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0051287; F:NAD binding; ISS: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:0008022; F:protein C-terminus binding; TAS:ProtInc.
DR GO; GO:0019904; F:protein domain specific binding; IDA:BHF-UCL.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:Ensembl.
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; IDA:BHF-UCL.
DR GO; GO:0001222; F:transcription corepressor binding; IPI:ARUK-UCL.
DR GO; GO:0031507; P:heterochromatin assembly; IMP:BHF-UCL.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:0035067; P:negative regulation of histone acetylation; IMP:BHF-UCL.
DR GO; GO:0090241; P:negative regulation of histone H4 acetylation; IMP:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0031065; P:positive regulation of histone deacetylation; IMP:BHF-UCL.
DR GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:BHF-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0019079; P:viral genome replication; TAS:ProtInc.
DR GO; GO:0050872; P:white fat cell differentiation; ISS:UniProtKB.
DR CDD; cd05299; CtBP_dh; 1.
DR IDEAL; IID00469; -.
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; Alternative splicing; Cytoplasm;
KW Differentiation; Direct protein sequencing; Disease variant;
KW Host-virus interaction; Intellectual disability; Isopeptide bond; NAD;
KW Nucleus; Oxidoreductase; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..440
FT /note="C-terminal-binding protein 1"
FT /id="PRO_0000076041"
FT REGION 1..70
FT /note="Interaction with GLIS2 1"
FT /evidence="ECO:0000250"
FT REGION 288..360
FT /note="Interaction with GLIS2 2"
FT /evidence="ECO:0000250"
FT REGION 408..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 266
FT /evidence="ECO:0000250"
FT ACT_SITE 295
FT /evidence="ECO:0000250"
FT ACT_SITE 315
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 180..185
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 237..243
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 264..266
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 290
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 315..318
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 375..376
FT /note="Cleavage; by CAPN1"
FT /evidence="ECO:0000269|PubMed:23707407"
FT SITE 387..388
FT /note="Cleavage; by CAPN1"
FT /evidence="ECO:0000269|PubMed:23707407"
FT SITE 409..410
FT /note="Cleavage; by CAPN1 and CAPN3"
FT /evidence="ECO:0000269|PubMed:23707407"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 422
FT /note="Phosphoserine; by HIPK2"
FT /evidence="ECO:0000269|PubMed:14567915"
FT CROSSLNK 428
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:12679040"
FT VAR_SEQ 1..13
FT /note="MGSSHLLNKGLPL -> MS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043305"
FT VARIANT 342
FT /note="R -> W (in HADDTS; dbSNP:rs869320802)"
FT /evidence="ECO:0000269|PubMed:27094857"
FT /id="VAR_080622"
FT MUTAGEN 52
FT /note="A->E: Loss of interaction with SIMC1. No effect on
FT its proteolytic processing mediated by CAPN3."
FT /evidence="ECO:0000269|PubMed:23707407"
FT MUTAGEN 66
FT /note="V->R: Loss of interaction with SIMC1. Reduced
FT proteolytic processing mediated by CAPN3."
FT /evidence="ECO:0000269|PubMed:23707407"
FT MUTAGEN 134
FT /note="C->A: Strongly reduces E1A binding; when associated
FT with A-138; A-141 and A-150."
FT /evidence="ECO:0000269|PubMed:12419229"
FT MUTAGEN 138
FT /note="N->A: Strongly reduces E1A binding; when associated
FT with A-134; A-141 and A-150."
FT /evidence="ECO:0000269|PubMed:12419229"
FT MUTAGEN 141..142
FT /note="RR->AA: Strongly reduces E1A binding; when
FT associated with A-163 and A-171."
FT /evidence="ECO:0000269|PubMed:12419229"
FT MUTAGEN 141
FT /note="R->A: Strongly reduces E1A binding; when associated
FT with A-134; A-138 and A-150."
FT /evidence="ECO:0000269|PubMed:12419229"
FT MUTAGEN 150
FT /note="L->A: Strongly reduces E1A binding; when associated
FT with A-134; A-138 and A-141."
FT /evidence="ECO:0000269|PubMed:12419229"
FT MUTAGEN 163
FT /note="R->A: Strongly reduces E1A binding; when associated
FT with A-141; A-142 and A-171."
FT /evidence="ECO:0000269|PubMed:12419229"
FT MUTAGEN 171
FT /note="R->A: Strongly reduces E1A binding; when associated
FT with A-141; A-142 and A-163."
FT /evidence="ECO:0000269|PubMed:12419229"
FT MUTAGEN 181
FT /note="G->V: Strongly reduces E1A binding; when associated
FT with V-183 and A-204."
FT /evidence="ECO:0000269|PubMed:12419229"
FT MUTAGEN 183
FT /note="G->A: Reduced proteolytic processing mediated by
FT CAPN3; when associated with A-186."
FT /evidence="ECO:0000269|PubMed:23707407"
FT MUTAGEN 183
FT /note="G->V: Strongly reduces E1A binding; when associated
FT with V-181 and A-204."
FT /evidence="ECO:0000269|PubMed:12419229"
FT MUTAGEN 186
FT /note="G->A: Reduced proteolytic processing mediated by
FT CAPN3; when associated with A-183."
FT /evidence="ECO:0000269|PubMed:23707407"
FT MUTAGEN 204
FT /note="D->A: Strongly reduces E1A binding; when associated
FT with V-181 and V-183."
FT /evidence="ECO:0000269|PubMed:12419229"
FT MUTAGEN 204
FT /note="D->L: Reduced proteolytic processing mediated by
FT CAPN3."
FT /evidence="ECO:0000269|PubMed:23707407"
FT MUTAGEN 266
FT /note="R->A: Strongly reduces E1A binding; when associated
FT with A-290; A-295 and A-315."
FT /evidence="ECO:0000269|PubMed:12419229"
FT MUTAGEN 290
FT /note="D->A: Strongly reduces E1A binding; when associated
FT with A-266; A-295 and A-315."
FT /evidence="ECO:0000269|PubMed:12419229"
FT MUTAGEN 295
FT /note="E->A: Strongly reduces E1A binding; when associated
FT with A-266; A-290 and A-315."
FT /evidence="ECO:0000269|PubMed:12419229"
FT MUTAGEN 315
FT /note="H->A: Strongly reduces E1A binding; when associated
FT with A-266; A-290 and A-295."
FT /evidence="ECO:0000269|PubMed:12419229"
FT MUTAGEN 422
FT /note="S->A: Abolishes phosphorylation by HIPK2 and
FT prevents UV-induced clearance."
FT /evidence="ECO:0000269|PubMed:14567915"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:1MX3"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:1MX3"
FT HELIX 42..45
FT /evidence="ECO:0007829|PDB:1MX3"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:1MX3"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:1MX3"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:1MX3"
FT HELIX 64..69
FT /evidence="ECO:0007829|PDB:1MX3"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:1MX3"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:1MX3"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:1MX3"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:1MX3"
FT HELIX 107..112
FT /evidence="ECO:0007829|PDB:1MX3"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:1MX3"
FT TURN 121..124
FT /evidence="ECO:0007829|PDB:4U6S"
FT HELIX 125..141
FT /evidence="ECO:0007829|PDB:1MX3"
FT HELIX 143..151
FT /evidence="ECO:0007829|PDB:1MX3"
FT HELIX 159..165
FT /evidence="ECO:0007829|PDB:1MX3"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:1MX3"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:1MX3"
FT HELIX 184..194
FT /evidence="ECO:0007829|PDB:1MX3"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:1MX3"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:1MX3"
FT HELIX 211..215
FT /evidence="ECO:0007829|PDB:1MX3"
FT HELIX 223..229
FT /evidence="ECO:0007829|PDB:1MX3"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:1MX3"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:1MX3"
FT HELIX 249..252
FT /evidence="ECO:0007829|PDB:1MX3"
FT STRAND 259..263
FT /evidence="ECO:0007829|PDB:1MX3"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:4U6S"
FT HELIX 272..280
FT /evidence="ECO:0007829|PDB:1MX3"
FT STRAND 283..290
FT /evidence="ECO:0007829|PDB:1MX3"
FT STRAND 293..296
FT /evidence="ECO:0007829|PDB:1MX3"
FT TURN 303..306
FT /evidence="ECO:0007829|PDB:1MX3"
FT STRAND 308..312
FT /evidence="ECO:0007829|PDB:1MX3"
FT HELIX 321..340
FT /evidence="ECO:0007829|PDB:1MX3"
FT TURN 343..346
FT /evidence="ECO:0007829|PDB:1MX3"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:1MX3"
FT TURN 353..355
FT /evidence="ECO:0007829|PDB:7KWM"
SQ SEQUENCE 440 AA; 47535 MW; F071DD30B385603F CRC64;
MGSSHLLNKG LPLGVRPPIM NGPLHPRPLV ALLDGRDCTV EMPILKDVAT VAFCDAQSTQ
EIHEKVLNEA VGALMYHTIT LTREDLEKFK ALRIIVRIGS GFDNIDIKSA GDLGIAVCNV
PAASVEETAD STLCHILNLY RRATWLHQAL REGTRVQSVE QIREVASGAA RIRGETLGII
GLGRVGQAVA LRAKAFGFNV LFYDPYLSDG VERALGLQRV STLQDLLFHS DCVTLHCGLN
EHNHHLINDF TVKQMRQGAF LVNTARGGLV DEKALAQALK EGRIRGAALD VHESEPFSFS
QGPLKDAPNL ICTPHAAWYS EQASIEMREE AAREIRRAIT GRIPDSLKNC VNKDHLTAAT
HWASMDPAVV HPELNGAAYR YPPGVVGVAP TGIPAAVEGI VPSAMSLSHG LPPVAHPPHA
PSPGQTVKPE ADRDHASDQL
