CTBP_ARATH
ID CTBP_ARATH Reviewed; 636 AA.
AC O23702; O03984; Q7DLS3; Q93YQ6; Q948X7; Q9LMM9;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=C-terminal binding protein AN {ECO:0000303|PubMed:11889033};
DE Short=CtBP {ECO:0000303|PubMed:11889033};
DE AltName: Full=Protein ANGUSTIFOLIA {ECO:0000303|PubMed:11889033};
DE AltName: Full=Protein DETORQUEO {ECO:0000303|PubMed:23368817};
GN Name=AN {ECO:0000303|PubMed:11889033};
GN Synonyms=DOQ {ECO:0000303|PubMed:23368817};
GN OrderedLocusNames=At1g01510 {ECO:0000312|Araport:AT1G01510};
GN ORFNames=F22L4.6 {ECO:0000312|EMBL:AAF81310.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE,
RP HOMODIMERIZATION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=11889033; DOI=10.1093/emboj/21.6.1267;
RA Kim G.-T., Shoda K., Tsuge T., Cho K.-H., Uchimiya H., Yokoyama R.,
RA Nishitani K., Tsukaya H.;
RT "The ANGUSTIFOLIA gene of Arabidopsis, a plant CtBP gene, regulates leaf-
RT cell expansion, the arrangement of cortical microtubules in leaf cells and
RT expression of a gene involved in cell-wall formation.";
RL EMBO J. 21:1267-1279(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9666060; DOI=10.1016/s0378-1119(98)00286-8;
RA Terryn N., Gielen J., De Keyser A., Van Den Daele H., Ardiles W., Neyt P.,
RA De Clercq R., Coppieters J., Dehais P., Villarroel R., Rouze P.,
RA van Montagu M.;
RT "Sequence analysis of a 40-kb Arabidopsis thaliana genomic region located
RT at the top of chromosome 1.";
RL Gene 215:11-17(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=8625845; DOI=10.1242/dev.122.5.1589;
RA Tsuge T., Tsukaya H., Uchimiya H.;
RT "Two independent and polarized processes of cell elongation regulate leaf
RT blade expansion in Arabidopsis thaliana (L.) Heynh.";
RL Development 122:1589-1600(1996).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9736998; DOI=10.1007/s004250050389;
RA Kim G.-T., Tsukaya H., Uchimiya H.;
RT "The CURLY LEAF gene controls both division and elongation of cells during
RT the expansion of the leaf blade in Arabidopsis thaliana.";
RL Planta 206:175-183(1998).
RN [8]
RP FUNCTION IN TRICHOME BRANCHING, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. RLD;
RX PubMed=10572032; DOI=10.1242/dev.126.24.5547;
RA Luo D., Oppenheimer D.G.;
RT "Genetic control of trichome branch number in Arabidopsis: the roles of the
RT FURCA loci.";
RL Development 126:5547-5557(1999).
RN [9]
RP FUNCTION IN TRICHOME BRANCHING, AND DISRUPTION PHENOTYPE.
RX PubMed=12079678; DOI=10.1098/rstb.2002.1087;
RA Schnittger A., Huelskamp M.;
RT "Trichome morphogenesis: a cell-cycle perspective.";
RL Philos. Trans. R. Soc. Lond., B, Biol. Sci. 357:823-826(2002).
RN [10]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, MUTAGENESIS OF GLU-118, AND
RP INTERACTION WITH KCBP.
RX PubMed=11889034; DOI=10.1093/emboj/21.6.1280;
RA Folkers U., Kirik V., Schoebinger U., Falk S., Krishnakumar S.,
RA Pollock M.A., Oppenheimer D.G., Day I., Reddy A.S., Juergens G.,
RA Huelskamp M., Reddy A.R.;
RT "The cell morphogenesis gene ANGUSTIFOLIA encodes a CtBP/BARS-like protein
RT and is involved in the control of the microtubule cytoskeleton.";
RL EMBO J. 21:1280-1288(2002).
RN [11]
RP REVIEW.
RX PubMed=11978864; DOI=10.1093/pcp/pcf051;
RA Tsukaya H.;
RT "The leaf index: heteroblasty, natural variation, and the genetic control
RT of polar processes of leaf expansion.";
RL Plant Cell Physiol. 43:372-378(2002).
RN [12]
RP FUNCTION.
RX PubMed=17972097; DOI=10.1007/s00427-007-0186-8;
RA Stern M.D., Aihara H., Cho K.-H., Kim G.-T., Horiguchi G., Roccaro G.A.,
RA Guevara E., Sun H.H., Negeri D., Tsukaya H., Nibu Y.;
RT "Structurally related Arabidopsis ANGUSTIFOLIA is functionally distinct
RT from the transcriptional corepressor CtBP.";
RL Dev. Genes Evol. 217:759-769(2007).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19843316; DOI=10.1111/j.1365-313x.2009.04050.x;
RA Bai Y., Falk S., Schnittger A., Jakoby M.J., Huelskamp M.;
RT "Tissue layer specific regulation of leaf length and width in Arabidopsis
RT as revealed by the cell autonomous action of ANGUSTIFOLIA.";
RL Plant J. 61:191-199(2010).
RN [14]
RP SUBCELLULAR LOCATION, SUBUNIT, DOMAIN, MUTAGENESIS OF 26-LEU--GLU-30;
RP 424-LYS--HIS-427 AND SER-456, AND TISSUE SPECIFICITY.
RX PubMed=21801251; DOI=10.1111/j.1365-313x.2011.04731.x;
RA Minamisawa N., Sato M., Cho K.H., Ueno H., Takechi K., Kajikawa M.,
RA Yamato K.T., Ohyama K., Toyooka K., Kim G.T., Horiguchi G., Takano H.,
RA Ueda T., Tsukaya H.;
RT "ANGUSTIFOLIA, a plant homolog of CtBP/BARS, functions outside the
RT nucleus.";
RL Plant J. 68:788-799(2011).
RN [15]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLY-170, AND INTERACTION
RP WITH SUB.
RX PubMed=23368817; DOI=10.1186/1471-2229-13-16;
RA Bai Y., Vaddepalli P., Fulton L., Bhasin H., Hulskamp M., Schneitz K.;
RT "ANGUSTIFOLIA is a central component of tissue morphogenesis mediated by
RT the atypical receptor-like kinase STRUBBELIG.";
RL BMC Plant Biol. 13:16-16(2013).
RN [16]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23672620; DOI=10.1186/1471-2229-13-79;
RA Gachomo E.W., Jimenez-Lopez J.C., Smith S.R., Cooksey A.B.,
RA Oghoghomeh O.M., Johnson N., Baba-Moussa L., Kotchoni S.O.;
RT "The cell morphogenesis ANGUSTIFOLIA (AN) gene, a plant homolog of
RT CtBP/BARS, is involved in abiotic and biotic stress response in higher
RT plants.";
RL BMC Plant Biol. 13:79-79(2013).
RN [17]
RP DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INTERACTION WITH SOK1;
RP SOK2; SOK3 AND SOK4.
RX PubMed=32004461; DOI=10.1016/j.cell.2020.01.011;
RA van Dop M., Fiedler M., Mutte S., de Keijzer J., Olijslager L.,
RA Albrecht C., Liao C.Y., Janson M.E., Bienz M., Weijers D.;
RT "DIX domain polymerization drives assembly of plant cell polarity
RT complexes.";
RL Cell 180:427.e12-439.e12(2020).
CC -!- FUNCTION: Involved in controlling the equilibrium between tubular and
CC stacked structures in the Golgi complex (By similarity). Required for
CC cortical microtubules (MTs) arrangement that confers cell shape.
CC Regulates the width of leaves by controlling the polar elongation of
CC leaf cells. Involved in the regulation of trichome branching. Seems to
CC not be able to regulate gene transcription. Regulates epidermal cell
CC divisions and elongation in a non-cell-autonomous manner (regulated by
CC subepidermal cells), but regulates epidermal cell polarity, shape,
CC trichome branching and elongation in a cell-autonomous manner.
CC Negatively regulates growth in the petiole elongation. Prevents lipid
CC peroxidation as a result of abiotic stress response. Is involved in the
CC SUB-dependent signaling mechanism and may act in a membrane trafficking
CC event around the trans-Golgi network. {ECO:0000250,
CC ECO:0000269|PubMed:10572032, ECO:0000269|PubMed:11889033,
CC ECO:0000269|PubMed:12079678, ECO:0000269|PubMed:17972097,
CC ECO:0000269|PubMed:19843316, ECO:0000269|PubMed:23368817,
CC ECO:0000269|PubMed:23672620, ECO:0000269|PubMed:8625845,
CC ECO:0000269|PubMed:9736998}.
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC Note=Cofactor binding induces a conformational change. {ECO:0000250};
CC -!- SUBUNIT: Homodimer (PubMed:21801251). Interacts with KCBP and SUB (via
CC intra-cellular domain); AN is not required for the correct subcellular
CC localization and recycling of SUB (PubMed:23368817, PubMed:11889034).
CC Binds to SOKs proteins polymers (e.g. SOK1, SOK2, SOK3 and SOK4)
CC (PubMed:32004461). {ECO:0000269|PubMed:11889034,
CC ECO:0000269|PubMed:21801251, ECO:0000269|PubMed:23368817,
CC ECO:0000269|PubMed:32004461}.
CC -!- INTERACTION:
CC O23702; O23702: AN; NbExp=3; IntAct=EBI-1578856, EBI-1578856;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11889033,
CC ECO:0000269|PubMed:11889034, ECO:0000269|PubMed:32004461}. Golgi
CC apparatus, trans-Golgi network {ECO:0000269|PubMed:21801251}. Note=Was
CC thought initially to be located in nucleus (PubMed:11889033 and
CC PubMed:11889034) but the large dot-like structures are now believed to
CC represent non-physiological aggregates (PubMed:11889033,
CC PubMed:11889034). In root cells, cytoplasmic polarized localization
CC near cell edges, at the vicinity of SOKs proteins (PubMed:32004461).
CC Associates with membranes in puncta in embryos (PubMed:32004461).
CC {ECO:0000269|PubMed:11889033, ECO:0000269|PubMed:11889034,
CC ECO:0000269|PubMed:32004461}.
CC -!- TISSUE SPECIFICITY: Expressed in cotyledons, leaves, roots, stems and
CC floral buds. {ECO:0000269|PubMed:11889033, ECO:0000269|PubMed:11889034,
CC ECO:0000269|PubMed:21801251}.
CC -!- DOMAIN: The C-terminal region (631-636) is indispenasble for
CC homodimerization. {ECO:0000269|PubMed:21801251}.
CC -!- DISRUPTION PHENOTYPE: Dwarfism. Impaired cortical microtubules (MTs)
CC arrangement leading to abnormal cell shapes (reduced complexity), and
CC narrow but thick leaves, characterized by cells small in the leaf-width
CC direction and large in the leaf-thickness direction; this phenotype is
CC also slightly observed in floral organs. Reduced trichome branching.
CC Twisted siliques and reduced seed productivity. Delayed flowering and
CC senescence, but increased tolerance to drought and pathogen attack. No
CC impact on polarized localization of SOKs proteins in root cells
CC (PubMed:32004461). {ECO:0000269|PubMed:10572032,
CC ECO:0000269|PubMed:11889033, ECO:0000269|PubMed:12079678,
CC ECO:0000269|PubMed:19843316, ECO:0000269|PubMed:23368817,
CC ECO:0000269|PubMed:23672620, ECO:0000269|PubMed:32004461,
CC ECO:0000269|PubMed:8625845, ECO:0000269|PubMed:9736998}.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. Plant AN subfamily. {ECO:0000305}.
CC -!- CAUTION: Was initially thought to function as a transcriptional
CC corepressor. {ECO:0000305|PubMed:11889033}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF81310.1; Type=Erroneous gene model prediction; Note=The predicted gene At1g01510 has been split into 3 genes: At1g01500, At1g01510 and At1g01520.; Evidence={ECO:0000305};
CC Sequence=CAA71175.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA73307.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB032060; BAB64262.1; -; mRNA.
DR EMBL; Y10086; CAA71175.1; ALT_INIT; Genomic_DNA.
DR EMBL; Y12776; CAA73306.1; -; Genomic_DNA.
DR EMBL; Y12776; CAA73307.1; ALT_INIT; Genomic_DNA.
DR EMBL; AC061957; AAF81310.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27298.1; -; Genomic_DNA.
DR EMBL; AY059829; AAL24311.1; -; mRNA.
DR EMBL; BT000155; AAN15474.1; -; mRNA.
DR PIR; G86145; G86145.
DR RefSeq; NP_563629.1; NM_100033.3.
DR AlphaFoldDB; O23702; -.
DR SMR; O23702; -.
DR BioGRID; 24636; 7.
DR IntAct; O23702; 4.
DR STRING; 3702.AT1G01510.1; -.
DR iPTMnet; O23702; -.
DR PaxDb; O23702; -.
DR PRIDE; O23702; -.
DR ProteomicsDB; 222722; -.
DR EnsemblPlants; AT1G01510.1; AT1G01510.1; AT1G01510.
DR GeneID; 839401; -.
DR Gramene; AT1G01510.1; AT1G01510.1; AT1G01510.
DR KEGG; ath:AT1G01510; -.
DR Araport; AT1G01510; -.
DR TAIR; locus:2025376; AT1G01510.
DR eggNOG; KOG0067; Eukaryota.
DR HOGENOM; CLU_013739_0_0_1; -.
DR InParanoid; O23702; -.
DR OMA; NCIEDCS; -.
DR OrthoDB; 579499at2759; -.
DR PhylomeDB; O23702; -.
DR PRO; PR:O23702; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O23702; baseline and differential.
DR Genevisible; O23702; AT.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005802; C:trans-Golgi network; IDA:TAIR.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0019900; F:kinase binding; IPI:TAIR.
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:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0043621; F:protein self-association; IPI:TAIR.
DR GO; GO:0003714; F:transcription corepressor activity; IEA:InterPro.
DR GO; GO:0048444; P:floral organ morphogenesis; IMP:UniProtKB.
DR GO; GO:0048530; P:fruit morphogenesis; IMP:UniProtKB.
DR GO; GO:0031129; P:inductive cell-cell signaling; IMP:UniProtKB.
DR GO; GO:0009965; P:leaf morphogenesis; IMP:TAIR.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:TAIR.
DR GO; GO:0042814; P:monopolar cell growth; IMP:TAIR.
DR GO; GO:0007097; P:nuclear migration; IMP:TAIR.
DR GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
DR GO; GO:0045604; P:regulation of epidermal cell differentiation; IMP:UniProtKB.
DR GO; GO:0010482; P:regulation of epidermal cell division; IMP:UniProtKB.
DR GO; GO:2000039; P:regulation of trichome morphogenesis; IMP:UniProtKB.
DR GO; GO:0006970; P:response to osmotic stress; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR GO; GO:0034063; P:stress granule assembly; IMP:TAIR.
DR GO; GO:0010091; P:trichome branching; IMP:UniProtKB.
DR CDD; cd05299; CtBP_dh; 1.
DR InterPro; IPR045015; AN-like.
DR InterPro; IPR043322; CtBP.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43254; PTHR43254; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Cell shape; Cytoplasm; Developmental protein; Golgi apparatus; Microtubule;
KW NAD; Reference proteome.
FT CHAIN 1..636
FT /note="C-terminal binding protein AN"
FT /id="PRO_0000408478"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 91
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 147..148
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9I3W9"
FT BINDING 169..174
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P26297"
FT BINDING 193
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P26297"
FT BINDING 231..237
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P26297"
FT BINDING 258..260
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P26297"
FT BINDING 284
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P26297"
FT BINDING 307..311
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9I3W9"
FT MUTAGEN 26..30
FT /note="LNCIE->RNRIG: No effect on activity."
FT /evidence="ECO:0000269|PubMed:21801251"
FT MUTAGEN 118
FT /note="E->K: In am-EM2; decreased trichome branching and
FT modified microtubule density along the basal-apical axis of
FT the trichome."
FT /evidence="ECO:0000269|PubMed:11889034"
FT MUTAGEN 170
FT /note="G->D: In doq-1; premature opening of flowers and
FT twisted petals."
FT /evidence="ECO:0000269|PubMed:23368817"
FT MUTAGEN 424..427
FT /note="KKRH->AAAA: No effect on activity."
FT /evidence="ECO:0000269|PubMed:21801251"
FT MUTAGEN 456
FT /note="S->A: No effect on activity."
FT /evidence="ECO:0000269|PubMed:21801251"
FT CONFLICT 299
FT /note="M -> I (in Ref. 1; BAB64262 and 2; CAA71175)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="S -> L (in Ref. 5; AAL24311/AAN15474)"
FT /evidence="ECO:0000305"
FT CONFLICT 543
FT /note="V -> L (in Ref. 5; AAL24311/AAN15474)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 636 AA; 70150 MW; 7D46FE0E55D05F91 CRC64;
MSKIRSSATM PHRDQPSPAS PHVVTLNCIE DCALEQDSLA GVAGVEYVPL SRIADGKIES
ATAVLLHSLA YLPRAAQRRL RPHQLILCLG SADRAVDSTL AADLGLRLVH VDTSRAEEIA
DTVMALILGL LRRTHLLSRH ALSASGWLGS LQPLCRGMRR CRGMVLGIVG RSVSARYLAS
RSLAFKMSVL YFDVPEGDEE RIRPSRFPRA ARRMDTLNDL LAASDVISLH CALTNDTVQI
LNAECLQHIK PGAFLVNTGS CQLLDDCAVK QLLIDGTIAG CALDGAEGPQ WMEAWVKEMP
NVLILPRSAD YSEEVWMEIR EKAISILHSF FLDGVIPSNT VSDEEVEESE ASEEEEQSPS
KHEKLAIVES TSRQQGESTL TSTEIVRREA SELKESLSPG QQHVSQNTAV KPEGRRSRSG
KKAKKRHSQQ KYMQKTDGSS GLNEESTSRR DDIAMSDTEE VLSSSSRCAS PEDSRSRKTP
LEVMQESSPN QLVMSSKKFI GKSSELLKDG YVVALYAKDL SGLHVSRQRT KNGGWFLDTL
SNVSKRDPAA QFIIAYRNKD TVGLRSFAAG GKLLQINRRM EFVFASHSFD VWESWSLEGS
LDECRLVNCR NSSAVLDVRV EILAMVGDDG ITRWID
