ID BEN1_ARATH Reviewed; 364 AA. AC O22133; DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 29-MAY-2024, entry version 139. DE RecName: Full=Protein BRI1-5 ENHANCED 1 {ECO:0000303|PubMed:17521414}; DE EC=1.1.1.- {ECO:0000305|PubMed:17521414}; GN Name=BEN1 {ECO:0000303|PubMed:17521414}; GN OrderedLocusNames=At2g45400 {ECO:0000312|EMBL:AEC10546.1}; GN ORFNames=F4L23.9 {ECO:0000312|EMBL:AAB82624.1}; 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 {ECO:0000312|Proteomes:UP000006548}; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=10617197; DOI=10.1038/45471; RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.; RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."; RL Nature 402:761-768(1999). RN [2] 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 [3] RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, RP DEVELOPMENTAL STAGE, MISCELLANEOUS, AND INDUCTION BY DARKNESS. RC STRAIN=cv. Columbia, and cv. Wassilewskija-2; RX PubMed=17521414; DOI=10.1111/j.1365-313x.2007.03129.x; RA Yuan T., Fujioka S., Takatsuto S., Matsumoto S., Gou X., He K., RA Russell S.D., Li J.; RT "BEN1, a gene encoding a dihydroflavonol 4-reductase (DFR)-like protein, RT regulates the levels of brassinosteroids in Arabidopsis thaliana."; RL Plant J. 51:220-233(2007). RN [4] RP FUNCTION, AND DISRUPTION PHENOTYPE. RC STRAIN=cv. Columbia; RX PubMed=23893742; DOI=10.1534/g3.113.006353; RA Sandhu K.S., Koirala P.S., Neff M.M.; RT "The ben1-1 brassinosteroid-catabolism mutation is unstable due to RT epigenetic modifications of the intronic T-DNA insertion."; RL G3 (Bethesda) 3:1587-1595(2013). CC -!- FUNCTION: Element of the brassinosteroid metabolic pathway that CC regulates typhasterol (TY), castasterone (CS) and brassinolide (BL) CC levels (PubMed:17521414). Involved in the control of organ elongation CC (PubMed:17521414, PubMed:23893742). {ECO:0000269|PubMed:17521414, CC ECO:0000269|PubMed:23893742}. CC -!- PATHWAY: Plant hormone biosynthesis; brassinosteroid biosynthesis. CC {ECO:0000269|PubMed:17521414}. CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q40316}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17521414}. CC -!- TISSUE SPECIFICITY: Mainly present in cell elongating-containing CC tissues. Strongly expressed in roots and flowers, also observed in CC petioles, stems, leaves and siliques. {ECO:0000269|PubMed:17521414}. CC -!- DEVELOPMENTAL STAGE: First observed after seed germination, mainly in CC the root cap, and in elongation and maturation zones, and, to a lower CC extent, in the apical meristem zone. Later present in roots, with CC higher levels in light conditions than in darkness. Weak levels in CC young flowers. Progressive accumulation in developing siliques, at both CC ends. In rosette leaves, mainly localized in vascular tissues and CC hydathodes. {ECO:0000269|PubMed:17521414}. CC -!- INDUCTION: Down-regulated in the dark. {ECO:0000269|PubMed:17521414}. CC -!- DISRUPTION PHENOTYPE: Abnormal organs elongation leading to long CC inflorescences, leaves and petioles, especially in the light. CC {ECO:0000269|PubMed:17521414, ECO:0000269|PubMed:23893742}. CC -!- MISCELLANEOUS: The ben1-1D (bri1-5 enhanced 1-1dominant) activation- CC tagging mutant suppresses the bri1-5 weak mutant allele of the CC brassinosteroid receptor gene BRI1. {ECO:0000269|PubMed:17521414}. CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase CC 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; AC002387; AAB82624.1; -; Genomic_DNA. DR EMBL; CP002685; AEC10546.1; -; Genomic_DNA. DR PIR; A84890; A84890. DR RefSeq; NP_182064.1; NM_130102.5. DR AlphaFoldDB; O22133; -. DR SMR; O22133; -. DR IntAct; O22133; 1. DR STRING; 3702.O22133; -. DR PaxDb; 3702-AT2G45400-1; -. DR ProteomicsDB; 240778; -. DR EnsemblPlants; AT2G45400.1; AT2G45400.1; AT2G45400. DR GeneID; 819146; -. DR Gramene; AT2G45400.1; AT2G45400.1; AT2G45400. DR KEGG; ath:AT2G45400; -. DR Araport; AT2G45400; -. DR TAIR; AT2G45400; BEN1. DR eggNOG; KOG1502; Eukaryota. DR HOGENOM; CLU_007383_9_0_1; -. DR InParanoid; O22133; -. DR OrthoDB; 1694166at2759; -. DR PhylomeDB; O22133; -. DR BioCyc; ARA:AT2G45400-MONOMER; -. DR UniPathway; UPA00381; -. DR PRO; PR:O22133; -. DR Proteomes; UP000006548; Chromosome 2. DR ExpressionAtlas; O22133; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:TAIR. DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:TreeGrafter. DR GO; GO:0016132; P:brassinosteroid biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0016131; P:brassinosteroid metabolic process; IMP:TAIR. DR GO; GO:0010422; P:regulation of brassinosteroid biosynthetic process; IMP:TAIR. DR GO; GO:0009646; P:response to absence of light; IEP:UniProtKB. DR CDD; cd08958; FR_SDR_e; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR001509; Epimerase_deHydtase. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR PANTHER; PTHR10366; NAD DEPENDENT EPIMERASE/DEHYDRATASE; 1. DR PANTHER; PTHR10366:SF689; PROTEIN BRI1-5 ENHANCED 1; 1. DR Pfam; PF01370; Epimerase; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. PE 2: Evidence at transcript level; KW Brassinosteroid biosynthesis; Cytoplasm; Developmental protein; KW Lipid biosynthesis; Lipid metabolism; NADP; Oxidoreductase; KW Reference proteome; Steroid biosynthesis. FT CHAIN 1..364 FT /note="Protein BRI1-5 ENHANCED 1" FT /id="PRO_0000434413" FT REGION 1..22 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 206 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:Q12068" FT BINDING 44..49 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:Q12068" FT BINDING 69 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:Q12068" FT BINDING 98..99 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:Q12068" FT BINDING 202 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:Q12068" FT BINDING 206 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:Q12068" FT BINDING 232 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:Q12068" FT BINDING 244 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:Q12068" SQ SEQUENCE 364 AA; 40261 MW; 03B2AD3D437A1037 CRC64; MVREEQEEDD NNNNNNGGGE RKLLVADETV PSLLDETGLV CVTGGSGFVA SWLIMRLLQR GYSVRATVRT NSEGNKKDIS YLTELPFASE RLQIFTADLN EPESFKPAIE GCKAVFHVAH PMDPNSNETE ETVTKRTVQG LMGILKSCLD AKTVKRFFYT SSAVTVFYSG GNGGGGGEVD ESVWSDVEVF RNQKEKRVSS SYVVSKMAAE TAALEFGGKN GLEVVTLVIP LVVGPFISSS LPSSVFISLA MLFGNYKEKY LFDTYNMVHI DDVARAMIFL LEKPVAKGRY ICSSVEMKID EVFEFLSTKF PQFQLPSIDL NKYKVEKRMG LSSKKLKSAG FEFKYGAEEI FSGAIRSCQA RGFL //