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 08-MAY-2019, entry version 117. 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; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC 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., RA Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., RA Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., RA Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., RA Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., RA Venter J.C.; RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis RT 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 RT reference genome."; RL Plant J. 89:789-804(2017). RN [3] RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, DEVELOPMENTAL STAGE, MISCELLANEOUS, AND INDUCTION BY RP 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 RT protein, regulates the levels of brassinosteroids in Arabidopsis RT 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, castasterone and brassinolide levels CC (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. CC {ECO:0000269|PubMed:17521414}. CC -!- DEVELOPMENTAL STAGE: First observed after seed germination, mainly CC in the root cap, and in elongation and maturation zones, and, to a CC lower extent, in the apical meristem zone. Later present in roots, CC with higher levels in light conditions than in darkness. Weak CC levels in young flowers. Progressive accumulation in developing CC siliques, at both ends. In rosette leaves, mainly localized in CC vascular tissues and hydathodes. {ECO:0000269|PubMed:17521414}. CC -!- INDUCTION: Down-regulated in the dark. CC {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) CC activation-tagging mutant suppresses the bri1-5 weak mutant allele CC of the brassinosteroid receptor gene BRI1. CC {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 SMR; O22133; -. DR STRING; 3702.AT2G45400.1; -. DR PaxDb; O22133; -. 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; locus:2050882; AT2G45400. DR eggNOG; KOG1502; Eukaryota. DR eggNOG; COG0451; LUCA. DR HOGENOM; HOG000167998; -. DR InParanoid; O22133; -. DR OrthoDB; 992332at2759; -. 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 Genevisible; O22133; AT. DR GO; GO:0005737; C:cytoplasm; IDA:TAIR. DR GO; GO:0050662; F:coenzyme binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central. DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central. DR GO; GO:0016132; P:brassinosteroid biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0016131; P:brassinosteroid metabolic process; IMP:TAIR. DR GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW. 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 InterPro; IPR001509; Epimerase_deHydtase. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR Pfam; PF01370; Epimerase; 1. DR SUPFAM; SSF51735; SSF51735; 1. PE 2: Evidence at transcript level; KW Brassinosteroid biosynthesis; Complete proteome; Cytoplasm; KW Developmental protein; Lipid biosynthesis; Lipid metabolism; NADP; KW Oxidoreductase; Reference proteome; Steroid biosynthesis. FT CHAIN 1 364 Protein BRI1-5 ENHANCED 1. FT /FTId=PRO_0000434413. FT NP_BIND 44 49 NADP. {ECO:0000250|UniProtKB:Q12068}. FT NP_BIND 98 99 NADP. {ECO:0000250|UniProtKB:Q12068}. FT ACT_SITE 206 206 Proton donor. FT {ECO:0000250|UniProtKB:Q12068}. FT BINDING 69 69 NADP. {ECO:0000250|UniProtKB:Q12068}. FT BINDING 202 202 NADP. {ECO:0000250|UniProtKB:Q12068}. FT BINDING 206 206 NADP. {ECO:0000250|UniProtKB:Q12068}. FT BINDING 232 232 NADP; via amide nitrogen. FT {ECO:0000250|UniProtKB:Q12068}. FT BINDING 244 244 NADP. {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 //