BEN1_ARATH
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 03-AUG-2022, entry version 132.
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.AT2G45400.1; -.
DR PaxDb; O22133; -.
DR PRIDE; O22133; -.
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; locus:2050882; AT2G45400.
DR eggNOG; KOG1502; Eukaryota.
DR HOGENOM; CLU_007383_9_0_1; -.
DR InParanoid; O22133; -.
DR OrthoDB; 992332at2759; -.
DR PhylomeDB; O22133; -.
DR BioCyc; ARA:AT2G45400-MON; -.
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: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: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; 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
