DIM_ARATH
ID DIM_ARATH Reviewed; 561 AA.
AC Q39085; Q0WWL4; Q38808; Q8RXF4;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2001, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Delta(24)-sterol reductase;
DE EC=1.3.1.72;
DE AltName: Full=Cell elongation protein DIMINUTO;
DE AltName: Full=Cell elongation protein Dwarf1;
DE AltName: Full=Protein CABBAGE1;
DE AltName: Full=Protein ENHANCED VERY-LOW-FLUENCE RESPONSE 1;
GN Name=DIM; Synonyms=CBB1, DWF1, EVE1; OrderedLocusNames=At3g19820;
GN ORFNames=MPN9.6;
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].
RC STRAIN=cv. Columbia;
RX PubMed=7828854; DOI=10.1101/gad.9.1.97;
RA Takahashi T., Gasch A., Nishizawa N., Chua N.-H.;
RT "The DIMINUTO gene of Arabidopsis is involved in regulating cell
RT elongation.";
RL Genes Dev. 9:97-107(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Dilkes B.P., Wu Y., Schulz B., Carlson T., Anna W., Feldman F.A.;
RT "The DWF1 locus of Arabidopsis thaliana encodes a novel protein required
RT for cell elongation.";
RL Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Fujita M., Mizukado S., Seki M., Shinozaki K., Mitsuda N., Takiguchi Y.,
RA Takagi M.;
RT "ORF cloning and analysis of Arabidopsis transcription factor genes.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=9761794; DOI=10.2307/3870765;
RA Klahre U., Noguchi T., Fujioka S., Takatsuto S., Yokota T., Nomura T.,
RA Yoshida S., Chua N.H.;
RT "The Arabidopsis DIMINUTO/DWARF1 gene encodes a protein involved in steroid
RT synthesis.";
RL Plant Cell 10:1677-1690(1998).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-131; GLY-163; GLY-172;
RP GLY-220 AND GLY-282, AND DISRUPTION PHENOTYPE.
RX PubMed=10069828; DOI=10.1104/pp.119.3.897;
RA Choe S., Dilkes B.P., Gregory B.D., Ross A.S., Yuan H., Noguchi T.,
RA Fujioka S., Takatsuto S., Tanaka A., Yoshida S., Tax F.E., Feldmann K.A.;
RT "The Arabidopsis dwarf1 mutant is defective in the conversion of 24-
RT methylenecholesterol to campesterol in brassinosteroid biosynthesis.";
RL Plant Physiol. 119:897-907(1999).
RN [10]
RP FUNCTION.
RX PubMed=11788763; DOI=10.1104/pp.010668;
RA Luccioni L.G., Oliverio K.A., Yanovsky M.J., Boccalandro H.E., Casal J.J.;
RT "Brassinosteroid mutants uncover fine tuning of phytochrome signaling.";
RL Plant Physiol. 128:173-181(2002).
RN [11]
RP INTERACTION WITH CALMODULIN, AND MUTAGENESIS OF 521-LYS--ARG-523 AND
RP VAL-531.
RX PubMed=16193053; DOI=10.1038/nature03973;
RA Du L., Poovaiah B.W.;
RT "Ca2+/calmodulin is critical for brassinosteroid biosynthesis and plant
RT growth.";
RL Nature 437:741-745(2005).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: Plays a critical role in the general process of plant cell
CC elongation. Involved in the synthesis of campesterol, an early
CC precursor of brassinolide. Required for the conversion of 24-
CC methylenecholesterol to campesterol and for the conversion of
CC isofucosterol to sitosterol. Necessary for both the isomerization and
CC reduction of 24-methylenecholesterol. Regulates indirectly phytochrome-
CC mediated light responses through the modulation of brassinosteroid
CC biosynthesis. {ECO:0000269|PubMed:10069828,
CC ECO:0000269|PubMed:11788763, ECO:0000269|PubMed:9761794}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=lathosterol + NADP(+) = 5alpha-cholesta-7,24-dien-3beta-ol +
CC H(+) + NADPH; Xref=Rhea:RHEA:13685, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16290, ChEBI:CHEBI:17168, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.3.1.72;
CC Evidence={ECO:0000269|PubMed:10069828, ECO:0000269|PubMed:9761794};
CC -!- SUBUNIT: Interacts with calmodulin. {ECO:0000269|PubMed:16193053}.
CC -!- INTERACTION:
CC Q39085; Q9M391: At3g54130; NbExp=3; IntAct=EBI-16906963, EBI-25520805;
CC -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000269|PubMed:9761794};
CC Single-pass type II membrane protein {ECO:0000269|PubMed:9761794};
CC Cytoplasmic side {ECO:0000269|PubMed:9761794}.
CC -!- DISRUPTION PHENOTYPE: Dwarf and reduced fertility.
CC {ECO:0000269|PubMed:10069828}.
CC -!- SIMILARITY: Belongs to the DIMINUTO family. {ECO:0000305}.
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DR EMBL; L38520; AAA67055.1; -; mRNA.
DR EMBL; U12400; AAA20244.1; -; mRNA.
DR EMBL; AB025631; BAB01296.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76293.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76294.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76295.1; -; Genomic_DNA.
DR EMBL; AY072216; AAL60037.1; -; mRNA.
DR EMBL; AY081286; AAL91175.1; -; mRNA.
DR EMBL; AY096472; AAM20112.1; -; mRNA.
DR EMBL; BT000367; AAN15686.1; -; mRNA.
DR EMBL; AK226335; BAE98484.1; -; mRNA.
DR EMBL; AB493623; BAH30461.1; -; mRNA.
DR PIR; S71189; S71189.
DR RefSeq; NP_001319595.1; NM_001338420.1.
DR RefSeq; NP_188616.1; NM_112872.3.
DR RefSeq; NP_850616.1; NM_180285.4.
DR AlphaFoldDB; Q39085; -.
DR SMR; Q39085; -.
DR BioGRID; 6851; 20.
DR IntAct; Q39085; 10.
DR STRING; 3702.AT3G19820.2; -.
DR iPTMnet; Q39085; -.
DR SwissPalm; Q39085; -.
DR PaxDb; Q39085; -.
DR PRIDE; Q39085; -.
DR ProteomicsDB; 224483; -.
DR EnsemblPlants; AT3G19820.1; AT3G19820.1; AT3G19820.
DR EnsemblPlants; AT3G19820.2; AT3G19820.2; AT3G19820.
DR EnsemblPlants; AT3G19820.3; AT3G19820.3; AT3G19820.
DR GeneID; 821519; -.
DR Gramene; AT3G19820.1; AT3G19820.1; AT3G19820.
DR Gramene; AT3G19820.2; AT3G19820.2; AT3G19820.
DR Gramene; AT3G19820.3; AT3G19820.3; AT3G19820.
DR KEGG; ath:AT3G19820; -.
DR Araport; AT3G19820; -.
DR TAIR; locus:2092276; AT3G19820.
DR eggNOG; KOG1262; Eukaryota.
DR HOGENOM; CLU_025883_4_0_1; -.
DR InParanoid; Q39085; -.
DR OMA; YIPSRHY; -.
DR OrthoDB; 733611at2759; -.
DR PhylomeDB; Q39085; -.
DR BioCyc; ARA:AT3G19820-MON; -.
DR BioCyc; MetaCyc:AT3G19820-MON; -.
DR BRENDA; 1.3.1.72; 399.
DR PRO; PR:Q39085; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q39085; baseline and differential.
DR Genevisible; Q39085; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IDA:TAIR.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0005516; F:calmodulin binding; IDA:TAIR.
DR GO; GO:0050614; F:delta24-sterol reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR GO; GO:0016132; P:brassinosteroid biosynthetic process; IDA:TAIR.
DR GO; GO:0009808; P:lignin metabolic process; IMP:TAIR.
DR GO; GO:0009834; P:plant-type secondary cell wall biogenesis; IMP:TAIR.
DR GO; GO:0008202; P:steroid metabolic process; IBA:GO_Central.
DR GO; GO:0009826; P:unidimensional cell growth; IMP:TAIR.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR040165; Diminuto-like.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR PANTHER; PTHR10801; PTHR10801; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 1: Evidence at protein level;
KW Calmodulin-binding; Endoplasmic reticulum; Membrane; Microsome; NADP;
KW Oxidoreductase; Phosphoprotein; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..561
FT /note="Delta(24)-sterol reductase"
FT /id="PRO_0000219495"
FT TOPO_DOM 1..25
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 26..46
FT /note="Helical; Signal-anchor"
FT /evidence="ECO:0000255"
FT TOPO_DOM 47..561
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 49..232
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT REGION 518..539
FT /note="Interaction with calmodulin"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MUTAGEN 131
FT /note="E->K: In dwf1-9; dwarf phenotype."
FT /evidence="ECO:0000269|PubMed:10069828"
FT MUTAGEN 163
FT /note="G->V: In dwf1-3; dwarf phenotype."
FT /evidence="ECO:0000269|PubMed:10069828"
FT MUTAGEN 172
FT /note="G->E: In dwf1-10; dwarf phenotype."
FT /evidence="ECO:0000269|PubMed:10069828"
FT MUTAGEN 220
FT /note="G->R: In dwf1-11; dwarf phenotype."
FT /evidence="ECO:0000269|PubMed:10069828"
FT MUTAGEN 282
FT /note="G->R: In dwf1-7; dwarf phenotype."
FT /evidence="ECO:0000269|PubMed:10069828"
FT MUTAGEN 521..523
FT /note="KYR->DGD: Loss of calmodulin binding and loss of
FT function."
FT /evidence="ECO:0000269|PubMed:16193053"
FT MUTAGEN 531
FT /note="V->D: Decreased calmodulin binding and partial loss
FT of function."
FT /evidence="ECO:0000269|PubMed:16193053"
FT CONFLICT 399
FT /note="L -> P (in Ref. 5; AAL91175/AAN15686)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="E -> G (in Ref. 1; AAA67055)"
FT /evidence="ECO:0000305"
FT CONFLICT 476
FT /note="S -> L (in Ref. 1; AAA67055)"
FT /evidence="ECO:0000305"
FT CONFLICT 506
FT /note="F -> L (in Ref. 1; AAA67055)"
FT /evidence="ECO:0000305"
FT CONFLICT 527
FT /note="T -> K (in Ref. 5; AAL91175/AAN15686)"
FT /evidence="ECO:0000305"
FT CONFLICT 556..558
FT /note="AYA -> PYP (in Ref. 1; AAA67055)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 561 AA; 65394 MW; CD25EF655AD44200 CRC64;
MSDLQTPLVR PKRKKTWVDY FVKFRWIIVI FIVLPFSATF YFLIYLGDMW SESKSFEKRQ
KEHDENVKKV IKRLKGRDAS KDGLVCTARK PWIAVGMRNV DYKRARHFEV DLGEFRNILE
INKEKMTARV EPLVNMGQIS RATVPMNLSL AVVAELDDLT VGGLINGYGI EGSSHIYGLF
ADTVEAYEIV LAGGELVRAT RDNEYSDLYY AIPWSQGTLG LLVAAEIRLI KVKEYMRLTY
IPVKGDLQAL AQGYIDSFAP KDGDKSKIPD FVEGMVYNPT EGVMMVGTYA SKEEAKKKGN
KINNVGWWFK PWFYQHAQTA LKKGQFVEYI PTREYYHRHT RCLYWEGKLI LPFGDQFWFR
YLLGWLMPPK VSLLKATQGE AIRNYYHDMH VIQDMLVPLY KVGDALEWVH REMEVYPIWL
CPHKLFKQPI KGQIYPEPGF EYENRQGDTE DAQMYTDVGV YYAPGCVLRG EEFDGSEAVR
RMEKWLIENH GFQPQYAVSE LDEKSFWRMF NGELYEECRK KYRAIGTFMS VYYKSKKGRK
TEKEVREAEQ AHLETAYAEA D
