DET2_ARATH
ID DET2_ARATH Reviewed; 262 AA.
AC Q38944; Q9SH83;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2002, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Steroid 5-alpha-reductase DET2 {ECO:0000303|PubMed:8602526};
DE EC=1.3.1.22 {ECO:0000269|PubMed:10398719, ECO:0000269|PubMed:15993049, ECO:0000269|PubMed:9108014};
DE AltName: Full=(22R,23R)-22,23-dihydroxycampest-4-en-3-one synthase {ECO:0000303|PubMed:22822057};
DE EC=1.3.1.- {ECO:0000269|PubMed:22822057};
DE AltName: Full=(22S,24R)-22-hydroxy-5alpha-ergostan-3-one synthase {ECO:0000303|PubMed:22822057};
DE EC=1.3.1.22 {ECO:0000269|PubMed:22822057};
DE AltName: Full=Campest-3-one synthase {ECO:0000303|PubMed:22822057};
DE EC=1.3.1.22 {ECO:0000269|PubMed:22822057};
DE AltName: Full=Protein COMPACT ROSETTE 1 {ECO:0000303|PubMed:10394910};
DE AltName: Full=Protein DEETIOLATED 2 {ECO:0000303|PubMed:8602526, ECO:0000303|PubMed:9108014, ECO:0000303|PubMed:9401120};
DE Short=AtDET2 {ECO:0000303|PubMed:8602526, ECO:0000303|PubMed:9108014, ECO:0000303|PubMed:9401120};
GN Name=DET2 {ECO:0000303|PubMed:8602526, ECO:0000303|PubMed:9108014,
GN ECO:0000303|PubMed:9401120}; Synonyms=CRO1 {ECO:0000303|PubMed:10394910};
GN OrderedLocusNames=At2g38050 {ECO:0000312|Araport:AT2G38050};
GN ORFNames=T8P21.4 {ECO:0000305};
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, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=8602526; DOI=10.1126/science.272.5260.398;
RA Li J., Nagpal P., Vitart V., McMorris T.C., Chory J.;
RT "A role for brassinosteroids in light-dependent development of
RT Arabidopsis.";
RL Science 272:398-401(1996).
RN [2]
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 [3]
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 [4]
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 [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLU-204.
RC STRAIN=cv. Columbia;
RX PubMed=9401120; DOI=10.2307/3870556;
RA Fujioka S., Li J., Choi Y.-H., Seto H., Takatsuto S., Noguchi T.,
RA Watanabe T., Kuriyama H., Yokota T., Chory J., Sakurai A.;
RT "The Arabidopsis deetiolated2 mutant is blocked early in brassinosteroid
RT biosynthesis.";
RL Plant Cell 9:1951-1962(1997).
RN [6]
RP FUNCTION, MUTAGENESIS OF GLU-204, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND ACTIVITY REGULATION.
RC STRAIN=cv. Columbia;
RX PubMed=9108014; DOI=10.1073/pnas.94.8.3554;
RA Li J., Biswas M.G., Chao A., Russell D.W., Chory J.;
RT "Conservation of function between mammalian and plant steroid 5alpha-
RT reductases.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:3554-3559(1997).
RN [7]
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLU-204.
RX PubMed=10394910; DOI=10.1007/s004380050016;
RA Serrano-Cartagena J., Robles P., Ponce M.R., Micol J.L.;
RT "Genetic analysis of leaf form mutants from the Arabidopsis information
RT service collection.";
RL Mol. Gen. Genet. 261:725-739(1999).
RN [8]
RP FUNCTION, MUTAGENESIS OF GLU-204, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Columbia;
RX PubMed=10398719; DOI=10.1104/pp.120.3.833;
RA Noguchi T., Fujioka S., Takatsuto S., Sakurai A., Yoshida S., Li J.,
RA Chory J.;
RT "Arabidopsis det2 is defective in the conversion of (24R)-24-methylcholest-
RT 4-en-3-one to (24R)-24-methyl-5alpha-cholestan-3-one in brassinosteroid
RT biosynthesis.";
RL Plant Physiol. 120:833-840(1999).
RN [9]
RP MUTAGENESIS OF GLU-204.
RX PubMed=11161033; DOI=10.1104/pp.125.2.763;
RA Steber C.M., McCourt P.;
RT "A role for brassinosteroids in germination in Arabidopsis.";
RL Plant Physiol. 125:763-769(2001).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=11867704; DOI=10.1093/pcp/pcf024;
RA Nakaya M., Tsukaya H., Murakami N., Kato M.;
RT "Brassinosteroids control the proliferation of leaf cells of Arabidopsis
RT thaliana.";
RL Plant Cell Physiol. 43:239-244(2002).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLU-204.
RC STRAIN=cv. Columbia;
RX PubMed=15993049; DOI=10.1016/j.jsbmb.2005.04.035;
RA Rosati F., Bardazzi I., De Blasi P., Simi L., Scarpi D., Guarna A.,
RA Serio M., Racchi M.L., Danza G.;
RT "5alpha-Reductase activity in Lycopersicon esculentum: cloning and
RT functional characterization of LeDET2 and evidence of the presence of two
RT isoenzymes.";
RL J. Steroid Biochem. Mol. Biol. 96:287-299(2005).
RN [12]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=cv. Columbia;
RX PubMed=22822057; DOI=10.1074/jbc.m112.392720;
RA Ohnishi T., Godza B., Watanabe B., Fujioka S., Hategan L., Ide K.,
RA Shibata K., Yokota T., Szekeres M., Mizutani M.;
RT "CYP90A1/CPD, a brassinosteroid biosynthetic cytochrome P450 of
RT Arabidopsis, catalyzes C-3 oxidation.";
RL J. Biol. Chem. 287:31551-31560(2012).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=23771896; DOI=10.1104/pp.113.217703;
RA Jiang W.B., Huang H.Y., Hu Y.W., Zhu S.W., Wang Z.Y., Lin W.H.;
RT "Brassinosteroid regulates seed size and shape in Arabidopsis.";
RL Plant Physiol. 162:1965-1977(2013).
CC -!- FUNCTION: Involved in a reduction step in the biosynthesis of the plant
CC steroid, brassinolide (BL); acts at the second step in brassinolide
CC biosynthesis in the 5alpha-reduction of (24R)- 24-methylcholest-4-en-3-
CC one, which is further modified to form campestanol. Can use
CC progesterone, testosterone, androstenedione and campestenone as
CC substrate. Catalyzes also the conversion of campest-4-en-3-one
CC (campesta-4-en-3-one, 4-en-3-one) to campest-3-one (campesta-3-one, 3-
CC one), of (22S,24R)-22-hydroxyergost-4-en-3-one (22-hydroxy-campesta-4-
CC en-3-one, 22-OH-4-en-3-one) to (22S,24R)-22-hydroxy-5alpha-ergostan-3-
CC one (22-hydroxy-campesta-3-one, 22-OH-3-one), and of (22R,23R)-22,23-
CC dihydroxy-5alpha-campestan-3-one (22,23,diOH-4-en-3-one) to (22R,23R)-
CC 22,23-dihydroxycampest-4-en-3-one (6-deoxo3DT) (PubMed:22822057).
CC Required for the brassinosteroid- (BR) dependent regulation of seed
CC size and shape as well as embryo development (PubMed:23771896).
CC {ECO:0000269|PubMed:10398719, ECO:0000269|PubMed:11867704,
CC ECO:0000269|PubMed:15993049, ECO:0000269|PubMed:22822057,
CC ECO:0000269|PubMed:23771896, ECO:0000269|PubMed:8602526,
CC ECO:0000269|PubMed:9108014, ECO:0000269|PubMed:9401120}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3-oxo-5alpha-steroid + NADP(+) = a 3-oxo-Delta(4)-steroid +
CC H(+) + NADPH; Xref=Rhea:RHEA:54384, ChEBI:CHEBI:13601,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:47909, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.3.1.22;
CC Evidence={ECO:0000269|PubMed:10398719, ECO:0000269|PubMed:15993049,
CC ECO:0000269|PubMed:9108014};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5alpha-campestan-3-one + NADP(+) = campest-4-en-3-one + H(+) +
CC NADPH; Xref=Rhea:RHEA:54416, ChEBI:CHEBI:15378, ChEBI:CHEBI:18533,
CC ChEBI:CHEBI:18534, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000269|PubMed:22822057};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:54418;
CC Evidence={ECO:0000269|PubMed:22822057};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(22S,24R)-22-hydroxy-5alpha-ergostan-3-one + NADP(+) = (22S)-
CC 22-hydroxycampest-4-en-3-one + H(+) + NADPH; Xref=Rhea:RHEA:69987,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:59411, ChEBI:CHEBI:72330;
CC Evidence={ECO:0000269|PubMed:22822057};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:69989;
CC Evidence={ECO:0000269|PubMed:22822057};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-dehydro-6-deoxoteasterone + NADP(+) = (22R,23R)-22,23-
CC dihydroxycampest-4-en-3-one + H(+) + NADPH; Xref=Rhea:RHEA:69991,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:20710, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:80402;
CC Evidence={ECO:0000269|PubMed:22822057};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69992;
CC Evidence={ECO:0000269|PubMed:22822057};
CC -!- ACTIVITY REGULATION: Inhibited by the 4-azasteroids 4-MA.
CC {ECO:0000269|PubMed:9108014}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=15.3 uM for campest-4-en-3-one {ECO:0000269|PubMed:22822057};
CC KM=3.9 uM for (22S,24R)-22-hydroxyergost-4-en-3-one
CC {ECO:0000269|PubMed:22822057};
CC KM=8.5 uM for cholest-4-en-3-one {ECO:0000269|PubMed:22822057};
CC KM=3.0 uM for (22R,23R)-22,23-dihydroxy-campest-4-en-3-one
CC {ECO:0000269|PubMed:22822057};
CC KM=2.5 uM for testosterone {ECO:0000269|PubMed:9108014};
CC KM=0.4 uM for progesterone {ECO:0000269|PubMed:9108014};
CC Vmax=1.4 umol/min/mg enzyme with campest-4-en-3-one as substrate
CC {ECO:0000269|PubMed:22822057};
CC Vmax=0.85 umol/min/mg enzyme with (22S,24R)-22-hydroxyergost-4-en-3-
CC one as substrate {ECO:0000269|PubMed:22822057};
CC Vmax=1.02 umol/min/mg enzyme with cholest-4-en-3-one as substrate
CC {ECO:0000269|PubMed:22822057};
CC Vmax=0.64 umol/min/mg enzyme with (22R,23R)-22,23-dihydroxy-campest-
CC 4-en-3-one as substrate {ECO:0000269|PubMed:22822057};
CC Vmax=0.2 nmol/min/mg enzyme with testosterone as substrate
CC {ECO:0000269|PubMed:9108014};
CC Vmax=0.5 nmol/min/mg enzyme with progesterone as substrate
CC {ECO:0000269|PubMed:9108014};
CC pH dependence:
CC Optimum pH is 6.8. {ECO:0000269|PubMed:9108014};
CC -!- PATHWAY: Plant hormone biosynthesis; brassinosteroid biosynthesis.
CC {ECO:0000269|PubMed:22822057}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Brassinolide-reversible dark- and light-grown
CC defects; small dark-green dwarf plants with a limited leaves expension
CC due to a reduced number of cells per leaf blade (PubMed:10394910,
CC PubMed:11867704, PubMed:8602526, PubMed:9401120). Small and less
CC elongated seeds due to a decreased seed cavity, reduced endosperm
CC volume and integument cell length (PubMed:22822057). Delay embryo
CC development, with a reduction in both the size and number of embryo
CC cells (PubMed:22822057). {ECO:0000269|PubMed:10394910,
CC ECO:0000269|PubMed:11867704, ECO:0000269|PubMed:22822057,
CC ECO:0000269|PubMed:8602526, ECO:0000269|PubMed:9401120}.
CC -!- SIMILARITY: Belongs to the steroid 5-alpha reductase family.
CC {ECO:0000305}.
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DR EMBL; U53860; AAC49264.1; -; mRNA.
DR EMBL; CP002685; AEC09484.1; -; Genomic_DNA.
DR EMBL; AY045926; AAK76600.1; -; mRNA.
DR EMBL; AY079337; AAL85068.1; -; mRNA.
DR PIR; C84800; C84800.
DR RefSeq; NP_181340.1; NM_129361.5.
DR AlphaFoldDB; Q38944; -.
DR SMR; Q38944; -.
DR BioGRID; 3727; 2.
DR IntAct; Q38944; 2.
DR STRING; 3702.AT2G38050.1; -.
DR PaxDb; Q38944; -.
DR PRIDE; Q38944; -.
DR ProteomicsDB; 224655; -.
DR EnsemblPlants; AT2G38050.1; AT2G38050.1; AT2G38050.
DR GeneID; 818383; -.
DR Gramene; AT2G38050.1; AT2G38050.1; AT2G38050.
DR KEGG; ath:AT2G38050; -.
DR Araport; AT2G38050; -.
DR TAIR; locus:2005506; AT2G38050.
DR eggNOG; KOG1638; Eukaryota.
DR HOGENOM; CLU_065395_1_0_1; -.
DR InParanoid; Q38944; -.
DR OMA; WLEWLGF; -.
DR OrthoDB; 1574389at2759; -.
DR PhylomeDB; Q38944; -.
DR BioCyc; ARA:AT2G38050-MON; -.
DR BioCyc; MetaCyc:AT2G38050-MON; -.
DR SABIO-RK; Q38944; -.
DR UniPathway; UPA00381; -.
DR PRO; PR:Q38944; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q38944; baseline and differential.
DR Genevisible; Q38944; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003865; F:3-oxo-5-alpha-steroid 4-dehydrogenase activity; IEA:InterPro.
DR GO; GO:0102728; F:campest-4-en-3-one,NADPH:steroid 5alpha-reductase activity; IEA:RHEA.
DR GO; GO:0047751; F:cholestenone 5-alpha-reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0050213; F:progesterone 5-alpha-reductase activity; IDA:UniProtKB.
DR GO; GO:0009917; F:sterol 5-alpha reductase activity; IDA:TAIR.
DR GO; GO:0016132; P:brassinosteroid biosynthetic process; IDA:TAIR.
DR GO; GO:0010268; P:brassinosteroid homeostasis; IEP:TAIR.
DR InterPro; IPR016636; 3-oxo-5-alpha-steroid_4-DH.
DR InterPro; IPR001104; 3-oxo-5_a-steroid_4-DH_C.
DR InterPro; IPR039357; SRD5A/TECR.
DR PANTHER; PTHR10556; PTHR10556; 1.
DR Pfam; PF02544; Steroid_dh; 1.
DR PIRSF; PIRSF015596; 5_alpha-SR2; 1.
DR PROSITE; PS50244; S5A_REDUCTASE; 1.
PE 1: Evidence at protein level;
KW Brassinosteroid biosynthesis; Lipid biosynthesis; Lipid metabolism;
KW Membrane; NADP; Oxidoreductase; Reference proteome; Steroid biosynthesis;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..262
FT /note="Steroid 5-alpha-reductase DET2"
FT /id="PRO_0000213681"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MUTAGEN 204
FT /note="E->K: In cro1-2 and det2-1; loss of activity,
FT enhanced sensitivity to abscisic acid (ABA) during seed
FT germination."
FT /evidence="ECO:0000269|PubMed:10394910,
FT ECO:0000269|PubMed:10398719, ECO:0000269|PubMed:11161033,
FT ECO:0000269|PubMed:15993049, ECO:0000269|PubMed:9108014,
FT ECO:0000269|PubMed:9401120"
FT CONFLICT 198
FT /note="C -> R (in Ref. 1; AAC49264)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 262 AA; 30635 MW; 88291B8A8AF55664 CRC64;
MEEIADKTFF RYCLLTLIFA GPPTAVLLKF LQAPYGKHNR TGWGPTVSPP IAWFVMESPT
LWLTLLLFPF GRHALNPKSL LLFSPYLIHY FHRTIIYPLR LFRSSFPAGK NGFPITIAAL
AFTFNLLNGY IQARWVSHYK DDYEDGNWFW WRFVIGMVVF ITGMYINITS DRTLVRLKKE
NRGGYVIPRG GWFELVSCPN YFGEAIEWLG WAVMTWSWAG IGFFLYTCSN LFPRARASHK
WYIAKFKEEY PKTRKAVIPF VY
