Q5K2N1 (DET2_SOLLC) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Steroid 5-alpha-reductase DET2
Short name=LeDET2
EC=1.3.1.22

Gene names

Name:

DET2

Organism

Solanum lycopersicum (Tomato) (Lycopersicon esculentum) [Reference proteome]

Taxonomic identifier

4081 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Solaneae › Solanum › Lycopersicon

Protein attributes

Sequence length	257 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in a reduction step in the biosynthesis of the plant steroid, brassinolide. Can use progesterone, testosterone, androstenedione and campestenone as substrate. Ref.1
Catalytic activity	A 3-oxo-5-alpha-steroid + NADP+ = a 3-oxo-Delta(4)-steroid + NADPH. Ref.1
Enzyme regulation	Repressed by steroid (4-MA, VG106, PD91, PD17, Finasteride) and non-steroid (AS601811, AFA27, AFA76, AFA131, AFA192) inhibitors; steroid inhibitors are generally more efficient. Ref.1
Pathway	Plant hormone biosynthesis; brassinosteroid biosynthesis.
Subcellular location	Membrane; Multi-pass membrane protein Potential.
Tissue specificity	Mostly expressed in leaves and hypocotyls and, to a lower extent, in stems, cotyledons, roots, seeds and callus. Ref.1
Sequence similarities	Belongs to the steroid 5-alpha reductase family.
Biophysicochemical properties	Kinetic parameters: KM=0.75 µM for progesterone (expressed in COS-7 cells, Ref.1) Ref.1 KM=26 µM for androstenedione (expressed in COS-7 cells, Ref.1) KM=40 µM for testosterone (expressed in COS-7 cells, Ref.1) Vmax=0.34 nmol/min/mg enzyme with progesterone as substrate (expressed in COS-7 cells, Ref.1) Vmax=0.32 nmol/min/mg enzyme with androstenedione as substrate (expressed in COS-7 cells, Ref.1) Vmax=0.21 nmol/min/mg enzyme with testosterone as substrate (expressed in COS-7 cells, Ref.1)

Ontologies

Keywords
Cellular component	Membrane
Domain	Transmembrane Transmembrane helix
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	brassinosteroid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from electronic annotation. Source: InterPro integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	3-oxo-5-alpha-steroid 4-dehydrogenase activity Inferred from electronic annotation. Source: InterPro cholestenone 5-alpha-reductase activity Inferred from electronic annotation. Source: EC progesterone 5-alpha-reductase activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 257	257	Steroid 5-alpha-reductase DET2		PRO_0000418515
Regions
	Transmembrane	11 – 31	21	Helical; Potential
	Transmembrane	47 – 67	21	Helical; Potential
	Transmembrane	78 – 97	20	Helical; Potential
	Transmembrane	110 – 130	21	Helical; Potential
	Transmembrane	151 – 171	21	Helical; Potential
	Transmembrane	200 – 220	21	Helical; Potential

Sequences

	Sequence		Length	Mass (Da)
	Q5K2N1 [UniParc]. Last modified February 15, 2005. Version 1. Checksum: 6D3DA1537BCC1CB7	FASTA	257	29,802
	10 20 30 40 50 60 MFSSDENLFN FIVFFILVMA FPTFILCQFF TSPYGKHYTS ADSGTTISPP IAWAFMESPT 70 80 90 100 110 120 LWLTIIVFRL GKNYTNPLAF LLISPYLFHY TNRTIIYPLR LRSRNTKNNF PLNIAVTAFI 130 140 150 160 170 180 FNLLNAYIQS RWVSHYANYQ EDDWFWVRFG IGLVIFGSGM LLNIWADGVL LGLKSQGGGY 190 200 210 220 230 240 KIPRGGLFDY VSSPNYLGEI MEWLGWALMT WSWAGLAFFV YTCANLVPRA VSNHKWYLQK 250 FGEDYPKNRK AVFPFLY

References

[1]

"5alpha-Reductase activity in Lycopersicon esculentum: cloning and functional characterization of LeDET2 and evidence of the presence of two isoenzymes." Rosati F., Bardazzi I., De Blasi P., Simi L., Scarpi D., Guarna A., Serio M., Racchi M.L., Danza G. J. Steroid Biochem. Mol. Biol. 96:287-299(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES. Strain: cv. Saint Pierre. Tissue: Leaf.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ786362 mRNA. Translation: CAH05260.1.
RefSeq	NP_001234040.1. NM_001247111.1.
UniGene	Les.5994.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	Solyc10g086500.1.1; Solyc10g086500.1.1; Solyc10g086500.1.
GeneID	543801.
Enzyme and pathway databases
BRENDA	1.3.1.30. 279253.
UniPathway	UPA00381.
Family and domain databases
InterPro	IPR016636. 3-oxo-5-alpha-steroid_4-DH. IPR001104. 3-oxo-5_a-steroid_4-DH_C. [Graphical view]
Pfam	PF02544. Steroid_dh. 1 hit. [Graphical view]
PIRSF	PIRSF015596. 5_alpha-SR2. 1 hit.
PROSITE	PS50244. S5A_REDUCTASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DET2_SOLLC

Accession

Primary (citable) accession number: Q5K2N1

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2012
Last sequence update:	February 15, 2005
Last modified:	March 6, 2013
This is version 27 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program