Reviewed, UniProtKB/Swiss-Prot Q9LDU6 (ST7R_ARATH)

Names and origin

Protein names

Recommended name:
    7-dehydrocholesterol reductase
      Short name=7-DHC reductase
    EC=1.3.1.21
Alternative name(s):
    Sterol Delta(7)-reductase
    Protein DWARF 5

Gene names

Name:	DWF5
Synonyms:	ST7R
Ordered Locus Names:	At1g50430
ORF Names:	F11F12.21

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	432 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Production of cholesterol by reduction of C7-C8 double bond of 7-dehydrocholesterol (7-DHC). Lesions in the gene coding for the enzyme cause dwarfism.
Catalytic activity	Cholesterol + NADP+ = cholesta-5,7-dien-3-beta-ol + NADPH.
Pathway	Lipid metabolism; steroid biosynthesis.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence similarities	Belongs to the ERG4/ERG24 family.

Ontologies

Keywords
Biological process	Cholesterol biosynthesis Lipid synthesis Steroid biosynthesis Sterol biosynthesis
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing
Domain	Transmembrane
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	brassinosteroid biosynthetic process Ref.2 Inferred from mutant phenotype. Source: TAIR cholesterol biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from direct assay. Source: TAIR
Molecular function	7-dehydrocholesterol reductase activity Inferred from electronic annotation. Source: EC sterol delta7 reductase activity Ref.2 Inferred from mutant phenotype. Source: TAIR
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q9LDU6-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 432	432	7-dehydrocholesterol reductase		PRO_0000207509
Regions
	Transmembrane	12 – 34	23	Potential
	Transmembrane	64 – 86	23	Potential
	Transmembrane	107 – 126	20	Potential
	Transmembrane	136 – 155	20	Potential
	Transmembrane	195 – 212	18	Potential
	Transmembrane	227 – 249	23	Potential
	Transmembrane	261 – 283	23	Potential
	Transmembrane	287 – 309	23	Potential
	Transmembrane	371 – 393	23	Potential
Experimental info
	Mutagenesis	257	1	D → N in DWF5-4; dwarf plant. Ref.2
	Sequence conflict	117	1	Y → H in AAC49278. Ref.1
	Sequence conflict	308	1	N → K in AAC49278. Ref.1
	Sequence conflict	391 – 392	2	Missing in AAC49278. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 5458E495BE1EF4B0	FASTA	432	49,591
	10 20 30 40 50 60 MAETVHSPIV TYASMLSLLA FCPPFVILLW YTMVHQDGSV TQTFGFFWEN GVQGLINIWP 70 80 90 100 110 120 RPTLIAWKII FCYGAFEAIL QLLLPGKRVE GPISPAGNRP VYKANGLAAY FVTLATYLGL 130 140 150 160 170 180 WWFGIFNPAI VYDHLGEIFS ALIFGSFIFC VLLYIKGHVA PSSSDSGSCG NLIIDFYWGM 190 200 210 220 230 240 ELYPRIGKSF DIKVFTNCRF GMMSWAVLAV TYCIKQYEIN GKVSDSMLVN TILMLVYVTK 250 260 270 280 290 300 FFWWEAGYWN TMDIAHDRAG FYICWGCLVW VPSVYTSPGM YLVNHPVELG TQLAIYILVA 310 320 330 340 350 360 GILCIYINYD CDRQRQEFRR TNGKCLVWGR APSKIVASYT TTSGETKTSL LLTSGWWGLA 370 380 390 400 410 420 RHFHYVPEIL SAFFWTVPAL FDNFLAYFYV IFLTLLLFDR AKRDDDRCRS KYGKYWKLYC 430 EKVKYRIIPG IY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning by metabolic interference in yeast and enzymatic characterization of Arabidopsis thaliana sterol delta 7-reductase." Lecain E., Chenivesse X., Spagnoli R., Pompon D. J. Biol. Chem. 271:10866-10873(1996) [PubMed: 8631902] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION. Tissue: Seedling.
[2]	"Lesions in the sterol delta reductase gene of Arabidopsis cause dwarfism due to a block in brassinosteroid biosynthesis." Choe S., Tanaka A., Noguchi T., Fujioka S., Takatsuto S., Ross A.S., Tax F.E., Yoshida S., Feldmann K.A. Plant J. 21:431-443(2000) [PubMed: 10758495] [Abstract] Cited for: NUCLEOTIDE SEQUENCE, MUTAGENESIS OF ASP-257. Strain: cv. Wassilewskija-2.
[3]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U49398 mRNA. Translation: AAC49278.1. AF239701 Genomic DNA. Translation: AAF63498.1. AC012561 Genomic DNA. Translation: AAF87888.1. AY099589 mRNA. Translation: AAM20440.1. BT000245 mRNA. Translation: AAN15564.1.
IPI	IPI00519262.
PIR	F96540.
RefSeq	NP_175460.1.
UniGene	At.25165
3D structure databases
ModBase	Search...
Proteomic databases
PRIDE	Q9LDU6.
Genome annotation databases
GeneID	841465.
GenomeReviews	Gene locus AT1G50430 in contig CT485782_GR.
NMPDR	fig|3702.1.peg.4516.
Organism-specific databases
TAIR	At1g50430.
Phylogenomic databases
OMA	Q9LDU6. TTISEFW.
Enzyme and pathway databases
BioCyc	MetaCyc:MON-7241.
BRENDA	1.3.1.21. 302.
Gene expression databases
ArrayExpress	Q9LDU6.
GermOnline	AT1G50430. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR001171. Ergosterol_biosynth_ERG4_ERG24. IPR018083. Sterol_reductase_CS. [Graphical view]
Pfam	PF01222. ERG4_ERG24. 1 hit. [Graphical view]
PROSITE	PS01017. STEROL_REDUCT_1. 1 hit. PS01018. STEROL_REDUCT_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ST7R_ARATH

Accession

Primary (citable) accession number: Q9LDU6
Secondary accession number(s): Q38930

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 31, 2002
Last sequence update:	October 1, 2000
Last modified:	May 5, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)