Q9STX2 (VEP1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-oxo-Delta(4,5)-steroid 5-beta-reductase
EC=1.3.1.3

Alternative name(s):
Delta(4)-3-oxosteroid 5-beta-reductase
Delta-4,5-steroid 5-beta-reductase
Short name=At5beta-StR
Progesterone 5-beta-reductase
Short name=5beta-POR
Protein VEIN PATTERNING 1

Gene names

Name:	VEP1
Synonyms:	AWI31
Ordered Locus Names:	At4g24220
ORF Names:	T22A6.50

Organism

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

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	388 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in vascular strand development. Catalyzes the stereospecific conversion of progesterone to 5-beta-pregnane-3,20-dione. Can use progesterone, testosterone, 21-acetyl cortexone, 2-cyclohexenone, but-1-en-3-one, ethyl acrylate, ethylmethacrylate, cortisone and canarigenone as substrates, lower activity with 3-methyl-2-cyclohexenone and 3,5,5-trimethyl-2-cyclohexenone as substrate, and no activity with canarigenin, canarigenin digitoxoside and pregnenolone. May be involved in the formation of 5-beta phytoecdysteroids. Ref.2 Ref.4
Catalytic activity	5-beta-cholestan-3-one + NADP+ = cholest-4-en-3-one + NADPH. Ref.4 Ref.9 Ref.10 17,21-dihydroxy-5-beta-pregnane-3,11,20-trione + NADP+ = cortisone. Ref.4 Ref.9 Ref.10
Subunit structure	Homodimer. Ref.4
Tissue specificity	Expressed in roots, stems, leaves, flowers, seeds and siliques. Expressed in the vascular bundles. Ref.2 Ref.4
Induction	Up-regulated by wounding. Not induced by drought, high salt, low temperature or herbicide treatment. Ref.1 Ref.2
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family. Highly divergent.
Biophysicochemical properties	Kinetic parameters: kcat is 10.11 min(-1) with progesterone as substrate. kcat is 66.85 min(-1) with 2-cyclohexen-1-one as substrate. KM=268 µM for progesterone Ref.4 Ref.10 KM=755 µM for cortisol KM=1423 µM for 4-androstene-3,17-dione KM=764 µM for cortexone KM=5 µM for NADPH KM=116 µM for 2-cyclohexen-1-one pH dependence: Optimum pH is 8.0. Temperature dependence: Optimum temperature is 45 degrees Celsius.
Sequence caution	The sequence CAA68126.1 differs from that shown. Reason: Frameshift at positions 225, 273 and 301.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	response to wounding Inferred from expression pattern Ref.2. Source: TAIR steroid metabolic process Inferred from direct assay Ref.4. Source: TAIR xylem and phloem pattern formation Inferred from mutant phenotype Ref.2. Source: TAIR
Cellular_component	cytosol Inferred from direct assay PubMed 21166475. Source: TAIR
Molecular_function	delta4-3-oxosteroid 5beta-reductase activity Inferred from electronic annotation. Source: EC enone reductase activity Inferred from direct assay Ref.4. Source: TAIR nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9STX2-1)

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.

Isoform 2 (identifier: Q9STX2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     13-13: Missing.

Note: Derived from EST data. No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 388	388	3-oxo-Delta(4,5)-steroid 5-beta-reductase		PRO_0000419904
Regions
	Nucleotide binding	35 – 37	3	NADP By similarity
	Nucleotide binding	63 – 64	2	NADP By similarity
	Nucleotide binding	81 – 82	2	NADP By similarity
	Nucleotide binding	212 – 214	3	NADP By similarity
Sites
	Active site	147	1	By similarity
	Active site	178	1	By similarity
	Binding site	105	1	NADP By similarity
	Binding site	143	1	NADP By similarity
	Binding site	178	1	NADP By similarity
	Binding site	205	1	NADP; via amide nitrogen By similarity
Natural variations
	Alternative sequence	13	1	Missing in isoform 2.		VSP_044368
Experimental info
	Sequence conflict	2	1	S → R in CAA68126. Ref.1
	Sequence conflict	36	1	G → A in CAA68126. Ref.1
	Sequence conflict	192	1	I → T in CAA68126. Ref.1
	Sequence conflict	359	1	S → R in CAA68126. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 5ED9D6C12330A161	FASTA	388	44,230
	10 20 30 40 50 60 MSWWWAGAIG AAKKKLDEDE PSQSFESVAL IIGVTGIVGN SLAEILPLSD TPGGPWKVYG 70 80 90 100 110 120 VARRPRPTWN ADHPIDYIQC DVSDAEDTRS KLSPLTDVTH VFYVTWTNRE SESENCEANG 130 140 150 160 170 180 SMLRNVLQAI IPYAPNLRHV CLQTGTKHYL GPFTNVDGPR HDPPFTEDMP RLQIQNFYYT 190 200 210 220 230 240 QEDILFEEIK KIETVTWSIH RPNMIFGFSP YSLMNIVGTL CVYAAICKHE GSPLLFPGSK 250 260 270 280 290 300 KAWEGFMTAS DADLIAEQQI WAAVDPYAKN EAFNCNNADI FKWKHLWKIL AEQFGIEEYG 310 320 330 340 350 360 FEEGKNLGLV EMMKGKERVW EEMVKENQLQ EKKLEEVGVW WFADVILGVE GMIDSMNKSK 370 380 EYGFLGFRNS NNSFISWIDK YKAFKIVP
	Isoform 2 [UniParc]. Checksum: CAC31EE997A67A1A	FASTA	387	44,102
	10 20 30 40 50 60 MSWWWAGAIG AAKKLDEDEP SQSFESVALI IGVTGIVGNS LAEILPLSDT PGGPWKVYGV 70 80 90 100 110 120 ARRPRPTWNA DHPIDYIQCD VSDAEDTRSK LSPLTDVTHV FYVTWTNRES ESENCEANGS 130 140 150 160 170 180 MLRNVLQAII PYAPNLRHVC LQTGTKHYLG PFTNVDGPRH DPPFTEDMPR LQIQNFYYTQ 190 200 210 220 230 240 EDILFEEIKK IETVTWSIHR PNMIFGFSPY SLMNIVGTLC VYAAICKHEG SPLLFPGSKK 250 260 270 280 290 300 AWEGFMTASD ADLIAEQQIW AAVDPYAKNE AFNCNNADIF KWKHLWKILA EQFGIEEYGF 310 320 330 340 350 360 EEGKNLGLVE MMKGKERVWE EMVKENQLQE KKLEEVGVWW FADVILGVEG MIDSMNKSKE 370 380 YGFLGFRNSN NSFISWIDKY KAFKIVP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure and expression of the AWI 31 gene specifically induced by wounding in Arabidopsis thaliana." Yang K.Y., Moon Y.H., Choi K.H., Kim Y.H., Eun M.Y., Guh J.O., Kim K.C., Cho B.H. Mol. Cells 7:131-135(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION.
[2]	"Involvement of the VEP1 gene in vascular strand development in Arabidopsis thaliana." Jun J.H., Ha C.M., Nam H.G. Plant Cell Physiol. 43:323-330(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, INDUCTION BY WOUNDING.
[3]	"Using progesterone 5beta-reductase, a gene encoding a key enzyme in the cardenolide biosynthesis, to infer the phylogeny of the genus Digitalis." Herl V., Albach D.C., Mueller-Uri F., Braeuchler C., Heubl G., Kreis W. Plant Syst. Evol. 271:65-78(2008) [AGRICOLA] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Leaf.
[4]	"The VEP1 gene (At4g24220) encodes a short-chain dehydrogenase/reductase with 3-oxo-Delta4,5-steroid 5beta-reductase activity in Arabidopsis thaliana L." Herl V., Fischer G., Reva V.A., Stiebritz M., Muller Y.A., Mueller-Uri F., Kreis W. Biochimie 91:517-525(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, TISSUE SPECIFICITY, SUBUNIT, 3D-STRUCTURE MODELING.
[5]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[6]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[7]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: cv. Columbia.
[8]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[9]	"Highly conserved progesterone 5 beta-reductase genes (P5 beta R) from 5 beta-cardenolide-free and 5 beta-cardenolide-producing angiosperms." Bauer P., Munkert J., Brydziun M., Burda E., Mueller-Uri F., Groeger H., Muller Y.A., Kreis W. Phytochemistry 71:1495-1505(2010) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY.
[10]	"Vein Patterning 1-encoded progesterone 5?-reductase: activity-guided improvement of catalytic efficiency." Bauer P., Rudolph K., Mueller-Uri F., Kreis W. Phytochemistry 77:53-59(2012) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X99793 Genomic DNA. Translation: CAA68126.1. Frameshift. EF579963 mRNA. Translation: ABU55811.1. AL078637 Genomic DNA. Translation: CAB45057.1. AL161561 Genomic DNA. Translation: CAB79332.1. CP002687 Genomic DNA. Translation: AEE84868.1. CP002687 Genomic DNA. Translation: AEE84869.1. AY062451 mRNA. Translation: AAL32529.1. BT008479 mRNA. Translation: AAP37838.1. AY087323 mRNA. Translation: AAM64873.1.
IPI	IPI00524911. IPI00540048. IPI00846354.
PIR	T09885.
RefSeq	NP_001078438.1. NM_001084969.1. NP_194153.1. NM_118555.4.
UniGene	At.32364. At.71005.
3D structure databases
ProteinModelPortal	Q9STX2.
SMR	Q9STX2. Positions 27-388.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT4G24220.1-P.
Proteomic databases
PRIDE	Q9STX2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G24220.1; AT4G24220.1; AT4G24220.
GeneID	828523.
KEGG	ath:AT4G24220.
Organism-specific databases
TAIR	At4g24220.
Phylogenomic databases
eggNOG	NOG46937.
HOGENOM	HOG000216741.
InParanoid	Q9STX2.
OMA	GLKHYLG.
PhylomeDB	Q9STX2.
ProtClustDB	CLSN2685402.
Enzyme and pathway databases
BioCyc	ARA:AT4G24220-MONOMER. MetaCyc:AT4G24220-MONOMER.
Gene expression databases
ArrayExpress	Q9STX2.
Genevestigator	Q9STX2.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
InterPro	IPR016040. NAD(P)-bd_dom. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

VEP1_ARATH

Accession

Primary (citable) accession number: Q9STX2
Secondary accession number(s): A8MRU3, Q39171

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2012
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program