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Protein

Delta(14)-sterol reductase

Gene

FK

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. Required for cell division and expansion and is involved in proper organization of the embryo.

Catalytic activityi

4,4-dimethyl-5-alpha-cholesta-8,24-dien-3-beta-ol + NADP+ = 4,4-dimethyl-5-alpha-cholesta-8,14,24-trien-3-beta-ol + NADPH.

Pathwayi: zymosterol biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes zymosterol from lanosterol.
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Delta(14)-sterol reductase (FK)
  3. no protein annotated in this organism
  4. 3beta-hydroxysteroid-dehydrogenase/decarboxylase isoform 3 (3BETAHSD/D3), 3beta-hydroxysteroid-dehydrogenase/decarboxylase isoform 1 (3BETAHSD/D1), 3beta-hydroxysteroid-dehydrogenase/decarboxylase isoform 2 (3BETAHSD/D2)
  5. no protein annotated in this organism
  6. no protein annotated in this organism
This subpathway is part of the pathway zymosterol biosynthesis, which is itself part of Steroid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes zymosterol from lanosterol, the pathway zymosterol biosynthesis and in Steroid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei265 – 2651NADPBy similarity
Binding sitei269 – 2691NADPBy similarity
Binding sitei289 – 2891NADP; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei294 – 2941NADPBy similarity
Binding sitei341 – 3411NADPBy similarity
Binding sitei356 – 3561NADPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi301 – 3022NADPBy similarity
Nucleotide bindingi345 – 3495NADPBy similarity

GO - Molecular functioni

  • delta14-sterol reductase activity Source: TAIR

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciARA:AT3G52940-MONOMER.
ARA:GQT-1533-MONOMER.
MetaCyc:AT3G52940-MONOMER.
ReactomeiR-ATH-191273. Cholesterol biosynthesis.
R-ATH-2426168. Activation of gene expression by SREBF (SREBP).
UniPathwayiUPA00770; UER00755.

Names & Taxonomyi

Protein namesi
Recommended name:
Delta(14)-sterol reductase (EC:1.3.1.70)
Alternative name(s):
C-14 sterol reductase
Protein FACKEL
Sterol C14-reductase
Gene namesi
Name:FK
Ordered Locus Names:At3g52940
ORF Names:F8J2_111
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G52940.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei15 – 3420HelicalSequence analysisAdd
BLAST
Transmembranei54 – 7623HelicalSequence analysisAdd
BLAST
Transmembranei86 – 10520HelicalSequence analysisAdd
BLAST
Transmembranei146 – 16823HelicalSequence analysisAdd
BLAST
Transmembranei178 – 19518HelicalSequence analysisAdd
BLAST
Transmembranei208 – 23023HelicalSequence analysisAdd
BLAST
Transmembranei240 – 26223HelicalSequence analysisAdd
BLAST
Transmembranei275 – 29723HelicalSequence analysisAdd
BLAST
Transmembranei317 – 33620HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 369369Delta(14)-sterol reductasePRO_0000207499Add
BLAST

Proteomic databases

PaxDbiQ9LDR4.
PRIDEiQ9LDR4.

Expressioni

Gene expression databases

ExpressionAtlasiQ9LDR4. baseline and differential.
GenevisibleiQ9LDR4. AT.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT3G52940.1.

Structurei

3D structure databases

ProteinModelPortaliQ9LDR4.
SMRiQ9LDR4. Positions 12-369.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ERG4/ERG24 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1435. Eukaryota.
ENOG410XP67. LUCA.
HOGENOMiHOG000193296.
InParanoidiQ9LDR4.
KOiK00222.
OMAiLPCGLSH.
PhylomeDBiQ9LDR4.

Family and domain databases

InterProiIPR001171. Ergosterol_biosynth_ERG4_ERG24.
IPR018083. Sterol_reductase_CS.
[Graphical view]
PfamiPF01222. ERG4_ERG24. 1 hit.
[Graphical view]
PROSITEiPS01017. STEROL_REDUCT_1. 1 hit.
PS01018. STEROL_REDUCT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

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

Isoform 1 (identifier: Q9LDR4-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MLLDMDLGVL LPSLQSVYVL VFYFVYLAVA GEILPGKVIR GVLLSDGSQL
60 70 80 90 100
RYRCNGLLAL ILLVAILGIC AKLGIVSPLV VADRGLELLS ATFIFCVLVT
110 120 130 140 150
LALYVTGRSS SNKGSSLKPH VSGNLVHDWW FGIQLNPQFM SIDLKFFFVR
160 170 180 190 200
AGMMGWLLIN LSILAKSVQD GSLSQSMILY QIFCALYILD YFVHEEYMTS
210 220 230 240 250
TWDIIAERLG FMLVFGDLLW IPFTFSIQGW WLLHNKVELT VPAIVVNCLV
260 270 280 290 300
FLIGYMVFRG ANKQKHIFKK NPKTPIWGKP PVVVGGKLLV SGYWGIARHC
310 320 330 340 350
NYLGDLMLAL SFSLPCGISS PVPYFYPIYL LILLIWRERR DEVRCAEKYK
360
EIWAEYLRLV PWRILPYVY
Length:369
Mass (Da):41,913
Last modified:January 31, 2002 - v2
Checksum:iF18674BCF27C0502
GO

Sequence cautioni

The sequence AAF81279.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAC01296.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF256535 mRNA. Translation: AAF82282.1.
AF256536 Genomic DNA. Translation: AAF82283.1.
AF257178 mRNA. Translation: AAF81279.1. Different initiation.
AF263244 Genomic DNA. Translation: AAF82768.1.
AL132969 Genomic DNA. Translation: CAC01296.1. Different initiation.
CP002686 Genomic DNA. Translation: AEE79013.1.
AY064964 mRNA. Translation: AAL38381.1.
AY133650 mRNA. Translation: AAM91480.1.
RefSeqiNP_566975.1. NM_115154.2. [Q9LDR4-1]
UniGeneiAt.9856.

Genome annotation databases

EnsemblPlantsiAT3G52940.1; AT3G52940.1; AT3G52940. [Q9LDR4-1]
GeneIDi824460.
KEGGiath:AT3G52940.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF256535 mRNA. Translation: AAF82282.1.
AF256536 Genomic DNA. Translation: AAF82283.1.
AF257178 mRNA. Translation: AAF81279.1. Different initiation.
AF263244 Genomic DNA. Translation: AAF82768.1.
AL132969 Genomic DNA. Translation: CAC01296.1. Different initiation.
CP002686 Genomic DNA. Translation: AEE79013.1.
AY064964 mRNA. Translation: AAL38381.1.
AY133650 mRNA. Translation: AAM91480.1.
RefSeqiNP_566975.1. NM_115154.2. [Q9LDR4-1]
UniGeneiAt.9856.

3D structure databases

ProteinModelPortaliQ9LDR4.
SMRiQ9LDR4. Positions 12-369.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT3G52940.1.

Proteomic databases

PaxDbiQ9LDR4.
PRIDEiQ9LDR4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G52940.1; AT3G52940.1; AT3G52940. [Q9LDR4-1]
GeneIDi824460.
KEGGiath:AT3G52940.

Organism-specific databases

TAIRiAT3G52940.

Phylogenomic databases

eggNOGiKOG1435. Eukaryota.
ENOG410XP67. LUCA.
HOGENOMiHOG000193296.
InParanoidiQ9LDR4.
KOiK00222.
OMAiLPCGLSH.
PhylomeDBiQ9LDR4.

Enzyme and pathway databases

UniPathwayiUPA00770; UER00755.
BioCyciARA:AT3G52940-MONOMER.
ARA:GQT-1533-MONOMER.
MetaCyc:AT3G52940-MONOMER.
ReactomeiR-ATH-191273. Cholesterol biosynthesis.
R-ATH-2426168. Activation of gene expression by SREBF (SREBP).

Miscellaneous databases

PROiQ9LDR4.

Gene expression databases

ExpressionAtlasiQ9LDR4. baseline and differential.
GenevisibleiQ9LDR4. AT.

Family and domain databases

InterProiIPR001171. Ergosterol_biosynth_ERG4_ERG24.
IPR018083. Sterol_reductase_CS.
[Graphical view]
PfamiPF01222. ERG4_ERG24. 1 hit.
[Graphical view]
PROSITEiPS01017. STEROL_REDUCT_1. 1 hit.
PS01018. STEROL_REDUCT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "FACKEL is a sterol C-14 reductase required for organized cell division and expansion in Arabidopsis embryogenesis."
    Schrick K., Mayer U., Horrichs A., Kuhnt C., Bellini C., Dangl J., Schmidt J., Juergens G.
    Genes Dev. 14:1471-1484(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
  2. "A critical role of sterols in embryonic patterning and meristem programming revealed by the fackel mutants of Arabidopsis thaliana."
    Jang J.-C., Fujioka S., Tasaka M., Seto H., Takatsuto S., Ishii A., Aida M., Yoshida S., Sheen J.
    Genes Dev. 14:1485-1497(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  3. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
    Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
    , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "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].
    Strain: cv. Columbia.

Entry informationi

Entry nameiERG24_ARATH
AccessioniPrimary (citable) accession number: Q9LDR4
Secondary accession number(s): Q9LD62
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: January 31, 2002
Last modified: July 6, 2016
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.