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Reviewed, UniProtKB/Swiss-Prot Q9LDR4 (ERG24_ARATH)

Last modified November 3, 2009. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Delta(14)-sterol reductase
    EC=1.3.1.70
Alternative name(s):
    C-14 sterol reductase
    Sterol C14-reductase
    Protein FACKEL
Gene names
Name: FK
Ordered Locus Names: At3g52940
ORF Names: F8J2_111
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IIBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length369 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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 activity

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.

Pathway

Steroid biosynthesis; zymosterol biosynthesis; zymosterol from lanosterol: step 2/6.

Subcellular location

Membrane; Multi-pass membrane protein Probable.

Sequence similarities

Belongs to the ERG4/ERG24 family.

Ontologies

Keywords
   Biological processLipid synthesis
Steroid biosynthesis
Sterol biosynthesis
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
   DomainTransmembrane
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

sterol biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiondelta14-sterol reductase activity Ref.1 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: Q9LDR4-1)

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 369369Delta(14)-sterol reductase
PRO_0000207499

Regions

Transmembrane15 – 3420 Potential
Transmembrane54 – 7623 Potential
Transmembrane86 – 10520 Potential
Transmembrane146 – 16823 Potential
Transmembrane178 – 19518 Potential
Transmembrane208 – 23023 Potential
Transmembrane240 – 26223 Potential
Transmembrane275 – 29723 Potential
Transmembrane317 – 33620 Potential

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 31, 2002. Version 2.
Checksum: F18674BCF27C0502

FASTA36941,913
        10         20         30         40         50         60 
MLLDMDLGVL LPSLQSVYVL VFYFVYLAVA GEILPGKVIR GVLLSDGSQL RYRCNGLLAL 

        70         80         90        100        110        120 
ILLVAILGIC AKLGIVSPLV VADRGLELLS ATFIFCVLVT LALYVTGRSS SNKGSSLKPH 

       130        140        150        160        170        180 
VSGNLVHDWW FGIQLNPQFM SIDLKFFFVR AGMMGWLLIN LSILAKSVQD GSLSQSMILY 

       190        200        210        220        230        240 
QIFCALYILD YFVHEEYMTS TWDIIAERLG FMLVFGDLLW IPFTFSIQGW WLLHNKVELT 

       250        260        270        280        290        300 
VPAIVVNCLV FLIGYMVFRG ANKQKHIFKK NPKTPIWGKP PVVVGGKLLV SGYWGIARHC 

       310        320        330        340        350        360 
NYLGDLMLAL SFSLPCGISS PVPYFYPIYL LILLIWRERR DEVRCAEKYK EIWAEYLRLV 


PWRILPYVY 

« Hide

References

« Hide 'large scale' references
[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: 10859166] [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: 10859167] [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. expand/collapse author list , 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: 11130713] [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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
AY064964 mRNA. Translation: AAL38381.1.
AY133650 mRNA. Translation: AAM91480.1.
IPIIPI00539254.
RefSeqNP_566975.1.
UniGeneAt.9856

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ9LDR4.

Proteomic databases

PRIDEQ9LDR4.

Genome annotation databases

GeneID824460.
GenomeReviewsGene locus AT3G52940 in contig BA000014_GR.
KEGGath:AT3G52940.
NMPDRfig|3702.1.peg.16568.

Organism-specific databases

TAIRAt3g52940.

Phylogenomic databases

OMAIQGWWLL.

Enzyme and pathway databases

BioCycMetaCyc:AT3G52940-MON.
BRENDA1.3.1.70. 302.

Gene expression databases

ArrayExpressQ9LDR4.
GenevestigatorQ9LDR4.

Family and domain databases

InterProIPR001171. Ergosterol_biosynth_ERG4_ERG24.
IPR018083. Sterol_reductase_CS.
[Graphical view]
PfamPF01222. ERG4_ERG24. 1 hit.
[Graphical view]
PROSITEPS01017. STEROL_REDUCT_1. 1 hit.
PS01018. STEROL_REDUCT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameERG24_ARATH
AccessionPrimary (citable) accession number: Q9LDR4
Secondary accession number(s): Q9LD62
Entry history
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: January 31, 2002
Last modified: November 3, 2009
This is version 60 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents