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Q17938 (DAF36_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cholesterol desaturase daf-36

EC=1.3.1.21
Gene names
Name:daf-36
ORF Names:C12D8.5
OrganismCaenorhabditis elegans [Reference proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length428 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the production of 7-dehydrocholesterol (7-DHC) by the desaturation of the C7-C8 single bond of cholesterol. This reaction is the first step in the synthesis of the steroid hormone delta(7)-dafachronic acid. Dafachronic acids bind directly to the nuclear hormone receptor (NHR) daf-12, suppressing dauer formation and inducing reproductive growth. Ref.2 Ref.3 Ref.4

Catalytic activity

Cholesterol + NADP+ = cholesta-5,7-dien-3-beta-ol + NADPH. Ref.3 Ref.4

Cofactor

Binds 1 2Fe-2S cluster per subunit By similarity.

Pathway

Steroid hormone biosynthesis; dafachronic acid biosynthesis. Ref.3 Ref.4

Subcellular location

Membrane; Single-pass membrane protein Potential.

Tissue specificity

Expressed in intestine at all postembryonic stages, including dauer. Expression is reduced in daf-2 mutants. Ref.2

Sequence similarities

Contains 1 Rieske domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 428428Cholesterol desaturase daf-36
PRO_0000421680

Regions

Transmembrane6 – 2621Helical; Potential
Domain81 – 187107Rieske

Sites

Metal binding1221Iron-sulfur (2Fe-2S) Probable
Metal binding1241Iron-sulfur (2Fe-2S); via pros nitrogen By similarity
Metal binding1431Iron-sulfur (2Fe-2S) By similarity
Metal binding1461Iron-sulfur (2Fe-2S); via pros nitrogen By similarity

Experimental info

Mutagenesis1221C → A: Abrogates cholesterol dehydrogenase activity. Ref.4
Mutagenesis2341D → A: Abrogates cholesterol dehydrogenase activity. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q17938 [UniParc].

Last modified October 1, 2003. Version 2.
Checksum: 93F0293DF344CBBA

FASTA42849,550
        10         20         30         40         50         60 
MLLEQIWGFL TAHPISVVTT ILIVYLIHIT LKPLNRVRRL GDVGLFFGKP ELKGFYRERQ 

        70         80         90        100        110        120 
LERLKLLRRV GDMPPVFPNG WYCVCESEKL ANNQIMEITV LGQFLSLIRS ESGAVYITDS 

       130        140        150        160        170        180 
YCPHIGANFN IGGRVVRDNC IQCPFHGWIF SAETGKCVEV PYDEGRIPEQ AKVTTWPCIE 

       190        200        210        220        230        240 
RNNNIYLWYH CDGAEPEWEI PEITEITDGF WHLGGRTEHE VMCHIQEIPE NGADIAHLNY 

       250        260        270        280        290        300 
LHKSAPPVTK GSDIIKTDLS DPQPAVQHVW DGKWEVKSEE DRHCGVMHLN QFMTFWGYKV 

       310        320        330        340        350        360 
PLTSSKLVAE QHGPGIVHML FDFGIWGKGV VFQTVTPEEA LLQRVRFRIF SNIPWFFVKF 

       370        380        390        400        410        420 
FMTVEAMQFE RDVFIWSNKK YIKSPLLVKN DGPIQKHRRW FSQFYTENSP KMLKDGSLSN 


QAKSIFDW 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of the nematode C. elegans: a platform for investigating biology."
The C. elegans sequencing consortium
Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.
[2]"Hormonal control of C. elegans dauer formation and life span by a Rieske-like oxygenase."
Rottiers V., Motola D.L., Gerisch B., Cummins C.L., Nishiwaki K., Mangelsdorf D.J., Antebi A.
Dev. Cell 10:473-482(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[3]"The Rieske oxygenase DAF-36 functions as a cholesterol 7-desaturase in steroidogenic pathways governing longevity."
Wollam J., Magomedova L., Magner D.B., Shen Y., Rottiers V., Motola D.L., Mangelsdorf D.J., Cummins C.L., Antebi A.
Aging Cell 10:879-884(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY.
[4]"The conserved Rieske oxygenase DAF-36/Neverland is a novel cholesterol-metabolizing enzyme."
Yoshiyama-Yanagawa T., Enya S., Shimada-Niwa Y., Yaguchi S., Haramoto Y., Matsuya T., Shiomi K., Sasakura Y., Takahashi S., Asashima M., Kataoka H., Niwa R.
J. Biol. Chem. 286:25756-25762(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY, MUTAGENESIS OF CYS-122 AND ASP-234.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z73969 Genomic DNA. Translation: CAA98235.2.
PIRT19219.
RefSeqNP_505629.2. NM_073228.4.
UniGeneCel.4822.

3D structure databases

ProteinModelPortalQ17938.
SMRQ17938. Positions 70-421.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING6239.C12D8.5.

Proteomic databases

PaxDbQ17938.
PRIDEQ17938.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaC12D8.5; C12D8.5; C12D8.5.
GeneID179422.
KEGGcel:CELE_C12D8.5.
UCSCC12D8.5. c. elegans.

Organism-specific databases

CTD179422.
WormBaseC12D8.5; CE34156; WBGene00007536; daf-36.

Phylogenomic databases

eggNOGCOG4638.
HOGENOMHOG000018897.
InParanoidQ17938.
OMAPNGWYRV.
OrthoDBEOG7N0C5Q.
PhylomeDBQ17938.

Enzyme and pathway databases

UniPathwayUPA01020.

Family and domain databases

Gene3D2.102.10.10. 1 hit.
InterProIPR017941. Rieske_2Fe-2S.
[Graphical view]
PfamPF00355. Rieske. 1 hit.
[Graphical view]
SUPFAMSSF50022. SSF50022. 1 hit.
PROSITEPS51296. RIESKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio905318.

Entry information

Entry nameDAF36_CAEEL
AccessionPrimary (citable) accession number: Q17938
Entry history
Integrated into UniProtKB/Swiss-Prot: March 6, 2013
Last sequence update: October 1, 2003
Last modified: April 16, 2014
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormBase