Q09517 (LE767_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Very-long-chain 3-oxooacyl-coA reductase let-767
EC=1.1.1.330

Alternative name(s):
Lethal protein 767
Putative steroid dehydrogenase let-767
Short-chain dehydrogenase 10

Gene names

Name:	let-767
Synonyms:	dhs-10
ORF Names:	C56G2.6

Organism

Caenorhabditis elegans [Reference proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	316 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for branched chain fatty acid synthesis. Catalyzes the reduction of the 3-ketoacyl-CoA intermediate that is formed in each cycle of fatty acid elongation. Very long-chain fatty acids (VLCFAs) serve as precursors for ceramide and sphingolipids. May also be required for sterol hormone production. Ref.3 Ref.4
Catalytic activity	A very-long-chain (3R)-3-hydroxyacyl-CoA + NADP+ = a very-long-chain 3-oxoacyl-CoA + NADPH. Ref.4
Pathway	Lipid metabolism; fatty acid biosynthesis. Ref.4
Tissue specificity	Expressed in the gut of larva and adult. Ref.3
Developmental stage	Expressed from first larval stage to adult. Ref.3
Disruption phenotype	Worms exhibit slow and retarded growth, reproductive and molting defects, defects in embryogenesis, and hypersensitivity to cholesterol limitation. Ref.3
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family. 17-beta-HSD 3 subfamily.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism Steroid biosynthesis
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	androgen metabolic process Inferred from mutant phenotype Ref.3. Source: WormBase embryo development Inferred from mutant phenotype Ref.3. Source: UniProtKB establishment or maintenance of epithelial cell apical/basal polarity Inferred from mutant phenotype PubMed 21926990. Source: UniProtKB estrogen metabolic process Inferred from mutant phenotype Ref.3. Source: WormBase female genitalia development Inferred from mutant phenotype Ref.3. Source: UniProtKB long-chain fatty acid biosynthetic process Inferred from direct assay Ref.4. Source: WormBase molting cycle, collagen and cuticulin-based cuticle Inferred from mutant phenotype Ref.3. Source: WormBase regulation of hormone metabolic process Inferred from mutant phenotype Ref.3. Source: UniProtKB steroid biosynthetic process Inferred from direct assay PubMed 17951538. Source: WormBase
Cellular_component	apical cortex Inferred from direct assay Ref.4. Source: WormBase endoplasmic reticulum Inferred from direct assay Ref.4. Source: WormBase
Molecular_function	long-chain-fatty-acyl-CoA reductase activity Inferred from direct assay Ref.4. Source: WormBase nucleotide binding Inferred from electronic annotation. Source: InterPro testosterone dehydrogenase [NAD(P)] activity Inferred from direct assay PubMed 17951538. Source: WormBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 316	316	Very-long-chain 3-oxooacyl-coA reductase let-767		PRO_0000054578
Regions
	Nucleotide binding	47 – 76	30	NADP By similarity
Sites
	Active site	202	1	Proton acceptor By similarity
	Binding site	106	1	NADP By similarity
	Binding site	189	1	Substrate By similarity
	Binding site	206	1	NADP By similarity
Experimental info
	Mutagenesis	135	1	G → R: Arrests at early larval stage. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q09517 [UniParc]. Last modified June 20, 2002. Version 2. Checksum: DA3C6377AC4C12CE	FASTA	316	34,309
	10 20 30 40 50 60 MACQCFLVGA GYVALAAVAY RLLTIFSNIL GPYVLLSPID LKKRAGASWA VVTGATDGIG 70 80 90 100 110 120 KAYAFELARR GFNVLLVSRT QSKLDETKKE ILEKYSSIEV RTAAFDFTNA APSAYKDLLA 130 140 150 160 170 180 TLNQVEIGVL INNVGMSYEY PDVLHKVDGG IERLANITTI NTLPPTLLSA GILPQMVARK 190 200 210 220 230 240 AGVIVNVGSS AGANQMALWA VYSATKKYVS WLTAILRKEY EHQGITVQTI APMMVATKMS 250 260 270 280 290 300 KVKRTSFFTP DGAVFAKSAL NTVGNTSDTT GYITHQLQLE LMDLIPTFIR DKILTNMSVG 310 TRAAALRKKE REAKSQ

References

	« Hide 'large scale' referencesShow '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]	"Let-767 is a gut-specific dehydrogenase." Kuervers L.M., O'Neil N.J., Baillie D.L. Worm Breeder's Gazette 15(3):34(1998) Cited for: IDENTIFICATION.
[3]	"The sterol modifying enzyme LET-767 is essential for growth, reproduction and development in Caenorhabditis elegans." Kuervers L.M., Jones C.L., O'Neil N.J., Baillie D.L. Mol. Genet. Genomics 270:121-131(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, MUTAGENESIS OF GLY-135, DISRUPTION PHENOTYPE.
[4]	"LET-767 is required for the production of branched chain and long chain fatty acids in Caenorhabditis elegans." Entchev E.V., Schwudke D., Zagoriy V., Matyash V., Bogdanova A., Habermann B., Zhu L., Shevchenko A., Kurzchalia T.V. J. Biol. Chem. 283:17550-17560(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS A 3-OXOACYL-COA REDUCTASE, CATALYTIC ACTIVITY, PATHWAY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	FO080744 Genomic DNA. Translation: CCD66337.1.
PIR	T15867.
RefSeq	NP_001254936.1. NM_001268007.1.
3D structure databases
ProteinModelPortal	Q09517.
SMR	Q09517. Positions 50-271.
ModBase	Search...
Protein-protein interaction databases
STRING	6239.C56G2.6.2.
Proteomic databases
PaxDb	Q09517.
PRIDE	Q09517.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	C56G2.6a.1; C56G2.6a.1; C56G2.6. C56G2.6a.2; C56G2.6a.2; C56G2.6.
GeneID	175895.
KEGG	cel:CELE_C56G2.6.
UCSC	C56G2.6.2. c. elegans.
Organism-specific databases
CTD	175895.
WormBase	C56G2.6a; CE30639; WBGene00002891; let-767.
Phylogenomic databases
eggNOG	COG0300.
GeneTree	ENSGT00390000010069.
HOGENOM	HOG000039237.
InParanoid	Q09517.
Enzyme and pathway databases
UniPathway	UPA00094.
Gene expression databases
ArrayExpress	Q09517.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
InterPro	IPR002198. DH_sc/Rdtase_SDR. IPR002347. Glc/ribitol_DH. IPR016040. NAD(P)-bd_dom. IPR020904. Sc_DH/Rdtase_CS. [Graphical view]
Pfam	PF00106. adh_short. 1 hit. [Graphical view]
PIRSF	PIRSF000126. 11-beta-HSD1. 1 hit.
PRINTS	PR00081. GDHRDH. PR00080. SDRFAMILY.
PROSITE	PS00061. ADH_SHORT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	890204.

Entry information

Entry name

LE767_CAEEL

Accession

Primary (citable) accession number: Q09517

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	June 20, 2002
Last modified:	May 1, 2013
This is version 92 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project