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Very-long-chain 3-oxooacyl-coA reductase let-767 (EC 1.1.1.330) (Lethal protein 767) (Putative steroid dehydrogenase let-767) (Short-chain dehydrogenase 10)

 LE767_CAEEL             Reviewed;         316 AA.
Q09517;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
20-JUN-2002, sequence version 2.
25-OCT-2017, entry version 124.
RecName: Full=Very-long-chain 3-oxooacyl-coA reductase let-767;
EC=1.1.1.330;
AltName: Full=Lethal protein 767;
AltName: Full=Putative steroid dehydrogenase let-767;
AltName: Full=Short-chain dehydrogenase 10;
Name=let-767; Synonyms=dhs-10; ORFNames=C56G2.6;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2;
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[2]
IDENTIFICATION.
Kuervers L.M., O'Neil N.J., Baillie D.L.;
"Let-767 is a gut-specific dehydrogenase.";
(er) Worm Breeder's Gazette 15(3):34(1998).
[3]
FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, MUTAGENESIS OF
GLY-135, AND DISRUPTION PHENOTYPE.
PubMed=12905072; DOI=10.1007/s00438-003-0900-9;
Kuervers L.M., Jones C.L., O'Neil N.J., Baillie D.L.;
"The sterol modifying enzyme LET-767 is essential for growth,
reproduction and development in Caenorhabditis elegans.";
Mol. Genet. Genomics 270:121-131(2003).
[4]
FUNCTION AS A 3-OXOACYL-COA REDUCTASE, CATALYTIC ACTIVITY, AND
PATHWAY.
PubMed=18390550; DOI=10.1074/jbc.M800965200;
Entchev E.V., Schwudke D., Zagoriy V., Matyash V., Bogdanova A.,
Habermann B., Zhu L., Shevchenko A., Kurzchalia T.V.;
"LET-767 is required for the production of branched chain and long
chain fatty acids in Caenorhabditis elegans.";
J. Biol. Chem. 283:17550-17560(2008).
-!- 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.
{ECO:0000269|PubMed:12905072, ECO:0000269|PubMed:18390550}.
-!- CATALYTIC ACTIVITY: A very-long-chain (3R)-3-hydroxyacyl-CoA +
NADP(+) = a very-long-chain 3-oxoacyl-CoA + NADPH.
{ECO:0000269|PubMed:18390550}.
-!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
{ECO:0000269|PubMed:18390550}.
-!- TISSUE SPECIFICITY: Expressed in the gut of larva and adult.
{ECO:0000269|PubMed:12905072}.
-!- DEVELOPMENTAL STAGE: Expressed from first larval stage to adult.
{ECO:0000269|PubMed:12905072}.
-!- DISRUPTION PHENOTYPE: Worms exhibit slow and retarded growth,
reproductive and molting defects, defects in embryogenesis, and
hypersensitivity to cholesterol limitation.
{ECO:0000269|PubMed:12905072}.
-!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
(SDR) family. 17-beta-HSD 3 subfamily. {ECO:0000305}.
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EMBL; FO080744; CCD66337.1; -; Genomic_DNA.
PIR; T15867; T15867.
RefSeq; NP_001254936.1; NM_001268007.1.
UniGene; Cel.38763; -.
ProteinModelPortal; Q09517; -.
SMR; Q09517; -.
BioGrid; 41115; 7.
STRING; 6239.C56G2.6b; -.
SwissLipids; SLP:000000030; -.
SwissLipids; SLP:000000178; -.
iPTMnet; Q09517; -.
EPD; Q09517; -.
PaxDb; Q09517; -.
PeptideAtlas; Q09517; -.
EnsemblMetazoa; C56G2.6a.1; C56G2.6a.1; WBGene00002891.
EnsemblMetazoa; C56G2.6a.2; C56G2.6a.2; WBGene00002891.
GeneID; 175895; -.
UCSC; C56G2.6.2; c. elegans.
CTD; 175895; -.
WormBase; C56G2.6a; CE30639; WBGene00002891; let-767.
eggNOG; KOG1014; Eukaryota.
eggNOG; COG0300; LUCA.
GeneTree; ENSGT00390000010069; -.
HOGENOM; HOG000039237; -.
InParanoid; Q09517; -.
PhylomeDB; Q09517; -.
UniPathway; UPA00094; -.
PRO; PR:Q09517; -.
Proteomes; UP000001940; Chromosome III.
Bgee; WBGene00002891; -.
ExpressionAtlas; Q09517; baseline.
GO; GO:0045179; C:apical cortex; IDA:WormBase.
GO; GO:0005783; C:endoplasmic reticulum; IDA:WormBase.
GO; GO:0102339; F:3-oxo-arachidoyl-CoA reductase activity; IEA:UniProtKB-EC.
GO; GO:0102340; F:3-oxo-behenoyl-CoA reductase activity; IEA:UniProtKB-EC.
GO; GO:0102342; F:3-oxo-cerotoyl-CoA reductase activity; IEA:UniProtKB-EC.
GO; GO:0102341; F:3-oxo-lignoceroyl-CoA reductase activity; IEA:UniProtKB-EC.
GO; GO:0050062; F:long-chain-fatty-acyl-CoA reductase activity; IDA:WormBase.
GO; GO:0030283; F:testosterone dehydrogenase [NAD(P)] activity; IDA:WormBase.
GO; GO:0008209; P:androgen metabolic process; IMP:WormBase.
GO; GO:0009790; P:embryo development; IMP:UniProtKB.
GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IMP:UniProtKB.
GO; GO:0008210; P:estrogen metabolic process; IMP:WormBase.
GO; GO:0030540; P:female genitalia development; IMP:UniProtKB.
GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IDA:WormBase.
GO; GO:0042303; P:molting cycle; IMP:UniProtKB.
GO; GO:0018996; P:molting cycle, collagen and cuticulin-based cuticle; IMP:WormBase.
GO; GO:0032350; P:regulation of hormone metabolic process; IMP:UniProtKB.
GO; GO:0000003; P:reproduction; IMP:UniProtKB.
GO; GO:0006694; P:steroid biosynthetic process; IDA:WormBase.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR020904; Sc_DH/Rdtase_CS.
InterPro; IPR002347; SDR_fam.
Pfam; PF00106; adh_short; 1.
PRINTS; PR00081; GDHRDH.
PRINTS; PR00080; SDRFAMILY.
SUPFAM; SSF51735; SSF51735; 1.
PROSITE; PS00061; ADH_SHORT; 1.
1: Evidence at protein level;
Complete proteome; Fatty acid biosynthesis; Fatty acid metabolism;
Lipid biosynthesis; Lipid metabolism; NADP; Oxidoreductase;
Reference proteome; Steroid biosynthesis.
CHAIN 1 316 Very-long-chain 3-oxooacyl-coA reductase
let-767.
/FTId=PRO_0000054578.
NP_BIND 47 76 NADP. {ECO:0000250}.
ACT_SITE 202 202 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10001}.
BINDING 106 106 NADP. {ECO:0000250}.
BINDING 189 189 Substrate. {ECO:0000250}.
BINDING 206 206 NADP. {ECO:0000250}.
MUTAGEN 135 135 G->R: Arrests at early larval stage.
{ECO:0000269|PubMed:12905072}.
SEQUENCE 316 AA; 34309 MW; DA3C6377AC4C12CE CRC64;
MACQCFLVGA GYVALAAVAY RLLTIFSNIL GPYVLLSPID LKKRAGASWA VVTGATDGIG
KAYAFELARR GFNVLLVSRT QSKLDETKKE ILEKYSSIEV RTAAFDFTNA APSAYKDLLA
TLNQVEIGVL INNVGMSYEY PDVLHKVDGG IERLANITTI NTLPPTLLSA GILPQMVARK
AGVIVNVGSS AGANQMALWA VYSATKKYVS WLTAILRKEY EHQGITVQTI APMMVATKMS
KVKRTSFFTP DGAVFAKSAL NTVGNTSDTT GYITHQLQLE LMDLIPTFIR DKILTNMSVG
TRAAALRKKE REAKSQ


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