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Q02769 (FDFT_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Squalene synthase

Short name=SQS
Short name=SS
EC=2.5.1.21
Alternative name(s):
FPP:FPP farnesyltransferase
Farnesyl-diphosphate farnesyltransferase
Gene names
Name:Fdft1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length416 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Critical branch point enzyme of isoprenoid biosynthesis that is thought to regulate the flux of isoprene intermediates through the sterol pathway.

Catalytic activity

2 farnesyl diphosphate + NAD(P)H = squalene + 2 diphosphate + NAD(P)+.

Cofactor

Magnesium.

Pathway

Terpene metabolism; lanosterol biosynthesis; lanosterol from farnesyl diphosphate: step 1/3.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.4.

Disruption phenotype

Hypomorphic mutations in the Lss gene and in this gene were identified, as well as a null mutation in the Lss gene. Cataract onset is associated with the specific combination of Lss and Fdft1 mutant alleles that decrease cholesterol levels in cataractous lenses to about 57% of normal. Cholesterol insufficiency may cause the deficient proliferation of lens epithelial cells in Shumiya cataract rats, resulting in the loss of homeostatic epithelial cell control of the underlying fiber cells and ultimately cataractogenesis. Ref.5

Sequence similarities

Belongs to the phytoene/squalene synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 416416Squalene synthase
PRO_0000067445

Regions

Transmembrane284 – 30421Helical; Potential
Transmembrane384 – 40421Helical; Potential

Natural variations

Natural variant1 – 6464Missing in truncated, active form.

Sequences

Sequence LengthMass (Da)Tools
Q02769 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: F4BC4D09C9F72169

FASTA41648,106
        10         20         30         40         50         60 
MEFVKCLGHP EEFYNLLRFR MGGRRNFIPK MDRNSLSNSL KTCYKYLDQT SRSFAAVIQA 

        70         80         90        100        110        120 
LDGDIRHAVC VFYLILRAMD TVEDDMAISV EKKIPLLRNF HTFLYEPEWR FTESKEKHRV 

       130        140        150        160        170        180 
VLEDFPTISL EFRNLAEKYQ TVIADICHRM GCGMAEFLNK DVTSKQDWDK YCHYVAGLVG 

       190        200        210        220        230        240 
IGLSRLFSAS EFEDPIVGED TECANSMGLF LQKTNIIRDY LEDQQEGRQF WPQEVWGKYV 

       250        260        270        280        290        300 
KKLEDFVKPE NVDVAVKCLN ELITNALQHI PDVITYLSRL RNQSVFNFCA IPQVMAIATL 

       310        320        330        340        350        360 
AACYNNHQVF KGVVKIRKGQ AVTLMMDATN MPAVKAIIYQ YIEEIYHRVP NSDPSASKAK 

       370        380        390        400        410 
QLISNIRTQS LPNCQLISRS HYSPIYLSFI MLLAALSWQY LSTLSQVTED YVQREH 

« Hide

References

« Hide 'large scale' references
[1]"Solubilization, purification, and characterization of a truncated form of rat hepatic squalene synthetase."
Shechter I., Klinger E., Rucker M.L., Engstrom R.G., Spirito J.A., Islam M.A., Boettcher B.R., Wienstein D.B.
J. Biol. Chem. 267:8628-8635(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Molecular cloning, expression, and characterization of the cDNA for the rat hepatic squalene synthase."
McKenzie T.L., Jiang G., Straubhaar J.R., Conrad D.G., Shechter I.
J. Biol. Chem. 267:21368-21374(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Heart.
[4]"Subcellular localization of squalene synthase in rat hepatic cells. Biochemical and immunochemical evidence."
Stamellos K.D., Shackelford J.E., Schechter I., Jiang G., Conrad D.G., Keller G.-A., Krisans S.K.
J. Biol. Chem. 268:12825-12836(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
Tissue: Liver.
[5]"Lanosterol synthase mutations cause cholesterol deficiency-associated cataracts in the Shumiya cataract rat."
Mori M., Li G., Abe I., Nakayama J., Guo Z., Sawashita J., Ugawa T., Nishizono S., Serikawa T., Higuchi K., Shumiya S.
J. Clin. Invest. 116:395-404(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M95591 mRNA. Translation: AAA42179.1.
BC081810 mRNA. Translation: AAH81810.1.
PIRA45105.
RefSeqNP_062111.1. NM_019238.2.
UniGeneRn.154404.

3D structure databases

ProteinModelPortalQ02769.
SMRQ02769. Positions 34-370.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-4569367.
STRING10116.ENSRNOP00000029808.

Chemistry

BindingDBQ02769.
ChEMBLCHEMBL3815.
GuidetoPHARMACOLOGY645.

Proteomic databases

PaxDbQ02769.
PRIDEQ02769.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000032089; ENSRNOP00000029808; ENSRNOG00000021314.
GeneID29580.
KEGGrno:29580.
UCSCRGD:61834. rat.

Organism-specific databases

CTD2222.
RGD61834. Fdft1.

Phylogenomic databases

eggNOGCOG1562.
GeneTreeENSGT00390000016034.
HOGENOMHOG000186940.
HOVERGENHBG002370.
InParanoidQ02769.
KOK00801.
OMAEMRHAVC.
OrthoDBEOG7QRQTS.
PhylomeDBQ02769.
TreeFamTF105316.

Enzyme and pathway databases

UniPathwayUPA00767; UER00751.

Gene expression databases

GenevestigatorQ02769.

Family and domain databases

Gene3D1.10.600.10. 1 hit.
InterProIPR002060. Squ/phyt_synthse.
IPR006449. Squal_synth.
IPR019845. Squalene/phytoene_synthase_CS.
IPR008949. Terpenoid_synth.
[Graphical view]
PfamPF00494. SQS_PSY. 1 hit.
[Graphical view]
SUPFAMSSF48576. SSF48576. 1 hit.
TIGRFAMsTIGR01559. squal_synth. 1 hit.
PROSITEPS01044. SQUALEN_PHYTOEN_SYN_1. 1 hit.
PS01045. SQUALEN_PHYTOEN_SYN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio609686.
PROQ02769.

Entry information

Entry nameFDFT_RAT
AccessionPrimary (citable) accession number: Q02769
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: April 16, 2014
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways