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Q02769

- FDFT_RAT

UniProt

Q02769 - FDFT_RAT

Protein

Squalene synthase

Gene

Fdft1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 1 (01 Jul 1993)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

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

    Cofactori

    Magnesium.

    Pathwayi

    GO - Molecular functioni

    1. farnesyl-diphosphate farnesyltransferase activity Source: RGD
    2. oxidoreductase activity Source: UniProtKB-KW
    3. squalene synthase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cholesterol biosynthetic process Source: RGD
    2. farnesyl diphosphate metabolic process Source: RGD
    3. isoprenoid biosynthetic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase, Transferase

    Keywords - Biological processi

    Cholesterol biosynthesis, Cholesterol metabolism, Isoprene biosynthesis, Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism

    Keywords - Ligandi

    Magnesium, NADP

    Enzyme and pathway databases

    ReactomeiREACT_196408. PPARA activates gene expression.
    REACT_198613. Activation of gene expression by SREBF (SREBP).
    UniPathwayiUPA00767; UER00751.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Squalene synthase (EC:2.5.1.21)
    Short name:
    SQS
    Short name:
    SS
    Alternative name(s):
    FPP:FPP farnesyltransferase
    Farnesyl-diphosphate farnesyltransferase
    Gene namesi
    Name:Fdft1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 15

    Organism-specific databases

    RGDi61834. Fdft1.

    Subcellular locationi

    Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW
    3. intracellular membrane-bounded organelle Source: RGD

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    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.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 416416Squalene synthasePRO_0000067445Add
    BLAST

    Proteomic databases

    PaxDbiQ02769.
    PRIDEiQ02769.

    Expressioni

    Gene expression databases

    GenevestigatoriQ02769.

    Interactioni

    Protein-protein interaction databases

    MINTiMINT-4569367.
    STRINGi10116.ENSRNOP00000029808.

    Structurei

    3D structure databases

    ProteinModelPortaliQ02769.
    SMRiQ02769. Positions 34-370.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei284 – 30421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei384 – 40421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the phytoene/squalene synthase family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1562.
    GeneTreeiENSGT00390000016034.
    HOGENOMiHOG000186940.
    HOVERGENiHBG002370.
    InParanoidiQ02769.
    KOiK00801.
    OMAiEMRHAVC.
    OrthoDBiEOG7QRQTS.
    PhylomeDBiQ02769.
    TreeFamiTF105316.

    Family and domain databases

    Gene3Di1.10.600.10. 1 hit.
    InterProiIPR002060. Squ/phyt_synthse.
    IPR006449. Squal_synth.
    IPR019845. Squalene/phytoene_synthase_CS.
    IPR008949. Terpenoid_synth.
    [Graphical view]
    PfamiPF00494. SQS_PSY. 1 hit.
    [Graphical view]
    SUPFAMiSSF48576. SSF48576. 1 hit.
    TIGRFAMsiTIGR01559. squal_synth. 1 hit.
    PROSITEiPS01044. SQUALEN_PHYTOEN_SYN_1. 1 hit.
    PS01045. SQUALEN_PHYTOEN_SYN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q02769-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEFVKCLGHP EEFYNLLRFR MGGRRNFIPK MDRNSLSNSL KTCYKYLDQT    50
    SRSFAAVIQA LDGDIRHAVC VFYLILRAMD TVEDDMAISV EKKIPLLRNF 100
    HTFLYEPEWR FTESKEKHRV VLEDFPTISL EFRNLAEKYQ TVIADICHRM 150
    GCGMAEFLNK DVTSKQDWDK YCHYVAGLVG IGLSRLFSAS EFEDPIVGED 200
    TECANSMGLF LQKTNIIRDY LEDQQEGRQF WPQEVWGKYV KKLEDFVKPE 250
    NVDVAVKCLN ELITNALQHI PDVITYLSRL RNQSVFNFCA IPQVMAIATL 300
    AACYNNHQVF KGVVKIRKGQ AVTLMMDATN MPAVKAIIYQ YIEEIYHRVP 350
    NSDPSASKAK QLISNIRTQS LPNCQLISRS HYSPIYLSFI MLLAALSWQY 400
    LSTLSQVTED YVQREH 416
    Length:416
    Mass (Da):48,106
    Last modified:July 1, 1993 - v1
    Checksum:iF4BC4D09C9F72169
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1 – 6464Missing in truncated, active form.
    Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M95591 mRNA. Translation: AAA42179.1.
    BC081810 mRNA. Translation: AAH81810.1.
    PIRiA45105.
    RefSeqiNP_062111.1. NM_019238.2.
    UniGeneiRn.154404.

    Genome annotation databases

    EnsembliENSRNOT00000032089; ENSRNOP00000029808; ENSRNOG00000021314.
    GeneIDi29580.
    KEGGirno:29580.
    UCSCiRGD:61834. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M95591 mRNA. Translation: AAA42179.1 .
    BC081810 mRNA. Translation: AAH81810.1 .
    PIRi A45105.
    RefSeqi NP_062111.1. NM_019238.2.
    UniGenei Rn.154404.

    3D structure databases

    ProteinModelPortali Q02769.
    SMRi Q02769. Positions 34-370.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-4569367.
    STRINGi 10116.ENSRNOP00000029808.

    Chemistry

    BindingDBi Q02769.
    ChEMBLi CHEMBL3815.
    GuidetoPHARMACOLOGYi 645.

    Proteomic databases

    PaxDbi Q02769.
    PRIDEi Q02769.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000032089 ; ENSRNOP00000029808 ; ENSRNOG00000021314 .
    GeneIDi 29580.
    KEGGi rno:29580.
    UCSCi RGD:61834. rat.

    Organism-specific databases

    CTDi 2222.
    RGDi 61834. Fdft1.

    Phylogenomic databases

    eggNOGi COG1562.
    GeneTreei ENSGT00390000016034.
    HOGENOMi HOG000186940.
    HOVERGENi HBG002370.
    InParanoidi Q02769.
    KOi K00801.
    OMAi EMRHAVC.
    OrthoDBi EOG7QRQTS.
    PhylomeDBi Q02769.
    TreeFami TF105316.

    Enzyme and pathway databases

    UniPathwayi UPA00767 ; UER00751 .
    Reactomei REACT_196408. PPARA activates gene expression.
    REACT_198613. Activation of gene expression by SREBF (SREBP).

    Miscellaneous databases

    NextBioi 609686.
    PROi Q02769.

    Gene expression databases

    Genevestigatori Q02769.

    Family and domain databases

    Gene3Di 1.10.600.10. 1 hit.
    InterProi IPR002060. Squ/phyt_synthse.
    IPR006449. Squal_synth.
    IPR019845. Squalene/phytoene_synthase_CS.
    IPR008949. Terpenoid_synth.
    [Graphical view ]
    Pfami PF00494. SQS_PSY. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48576. SSF48576. 1 hit.
    TIGRFAMsi TIGR01559. squal_synth. 1 hit.
    PROSITEi PS01044. SQUALEN_PHYTOEN_SYN_1. 1 hit.
    PS01045. SQUALEN_PHYTOEN_SYN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiFDFT_RAT
    AccessioniPrimary (citable) accession number: Q02769
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: July 1, 1993
    Last modified: October 1, 2014
    This is version 114 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3