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P53798

- FDFT_MOUSE

UniProt

P53798 - FDFT_MOUSE

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Protein
Squalene synthase
Gene
Fdft1, Erg9
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

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: UniProtKB-EC
  2. oxidoreductase activity Source: UniProtKB-KW
  3. squalene synthase activity Source: UniProtKB-EC

GO - Biological processi

  1. cholesterol biosynthetic process Source: UniProtKB-KW
  2. farnesyl diphosphate metabolic process Source: Ensembl
  3. isoprenoid biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

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_198602. PPARA activates gene expression.
REACT_198969. Activation of gene expression by SREBF (SREBP).
REACT_208531. Cholesterol biosynthesis.
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
Synonyms:Erg9
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 14

Organism-specific databases

MGIiMGI:102706. Fdft1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei284 – 30421Helical; Reviewed prediction
Add
BLAST
Transmembranei384 – 40421Helical; Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 416416Squalene synthase
PRO_0000067444Add
BLAST

Proteomic databases

MaxQBiP53798.
PaxDbiP53798.
PRIDEiP53798.

PTM databases

PhosphoSiteiP53798.

Expressioni

Gene expression databases

BgeeiP53798.
CleanExiMM_FDFT1.
GenevestigatoriP53798.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000055313.

Structurei

3D structure databases

ProteinModelPortaliP53798.
SMRiP53798. Positions 35-369.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1562.
GeneTreeiENSGT00390000016034.
HOGENOMiHOG000186940.
HOVERGENiHBG002370.
InParanoidiQ8BPF5.
KOiK00801.
OMAiEMRHAVC.
OrthoDBiEOG7QRQTS.
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.

P53798-1 [UniParc]FASTAAdd to Basket

« Hide

MEFVKCLGHP EEFYNLLRFR MGGRRNFIPK MDQDSLSSSL KTCYKYLNQT    50
SRSFAAVIQA LDGDIRHAIC VFYLVLRALD TVEDDMSISV EKKIPLLCNF 100
HTFLYDPEWR FTESKEKDRQ VLEDFPTISL EFRNLAEKYQ TVIDDICHRM 150
GCGMAEFVDK DVTSKQDWDK YCHYVAGLVG IGLSRLFSAS EFEDPIVGED 200
IECANSMGLF LQKTNIIRDY LEDQQEGRKF WPQEVWGRYI KKLEDFAKPE 250
NVDVAVQCLN ELITNTLQHI PDVLTYLSRL RNQSVFNFCA IPQVMAIATL 300
AACYNNQQVF KGVVKIRKGQ AVTLMMDATN MPAVKAIIYQ YIEEIYHRIP 350
NSDPSSSKTK QVISKIRTQN LPNCQLISRS HYSPIYLSFI MLLAALSWQY 400
LSTLSQVTED YVQREH 416
Length:416
Mass (Da):48,154
Last modified:July 27, 2011 - v2
Checksum:i12C63625DD4FF92B
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti149 – 1491R → Q in BAA06102. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D29016 mRNA. Translation: BAA06102.1.
AK076062 mRNA. Translation: BAC36156.1.
AK146766 mRNA. Translation: BAE27418.1.
AK158633 mRNA. Translation: BAE34590.1.
AK168629 mRNA. Translation: BAE40489.1.
AK169317 mRNA. Translation: BAE41072.1.
CH466535 Genomic DNA. Translation: EDL36069.1.
BC054722 mRNA. Translation: AAH54722.1.
BC138301 mRNA. Translation: AAI38302.1.
BC138302 mRNA. Translation: AAI38303.1.
CCDSiCCDS27198.1.
PIRiS52075.
RefSeqiNP_034321.2. NM_010191.2.
XP_006518609.1. XM_006518546.1.
UniGeneiMm.474432.

Genome annotation databases

EnsembliENSMUST00000054963; ENSMUSP00000055313; ENSMUSG00000021273.
GeneIDi14137.
KEGGimmu:14137.
UCSCiuc007uhi.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D29016 mRNA. Translation: BAA06102.1 .
AK076062 mRNA. Translation: BAC36156.1 .
AK146766 mRNA. Translation: BAE27418.1 .
AK158633 mRNA. Translation: BAE34590.1 .
AK168629 mRNA. Translation: BAE40489.1 .
AK169317 mRNA. Translation: BAE41072.1 .
CH466535 Genomic DNA. Translation: EDL36069.1 .
BC054722 mRNA. Translation: AAH54722.1 .
BC138301 mRNA. Translation: AAI38302.1 .
BC138302 mRNA. Translation: AAI38303.1 .
CCDSi CCDS27198.1.
PIRi S52075.
RefSeqi NP_034321.2. NM_010191.2.
XP_006518609.1. XM_006518546.1.
UniGenei Mm.474432.

3D structure databases

ProteinModelPortali P53798.
SMRi P53798. Positions 35-369.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000055313.

Chemistry

ChEMBLi CHEMBL4778.

PTM databases

PhosphoSitei P53798.

Proteomic databases

MaxQBi P53798.
PaxDbi P53798.
PRIDEi P53798.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000054963 ; ENSMUSP00000055313 ; ENSMUSG00000021273 .
GeneIDi 14137.
KEGGi mmu:14137.
UCSCi uc007uhi.2. mouse.

Organism-specific databases

CTDi 2222.
MGIi MGI:102706. Fdft1.

Phylogenomic databases

eggNOGi COG1562.
GeneTreei ENSGT00390000016034.
HOGENOMi HOG000186940.
HOVERGENi HBG002370.
InParanoidi Q8BPF5.
KOi K00801.
OMAi EMRHAVC.
OrthoDBi EOG7QRQTS.
TreeFami TF105316.

Enzyme and pathway databases

UniPathwayi UPA00767 ; UER00751 .
Reactomei REACT_198602. PPARA activates gene expression.
REACT_198969. Activation of gene expression by SREBF (SREBP).
REACT_208531. Cholesterol biosynthesis.

Miscellaneous databases

NextBioi 285250.
PROi P53798.
SOURCEi Search...

Gene expression databases

Bgeei P53798.
CleanExi MM_FDFT1.
Genevestigatori P53798.

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

« Hide 'large scale' publications
  1. "Molecular cloning and functional expression of a cDNA for mouse squalene synthase."
    Inoue T., Osumi T., Hata S.
    Biochim. Biophys. Acta 1260:49-54(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6 X CBA.
    Tissue: Liver.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Amnion, Embryo, Heart, Kidney and Visual cortex.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].

Entry informationi

Entry nameiFDFT_MOUSE
AccessioniPrimary (citable) accession number: P53798
Secondary accession number(s): Q8BPF5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: September 3, 2014
This is version 119 of the entry and version 2 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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