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P53798 (FDFT_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
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
Synonyms:Erg9
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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.

Sequence similarities

Belongs to the phytoene/squalene synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 416416Squalene synthase
PRO_0000067444

Regions

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

Experimental info

Sequence conflict1491R → Q in BAA06102. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P53798 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 12C63625DD4FF92B

FASTA41648,154
        10         20         30         40         50         60 
MEFVKCLGHP EEFYNLLRFR MGGRRNFIPK MDQDSLSSSL KTCYKYLNQT SRSFAAVIQA 

        70         80         90        100        110        120 
LDGDIRHAIC VFYLVLRALD TVEDDMSISV EKKIPLLCNF HTFLYDPEWR FTESKEKDRQ 

       130        140        150        160        170        180 
VLEDFPTISL EFRNLAEKYQ TVIDDICHRM GCGMAEFVDK DVTSKQDWDK YCHYVAGLVG 

       190        200        210        220        230        240 
IGLSRLFSAS EFEDPIVGED IECANSMGLF LQKTNIIRDY LEDQQEGRKF WPQEVWGRYI 

       250        260        270        280        290        300 
KKLEDFAKPE NVDVAVQCLN ELITNTLQHI PDVLTYLSRL RNQSVFNFCA IPQVMAIATL 

       310        320        330        340        350        360 
AACYNNQQVF KGVVKIRKGQ AVTLMMDATN MPAVKAIIYQ YIEEIYHRIP NSDPSSSKTK 

       370        380        390        400        410 
QVISKIRTQN LPNCQLISRS HYSPIYLSFI MLLAALSWQY LSTLSQVTED YVQREH

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00134836.
PIRS52075.
RefSeqNP_034321.2. NM_010191.2.
UniGeneMm.474432.

3D structure databases

ProteinModelPortalP53798.
SMRP53798. Positions 35-369.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000055313.

PTM databases

PhosphoSiteP53798.

Proteomic databases

PaxDbP53798.
PRIDEP53798.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000054963; ENSMUSP00000055313; ENSMUSG00000021273.
GeneID14137.
KEGGmmu:14137.
UCSCuc007uhi.2. mouse.

Organism-specific databases

CTD2222.
MGIMGI:102706. Fdft1.

Phylogenomic databases

eggNOGCOG1562.
GeneTreeENSGT00390000016034.
HOGENOMHOG000186940.
HOVERGENHBG002370.
InParanoidQ8BPF5.
KOK00801.
OMAELRHAVC.
OrthoDBEOG4QVCC2.

Enzyme and pathway databases

UniPathwayUPA00767; UER00751.

Gene expression databases

BgeeP53798.
CleanExMM_FDFT1.
GenevestigatorP53798.
GermOnlineENSMUSG00000021273. Mus musculus.

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. Terpenoid_synth. 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

ChEMBLCHEMBL4778.
NextBio285250.
SOURCESearch...

Entry information

Entry nameFDFT_MOUSE
AccessionPrimary (citable) accession number: P53798
Secondary accession number(s): Q8BPF5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: May 29, 2013
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents