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P53799 (FDFT_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. 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

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:SQS1
Ordered Locus Names:At4g34640
ORF Names:T4L20.220
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length410 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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 By similarity.

Tissue specificity

Expressed in all tissues analyzed (inflorescences, leaves, stems and roots). Highly expressed in roots. Ref.2

Sequence similarities

Belongs to the phytoene/squalene synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 410409Squalene synthase
PRO_0000067455

Regions

Transmembrane283 – 30321Helical; Potential
Transmembrane387 – 40721Helical; Potential

Amino acid modifications

Modified residue21N-acetylglycine Ref.8

Sequences

Sequence LengthMass (Da)Tools
P53799 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 6178DD9381A441ED

FASTA41047,142
        10         20         30         40         50         60 
MGSLGTMLRY PDDIYPLLKM KRAIEKAEKQ IPPEPHWGFC YSMLHKVSRS FSLVIQQLNT 

        70         80         90        100        110        120 
ELRNAVCVFY LVLRALDTVE DDTSIPTDEK VPILIAFHRH IYDTDWHYSC GTKEYKILMD 

       130        140        150        160        170        180 
QFHHVSAAFL ELEKGYQEAI EEITRRMGAG MAKFICQEVE TVDDYDEYCH YVAGLVGLGL 

       190        200        210        220        230        240 
SKLFLAAGSE VLTPDWEAIS NSMGLFLQKT NIIRDYLEDI NEIPKSRMFW PREIWGKYAD 

       250        260        270        280        290        300 
KLEDLKYEEN TNKSVQCLNE MVTNALMHIE DCLKYMVSLR DPSIFRFCAI PQIMAIGTLA 

       310        320        330        340        350        360 
LCYNNEQVFR GVVKLRRGLT AKVIDRTKTM ADVYGAFYDF SCMLKTKVDK NDPNASKTLN 

       370        380        390        400        410 
RLEAVQKLCR DAGVLQNRKS YVNDKGQPNS VFIIMVVILL AIVFAYLRAN 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, expression, and characterization of cDNAs encoding Arabidopsis thaliana squalene synthase."
Nakashima T., Inoue T., Oka A., Nishino T., Osumi T., Hata S.
Proc. Natl. Acad. Sci. U.S.A. 92:2328-2332(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Columbia.
[2]"Cloning and characterization of the Arabidopsis thaliana SQS1 gene encoding squalene synthase -- involvement of the C-terminal region of the enzyme in the channeling of squalene through the sterol pathway."
Kribii R., Arro M., Del Arco A., Gonzalez V., Balcells L., Delourme D., Ferrer A., Karst F., Boronat A.
Eur. J. Biochem. 249:61-69(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Strain: cv. Landsberg erecta.
[3]Kribii R., Arro M., del Arco A., Gonzalez V., Balcells L.L., Delourme D., Ferrer A., Karst F., Boronat A.
Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Isolation and characterization of squalene synthase from Arabidopsis thaliana."
Connolly E.L., Learned R.M.
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. expand/collapse author list , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[6]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[7]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[8]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D29017 mRNA. Translation: BAA06103.1.
X86692 mRNA. Translation: CAA60385.1.
AF004560 Genomic DNA. Translation: AAB62242.1.
U79159 mRNA. Translation: AAD00296.1.
AL023094 Genomic DNA. Translation: CAA18843.1.
AL161585 Genomic DNA. Translation: CAB80181.1.
CP002687 Genomic DNA. Translation: AEE86403.1.
AY099868 mRNA. Translation: AAM20719.1.
BT003419 mRNA. Translation: AAO30082.1.
PIRS54251.
RefSeqNP_195190.1. NM_119630.3.
UniGeneAt.20898.
At.67805.

3D structure databases

ProteinModelPortalP53799.
SMRP53799. Positions 40-358.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid14898. 3 interactions.
IntActP53799. 3 interactions.
STRING3702.AT4G34640.1-P.

Proteomic databases

PaxDbP53799.
PRIDEP53799.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G34640.1; AT4G34640.1; AT4G34640.
GeneID829616.
KEGGath:AT4G34640.

Organism-specific databases

TAIRAT4G34640.

Phylogenomic databases

eggNOGCOG1562.
HOGENOMHOG000186940.
InParanoidP53799.
KOK00801.
OMAEELEEYC.
PhylomeDBP53799.
ProtClustDBCLSN2685914.

Enzyme and pathway databases

BioCycARA:AT4G34640-MONOMER.
MetaCyc:AT4G34640-MONOMER.
UniPathwayUPA00767; UER00751.

Gene expression databases

GenevestigatorP53799.

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

PROP53799.

Entry information

Entry nameFDFT_ARATH
AccessionPrimary (citable) accession number: P53799
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names