Squalene synthetase - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P37268 (FDFT_HUMAN)

Last modified November 25, 2008. Version 92. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Squalene synthetase
      Short name=SQS
      Short name=SS
    EC=2.5.1.21
Alternative name(s):
    Farnesyl-diphosphate farnesyltransferase
    FPP:FPP farnesyltransferase

Gene names

Name:

FDFT1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	417 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Catalytic activity	2 farnesyl diphosphate = diphosphate + presqualene diphosphate. Presqualene diphosphate + NAD(P)H = squalene + diphosphate + NAD(P)(+).
Cofactor	Magnesium.
Pathway	Terpene metabolism; lanosterol biosynthesis; lanosterol from farnesyl-PP: step 1/3.
Subunit structure	Monomer By similarity.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence similarities	Belongs to the phytoene/squalene synthetase family.

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Ontologies

Keywords
Biological process	Cholesterol biosynthesis Isoprene biosynthesis Lipid synthesis Steroid biosynthesis Sterol biosynthesis
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Polymorphism
Domain	Transmembrane
Ligand	Magnesium NADP
Molecular function	Oxidoreductase Transferase
Technical term	3D-structure Multifunctional enzyme
Gene Ontology (GO)
Biological process	cholesterol biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW isoprenoid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum membrane Ref.6 Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Ref.1 Traceable author statement. Source: ProtInc
Molecular function	farnesyl-diphosphate farnesyltransferase activity Ref.6 Inferred from electronic annotation. Source: InterPro magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
RUVBL1	Q9Y265	1	EBI-714550,EBI-353675

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 417

417

Squalene synthetase

PRO_0000067443

Regions

Transmembrane

284 – 304

Potential

Transmembrane

384 – 404

Potential

Natural variations

Natural variant

K → R: dbSNP rs11549147.

VAR_011786

Natural variant

392

L → P: dbSNP rs1804473.

VAR_011787

Experimental info

Sequence conflict

353

D → N in AAB33404. Ref.4

Sequence conflict

402

T → A in CAA48896. Ref.3

Secondary structure

417

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P37268-1 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: D36CBC8382F827EC
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FASTA

417

48,115

        10         20         30         40         50         60 
MEFVKCLGHP EEFYNLVRFR IGGKRKVMPK MDQDSLSSSL KTCYKYLNQT SRSFAAVIQA 

        70         80         90        100        110        120 
LDGEMRNAVC IFYLVLRALD TLEDDMTISV EKKVPLLHNF HSFLYQPDWR FMESKEKDRQ 

       130        140        150        160        170        180 
VLEDFPTISL EFRNLAEKYQ TVIADICRRM GIGMAEFLDK HVTSEQEWDK YCHYVAGLVG 

       190        200        210        220        230        240 
IGLSRLFSAS EFEDPLVGED TERANSMGLF LQKTNIIRDY LEDQQGGREF WPQEVWSRYV 

       250        260        270        280        290        300 
KKLGDFAKPE NIDLAVQCLN ELITNALHHI PDVITYLSRL RNQSVFNFCA IPQVMAIATL 

       310        320        330        340        350        360 
AACYNNQQVF KGAVKIRKGQ AVTLMMDATN MPAVKAIIYQ YMEEIYHRIP DSDPSSSKTR 

       370        380        390        400        410 
QIISTIRTQN LPNCQLISRS HYSPIYLSFV MLLAALSWQY LTTLSQVTED YVQTGEH

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Conservation between human and fungal squalene synthetases: similarities in structure, function, and regulation." Robinson G.W., Tsay Y.H., Kienzle B.K., Smith-Monroy C.A., Bishop R.W. Mol. Cell. Biol. 13:2706-2717(1993) [PubMed: 8474436] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Transcriptional regulation by lovastatin and 25-hydroxycholesterol in HepG2 cells and molecular cloning and expression of the cDNA for the human hepatic squalene synthase." Jiang G., McKenzie T.L., Conrad D.G., Shechter I. J. Biol. Chem. 268:12818-12824(1993) [PubMed: 7685352] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[3]	"Cloning, expression and characterisation of the cDNA encoding human hepatic squalene synthase, and its relationship to phytoene synthase." Summers C., Karst F., Charles A.D. Gene 136:185-192(1993) [PubMed: 8294001] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[4]	"Expression, purification, and characterization of the human squalene synthase: use of yeast and baculoviral systems." Soltis D.A., McMahon G., Caplan S.L., Dudas D.A., Chamberlin H.A., Vattay A., Dottavio D., Rucker M.L., Engstrom R.G., Cornell-Kennon S.A. Arch. Biochem. Biophys. 316:713-723(1995) [PubMed: 7864626] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[5]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-45. Tissue: Lung, Muscle and Urinary bladder.
[6]	"Crystal structure of human squalene synthase. A key enzyme in cholesterol biosynthesis." Pandit J., Danley D.E., Schulte G.K., Mazzalupo S., Pauly T.A., Hayward C.M., Hamanaka E.S., Thompson J.F., Harwood H.J. Jr. J. Biol. Chem. 275:30610-30617(2000) [PubMed: 10896663] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 39-370.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

L06070 mRNA. Translation: AAA60582.1.
L06105 mRNA. Translation: AAA36645.1.
X69141 mRNA. Translation: CAA48896.1.
S76822 mRNA. Translation: AAB33404.1.
BC003573 mRNA. Translation: AAH03573.1.
BC009251 mRNA. Translation: AAH09251.1.
BC029641 mRNA. Translation: AAH29641.1.

PIR

A45998.
I38245.
I52090.

RefSeq

NP_004453.3.

UniGene

Hs.593928

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EZF	X-ray	2.15	A/C	35-370	[»]
			B	31-370	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P37268.

PTM databases

PhosphoSite

P37268.

Proteomic databases

PeptideAtlas

P37268.

Genome annotation databases

Ensembl

ENSG00000079459. Homo sapiens. [Contig view]

GeneID

2222.

KEGG

hsa:2222.

Organism-specific databases

H-InvDB

HIX0007319.

HGNC

HGNC:3629. FDFT1.

HPA

HPA008874.

MIM

184420. gene.

PharmGKB

PA28073.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOGENOM

P37268.

HOVERGEN

P37268.

Enzyme and pathway databases

BioCyc

MetaCyc:ENSG00000079459-MON.

Reactome

REACT_602. Lipid and lipoprotein metabolism.

Gene expression databases

ArrayExpress

P37268.

CleanEx

HS_FDFT1.

GermOnline

ENSG00000079459. Homo sapiens.

Family and domain databases

InterPro

IPR002060. Squ/phyt_synthse.
IPR006449. Squal_synth.
IPR008949. Terpenoid_synth.
[Graphical view]

Gene3D

G3DSA:1.10.600.10. Terpenoid_synth. 1 hit.

Pfam

PF00494. SQS_PSY. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01559. squal_synth. 1 hit.

PROSITE

PS01044. SQUALEN_PHYTOEN_SYN_1. 1 hit.
PS01045. SQUALEN_PHYTOEN_SYN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

9013.

SOURCE

Search...

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Entry information

Entry name

FDFT_HUMAN

Accession

Primary (citable) accession number: P37268
Secondary accession number(s): Q96GT0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	November 25, 2008
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Natural variations

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents