Fdft1
entrez
29580
canonical
uniprot
Q02769
canonical
ensembl
ENSRNOG00000021314
resolver
ensembl
ENSRNOG00065030182
resolver
ensp
ENSRNOP00000029808
resolver
ensp
ENSRNOP00065042871
resolver
enst
ENSRNOT00000032089
resolver
enst
ENSRNOT00065052092
resolver
genesymbol
Fdft1
resolver
uniprot_entry
FDFT_RAT
resolver
amino_acid_sequence
MEFVKCLGHPEEFYNLLRFRMGGRRNFIPKMDRNSLSNSLKTCYKYLDQTSRSFAAVIQALDGDIRHAVCVFYLILRAMDTVEDDMAISVEKKIPLLRNFHTFLYEPEWRFTESKEKHRVVLEDFPTISLEFRNLAEKYQTVIADICHRMGCGMAEFLNKDVTSKQDWDKYCHYVAGLVGIGLSRLFSASEFEDPIVGEDTECANSMGLFLQKTNIIRDYLEDQQEGRQFWPQEVWGKYVKKLEDFVKPENVDVAVKCLNELITNALQHIPDVITYLSRLRNQSVFNFCAIPQVMAIATLAACYNNHQVFKGVVKIRKGQAVTLMMDATNMPAVKAIIYQYIEEIYHRVPNSDPSASKAKQLISNIRTQSLPNCQLISRSHYSPIYLSFIMLLAALSWQYLSTLSQVTEDYVQREH
uniprot
proteins
disease_involvement
DISEASE: Note=Defects in Lss and Fdft1 are the cause of Shumiya cataract rat (SCR). This strain develop mature cataracts at around 11 weeks of age, exhibiting opacity from the perinuclear zone to the cortical intermediate layer. Cholesterol levels in cataractous lenses decreased 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. {ECO:0000269|PubMed:16440058}.
uniprot
proteins
ec_number
2.5.1.21
uniprot
proteins
function
FUNCTION: Catalyzes the condensation of 2 farnesyl pyrophosphate (FPP) moieties to form squalene (PubMed:9575210). Proceeds in two distinct steps. In the first half-reaction, two molecules of FPP react to form the stable presqualene diphosphate intermediate (PSQPP), with concomitant release of a proton and a molecule of inorganic diphosphate. In the second half-reaction, PSQPP undergoes heterolysis, isomerization, and reduction with NADPH or NADH to form squalene. It is the first committed enzyme of the sterol biosynthesis pathway (By similarity). {ECO:0000250|UniProtKB:P37268, ECO:0000269|PubMed:9575210}.
uniprot
proteins
mass_dalton
48106
uniprot
proteins
mutagenesis
MUTAGEN 171; /note="Y->F,S,W: Completely abolishes formation of PSPP or squalene from FPP."; /evidence="ECO:0000269|PubMed:9575210"; MUTAGEN 174; /note="Y->F,S,W: Has little effect on the total squalene synthase activity."; /evidence="ECO:0000269|PubMed:9575210"; MUTAGEN 185; /note="R->G: Does not affect squalene synthase activity."; /evidence="ECO:0000269|PubMed:9575210"; MUTAGEN 283; /note="Q->E,N: Retains partial activity of the first reaction. Retains partial activity of the second reaction."; /evidence="ECO:0000269|PubMed:9575210"; MUTAGEN 286; /note="F->D,R: Completely eliminates the activities of both the first and the second reactions."; /evidence="ECO:0000269|PubMed:9575210"; MUTAGEN 286; /note="F->Y,W,L: Retains partial activity of the first reaction. Retains partial activity of the second reaction."; /evidence="ECO:0000269|PubMed:9575210"; MUTAGEN 288; /note="F->D,R: Completely eliminates the activities of both the first and the second reactions."; /evidence="ECO:0000269|PubMed:9575210"; MUTAGEN 288; /note="F->L: Retains partial activity of the first reaction. Completely eliminates the activity of the second reaction."; /evidence="ECO:0000269|PubMed:9575210"; MUTAGEN 288; /note="F->Y,W,L: Retains partial activity of the first reaction. Retains partial activity of the second reaction."; /evidence="ECO:0000269|PubMed:9575210"; MUTAGEN 293; /note="Q->N,E: Retains partial activity of the first reaction. Retains partial activity of the second reaction."; /evidence="ECO:0000269|PubMed:9575210
uniprot
proteins
pathway_participation
PATHWAY: Terpene metabolism; lanosterol biosynthesis; lanosterol from farnesyl diphosphate: step 1/3. {ECO:0000305}.
uniprot
proteins
protein_family
Phytoene/squalene synthase family
uniprot
proteins
pubmed
1400448
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1569107
uniprot
proteins
pubmed
16440058
uniprot
proteins
pubmed
8509416
uniprot
proteins
pubmed
9575210
uniprot
proteins
sequence_length
416
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:8509416}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 284..304; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 384..404; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins