Search Results
Overview
| Uniprot ID | A0A5G2RCH3 |
|---|---|
| Protein Name | Squalene synthase |
| Gene Name | FDFT1 |
| Organism | Sus scrofa |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 27 | SSLKTCYKYLNQTSR |
Function
Catalyzes the condensation of 2 farnesyl pyrophosphate (FPP) moieties to form squalene. 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
Protein Sequence
10
ISSASPTAVC
20
VLCPQDSLSS
30
SLKTCYKYLN
40
QTSRSFAAVI
50
QALDGEMRHA
60
VCIFYLVLRA
70
LDTLEDDMTI
80
SIEKKIPLLH
90
NFHLHLYESD
100
WRFTESKEKD
110
RQVLEDFPTI
120
ALEFRNLAEK
130
YQVVIVDVCR
140
KMGFGMAEFL
150
NKHVTSEREW
160
DKYCHYVAGL
170
VGIGLSRLFS
180
ASELEDPLVG
190
EDTERANSMG
200
LFLQKTNIIR
210
DYLEDQQEGR
220
EFWPQEVWSK
230
YVKKLGDFAK
240
PENVDLAVQC
250
LNELVTSTLH
260
HIPDVITYLS
270
RLRNQSIFNF
280
CAIPQVMAIA
290
TLAACYNNQQ
300
VFKGVVKIRK
310
GQAVTLMMDA
320
TNMPAVKAII
330
HQYMEEIYHR
340
IPDSDPYSAK
350
TRQIISTIRT
360
QNLPNCQLIS
370
RSHYSPIYLS
380
FVMLLAALSW
390
QYLSTLSQVT
EDYVQTGEH
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005789 | endoplasmic reticulum membrane |
| Molecular Function | GO:0055056 | D-glucose transmembrane transporter activity |
| Molecular Function | GO:0046872 | metal ion binding |
| Molecular Function | GO:0051996 | squalene synthase [NAD(P)H] activity |
| Biological Process | GO:0006695 | cholesterol biosynthetic process |
| Biological Process | GO:0045338 | farnesyl diphosphate metabolic process |
Reference
[1] Fan S, Zhou R, Wen H, Ye H, Ma S et al.. Global profiling of protein lactylome in porcine granulosa cells.. J Ovarian Res 18(1):177. 2025 Aug 8. PMID: 40781717.