ID FDFT1_ARATH Reviewed; 410 AA. AC P53799; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 24-JAN-2024, entry version 171. DE RecName: Full=Squalene synthase 1 {ECO:0000303|PubMed:9363754}; DE Short=SQS 1 {ECO:0000303|PubMed:9363754}; DE Short=SS 1 {ECO:0000303|PubMed:9363754}; DE EC=2.5.1.21 {ECO:0000269|PubMed:18236008, ECO:0000269|PubMed:7892265}; DE AltName: Full=FPP:FPP farnesyltransferase 1 {ECO:0000305}; DE AltName: Full=Farnesyl-diphosphate farnesyltransferase 1 {ECO:0000305}; GN Name=SQS1 {ECO:0000303|PubMed:9363754}; OrderedLocusNames=At4g34640; GN ORFNames=T4L20.220; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], COFACTOR, CATALYTIC ACTIVITY, AND PATHWAY. RC STRAIN=cv. Columbia; RX PubMed=7892265; DOI=10.1073/pnas.92.6.2328; RA Nakashima T., Inoue T., Oka A., Nishino T., Osumi T., Hata S.; RT "Cloning, expression, and characterization of cDNAs encoding Arabidopsis RT thaliana squalene synthase."; RL Proc. Natl. Acad. Sci. U.S.A. 92:2328-2332(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC STRAIN=cv. Landsberg erecta; RX PubMed=9363754; DOI=10.1111/j.1432-1033.1997.00061.x; RA Kribii R., Arro M., Del Arco A., Gonzalez V., Balcells L., Delourme D., RA Ferrer A., Karst F., Boronat A.; RT "Cloning and characterization of the Arabidopsis thaliana SQS1 gene RT encoding squalene synthase -- involvement of the C-terminal region of the RT enzyme in the channeling of squalene through the sterol pathway."; RL Eur. J. Biochem. 249:61-69(1997). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Kribii R., Arro M., del Arco A., Gonzalez V., Balcells L.L., Delourme D., RA Ferrer A., Karst F., Boronat A.; RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Connolly E.L., Learned R.M.; RT "Isolation and characterization of squalene synthase from Arabidopsis RT thaliana."; RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=10617198; DOI=10.1038/47134; RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M., RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., RA Martienssen R., McCombie W.R.; RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."; RL Nature 402:769-777(1999). RN [6] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RX PubMed=27862469; DOI=10.1111/tpj.13415; RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S., RA Town C.D.; RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference RT genome."; RL Plant J. 89:789-804(2017). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., RA Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [8] RP MUTAGENESIS OF PHE-287, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, RP DEVELOPMENTAL STAGE, COFACTOR, AND CATALYTIC ACTIVITY. RX PubMed=18236008; DOI=10.1007/s11103-008-9299-3; RA Busquets A., Keim V., Closa M., del Arco A., Boronat A., Arro M., RA Ferrer A.; RT "Arabidopsis thaliana contains a single gene encoding squalene synthase."; RL Plant Mol. Biol. 67:25-36(2008). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). CC -!- CATALYTIC ACTIVITY: CC Reaction=2 (2E,6E)-farnesyl diphosphate + H(+) + NADPH = 2 diphosphate CC + NADP(+) + squalene; Xref=Rhea:RHEA:32295, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15440, ChEBI:CHEBI:33019, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349, ChEBI:CHEBI:175763; EC=2.5.1.21; CC Evidence={ECO:0000269|PubMed:18236008, ECO:0000269|PubMed:7892265}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2 (2E,6E)-farnesyl diphosphate + H(+) + NADH = 2 diphosphate + CC NAD(+) + squalene; Xref=Rhea:RHEA:32299, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15440, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945, ChEBI:CHEBI:175763; EC=2.5.1.21; CC Evidence={ECO:0000269|PubMed:18236008, ECO:0000269|PubMed:7892265}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:18236008, ECO:0000269|PubMed:7892265}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:18236008}; CC -!- PATHWAY: Terpene metabolism; lanosterol biosynthesis; lanosterol from CC farnesyl diphosphate: step 1/3. {ECO:0000269|PubMed:7892265}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:18236008}; Multi-pass membrane protein CC {ECO:0000255}. CC -!- TISSUE SPECIFICITY: Expressed in all tissues analyzed (seedlings, CC cotyledons, inflorescences, siliques, leaves, stems and roots). Highly CC expressed in roots and pollen. {ECO:0000269|PubMed:18236008, CC ECO:0000269|PubMed:9363754}. CC -!- DEVELOPMENTAL STAGE: First observed in very early stages of seedling CC development. Particularly expressed in the vascular tissues and the CC petioles. {ECO:0000269|PubMed:18236008}. CC -!- SIMILARITY: Belongs to the phytoene/squalene synthase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D29017; BAA06103.1; -; mRNA. DR EMBL; X86692; CAA60385.1; -; mRNA. DR EMBL; AF004560; AAB62242.1; -; Genomic_DNA. DR EMBL; U79159; AAD00296.1; -; mRNA. DR EMBL; AL023094; CAA18843.1; -; Genomic_DNA. DR EMBL; AL161585; CAB80181.1; -; Genomic_DNA. DR EMBL; CP002687; AEE86403.1; -; Genomic_DNA. DR EMBL; AY099868; AAM20719.1; -; mRNA. DR EMBL; BT003419; AAO30082.1; -; mRNA. DR PIR; S54251; S54251. DR RefSeq; NP_195190.1; NM_119630.4. DR AlphaFoldDB; P53799; -. DR SMR; P53799; -. DR BioGRID; 14898; 9. DR IntAct; P53799; 9. DR STRING; 3702.P53799; -. DR iPTMnet; P53799; -. DR PaxDb; 3702-AT4G34640-1; -. DR ProteomicsDB; 232076; -. DR EnsemblPlants; AT4G34640.1; AT4G34640.1; AT4G34640. DR GeneID; 829616; -. DR Gramene; AT4G34640.1; AT4G34640.1; AT4G34640. DR KEGG; ath:AT4G34640; -. DR Araport; AT4G34640; -. DR TAIR; AT4G34640; SQS1. DR eggNOG; KOG1459; Eukaryota. DR HOGENOM; CLU_031981_0_0_1; -. DR InParanoid; P53799; -. DR OMA; GEACQLM; -. DR OrthoDB; 5487739at2759; -. DR PhylomeDB; P53799; -. DR BioCyc; ARA:AT4G34640-MONOMER; -. DR BioCyc; MetaCyc:AT4G34640-MONOMER; -. DR BRENDA; 2.5.1.21; 399. DR UniPathway; UPA00767; UER00751. DR PRO; PR:P53799; -. DR Proteomes; UP000006548; Chromosome 4. DR ExpressionAtlas; P53799; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; HDA:TAIR. DR GO; GO:0004310; F:farnesyl-diphosphate farnesyltransferase activity; IDA:TAIR. DR GO; GO:0051996; F:squalene synthase activity; IDA:UniProtKB. DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0016126; P:sterol biosynthetic process; TAS:TAIR. DR CDD; cd00683; Trans_IPPS_HH; 1. DR Gene3D; 1.10.600.10; Farnesyl Diphosphate Synthase; 1. DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf. DR InterPro; IPR002060; Squ/phyt_synthse. DR InterPro; IPR006449; Squal_synth-like. DR InterPro; IPR019845; Squalene/phytoene_synthase_CS. DR InterPro; IPR044844; Trans_IPPS_euk-type. DR InterPro; IPR033904; Trans_IPPS_HH. DR NCBIfam; TIGR01559; squal_synth; 1. DR PANTHER; PTHR11626; FARNESYL-DIPHOSPHATE FARNESYLTRANSFERASE; 1. DR PANTHER; PTHR11626:SF2; SQUALENE SYNTHASE; 1. DR Pfam; PF00494; SQS_PSY; 1. DR SFLD; SFLDS00005; Isoprenoid_Synthase_Type_I; 1. DR SFLD; SFLDG01018; Squalene/Phytoene_Synthase_Lik; 1. DR SUPFAM; SSF48576; Terpenoid synthases; 1. DR PROSITE; PS01044; SQUALEN_PHYTOEN_SYN_1; 1. DR PROSITE; PS01045; SQUALEN_PHYTOEN_SYN_2; 1. DR Genevisible; P53799; AT. PE 1: Evidence at protein level; KW Acetylation; Endoplasmic reticulum; Isoprene biosynthesis; Magnesium; KW Membrane; Multifunctional enzyme; NADP; Reference proteome; Transferase; KW Transmembrane; Transmembrane helix. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22223895" FT CHAIN 2..410 FT /note="Squalene synthase 1" FT /id="PRO_0000067455" FT TRANSMEM 283..303 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 387..407 FT /note="Helical" FT /evidence="ECO:0000255" FT MOD_RES 2 FT /note="N-acetylglycine" FT /evidence="ECO:0007744|PubMed:22223895" FT MUTAGEN 287 FT /note="F->S: Drastic reduction of squalene synthase FT activity." FT /evidence="ECO:0000269|PubMed:18236008" SQ SEQUENCE 410 AA; 47142 MW; 6178DD9381A441ED CRC64; MGSLGTMLRY PDDIYPLLKM KRAIEKAEKQ IPPEPHWGFC YSMLHKVSRS FSLVIQQLNT ELRNAVCVFY LVLRALDTVE DDTSIPTDEK VPILIAFHRH IYDTDWHYSC GTKEYKILMD QFHHVSAAFL ELEKGYQEAI EEITRRMGAG MAKFICQEVE TVDDYDEYCH YVAGLVGLGL SKLFLAAGSE VLTPDWEAIS NSMGLFLQKT NIIRDYLEDI NEIPKSRMFW PREIWGKYAD KLEDLKYEEN TNKSVQCLNE MVTNALMHIE DCLKYMVSLR DPSIFRFCAI PQIMAIGTLA LCYNNEQVFR GVVKLRRGLT AKVIDRTKTM ADVYGAFYDF SCMLKTKVDK NDPNASKTLN RLEAVQKLCR DAGVLQNRKS YVNDKGQPNS VFIIMVVILL AIVFAYLRAN //