FDFT1_ARATH
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 03-AUG-2022, entry version 164.
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}.
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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.AT4G34640.1; -.
DR iPTMnet; P53799; -.
DR PaxDb; P53799; -.
DR PRIDE; P53799; -.
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; locus:2139514; AT4G34640.
DR eggNOG; KOG1459; Eukaryota.
DR HOGENOM; CLU_031981_0_0_1; -.
DR InParanoid; P53799; -.
DR OMA; RFWPKEI; -.
DR OrthoDB; 563702at2759; -.
DR PhylomeDB; P53799; -.
DR BioCyc; ARA:AT4G34640-MON; -.
DR BioCyc; MetaCyc:AT4G34640-MON; -.
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 Genevisible; P53799; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0045338; P:farnesyl diphosphate metabolic process; IBA:GO_Central.
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; -; 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 PANTHER; PTHR11626; PTHR11626; 1.
DR Pfam; PF00494; SQS_PSY; 1.
DR SFLD; SFLDG01018; Squalene/Phytoene_Synthase_Lik; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
DR TIGRFAMs; TIGR01559; squal_synth; 1.
DR PROSITE; PS01044; SQUALEN_PHYTOEN_SYN_1; 1.
DR PROSITE; PS01045; SQUALEN_PHYTOEN_SYN_2; 1.
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
