FDFT2_ARATH
ID FDFT2_ARATH Reviewed; 413 AA.
AC O65688; O23118;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Inactive squalene synthase 2 {ECO:0000303|PubMed:18236008};
GN Name=SQS2 {ECO:0000312|EMBL:AEE86404.1};
GN OrderedLocusNames=At4g34650 {ECO:0000312|Araport:AT4G34650};
GN ORFNames=T4L20.230 {ECO:0000312|EMBL:CAA18844.2};
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 [GENOMIC DNA].
RC STRAIN=cv. Columbia;
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 [2]
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 [3]
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 [4]
RP REVIEW.
RX PubMed=12777052; DOI=10.1023/a:1023005504702;
RA Lange B.M., Ghassemian M.;
RT "Genome organization in Arabidopsis thaliana: a survey for genes involved
RT in isoprenoid and chlorophyll metabolism.";
RL Plant Mol. Biol. 51:925-948(2003).
RN [5]
RP CAUTION, MUTAGENESIS OF SER-287, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
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).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P53799};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P53799};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P53799}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in hypocotyls, leaves and
CC cotyledons, and, to a lower extent, in stems.
CC {ECO:0000269|PubMed:18236008}.
CC -!- DEVELOPMENTAL STAGE: Primarily detected in the vascular tissue of leaf
CC and cotyledon petioles, and the hypocotyl of one week-old seedlings.
CC {ECO:0000269|PubMed:18236008}.
CC -!- SIMILARITY: Belongs to the phytoene/squalene synthase family.
CC {ECO:0000305}.
CC -!- CAUTION: Does not show squalene synthase activity.
CC {ECO:0000269|PubMed:18236008}.
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DR EMBL; AF004396; AAB61927.1; -; Genomic_DNA.
DR EMBL; AL023094; CAA18844.2; -; Genomic_DNA.
DR EMBL; AL161585; CAB80182.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86404.1; -; Genomic_DNA.
DR PIR; E85408; E85408.
DR PIR; T05285; T05285.
DR PIR; T44924; T44924.
DR RefSeq; NP_195191.2; NM_119631.3.
DR AlphaFoldDB; O65688; -.
DR SMR; O65688; -.
DR STRING; 3702.AT4G34650.1; -.
DR PaxDb; O65688; -.
DR PRIDE; O65688; -.
DR ProteomicsDB; 230505; -.
DR EnsemblPlants; AT4G34650.1; AT4G34650.1; AT4G34650.
DR GeneID; 829617; -.
DR Gramene; AT4G34650.1; AT4G34650.1; AT4G34650.
DR KEGG; ath:AT4G34650; -.
DR Araport; AT4G34650; -.
DR TAIR; locus:2139534; AT4G34650.
DR eggNOG; KOG1459; Eukaryota.
DR HOGENOM; CLU_031981_0_0_1; -.
DR InParanoid; O65688; -.
DR OMA; KNDPNAM; -.
DR OrthoDB; 563702at2759; -.
DR PhylomeDB; O65688; -.
DR BioCyc; MetaCyc:AT4G34650-MON; -.
DR BRENDA; 2.5.1.21; 399.
DR PRO; PR:O65688; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O65688; baseline and differential.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004310; F:farnesyl-diphosphate farnesyltransferase activity; ISS:TAIR.
DR GO; GO:0045338; P:farnesyl diphosphate metabolic process; IBA:GO_Central.
DR GO; GO:0016126; P:sterol biosynthetic process; ISS: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; 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.
PE 1: Evidence at protein level;
KW Acetylation; Endoplasmic reticulum; Magnesium; Manganese; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P53799"
FT CHAIN 2..413
FT /note="Inactive squalene synthase 2"
FT /id="PRO_0000436937"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000250|UniProtKB:P53799"
FT MUTAGEN 287
FT /note="S->F: No squalene synthase activity."
FT /evidence="ECO:0000269|PubMed:18236008"
FT CONFLICT 300
FT /note="A -> T (in Ref. 1; AAB61927)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="L -> M (in Ref. 1; AAB61927)"
FT /evidence="ECO:0000305"
FT CONFLICT 368..374
FT /note="FCKENGG -> VCRENGV (in Ref. 1; AAB61927)"
FT /evidence="ECO:0000305"
FT CONFLICT 412
FT /note="C -> R (in Ref. 1; AAB61927)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 413 AA; 47183 MW; 6F461C41D3849C15 CRC64;
MGSLSTILRH PDELYPLLKL KLAITKAQKQ IPLEPHLAFC YSILHKVSKS FSLVIQQLGT
ELRNAVCVFY LILRALDTVE DDTSVPVEIK VPILIAFHRH IYDGDWHFSC GTKEYKLLMD
QFHHVSAAFL KLEKGYQEAI EDITKRMGAG MAKFICKEVE TIDDYDEYCH YAAGLVGLGL
SKIFIASELE ILTPDWKQIS NSTGLFLQKT NIIKDYLEDI NERPKSRMFW PREIWGKYVD
KLEDFKNEEK ATKAVQCLNE MVTNALNHVE DCLKSLASLR DPAIFQSCAI PQIVAIGTLA
LCYNNVQVFR GVVRLRRGLI AKVIDRTKTM DDVYGAFYDF SCMLQTKVDN NDPNAMKTLN
RLETIKKFCK ENGGLHKRKS YVNDETQSKA IFVVMFVLLL AIVVVYLKAN QCK
