ERG12_ARATH
ID ERG12_ARATH Reviewed; 517 AA.
AC O65402;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Squalene epoxidase 6;
DE Short=AtSQE6;
DE EC=1.14.14.17 {ECO:0000250|UniProtKB:Q9SM02};
DE AltName: Full=Squalene monooxygenase 1,2;
DE Short=SE 1,2;
GN Name=SQE6; Synonyms=SQP1,2; OrderedLocusNames=At5g24160; ORFNames=K12G2.4;
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].
RC STRAIN=cv. Columbia;
RX PubMed=10350086; DOI=10.1023/a:1006172120929;
RA Schafer U.A., Reed D.W., Hunter D.G., Yao K., Weninger A.M., Tsang E.W.T.,
RA Reaney M.J.T., MacKenzie S.L., Covello P.S.;
RT "An example of intron junctional sliding in the gene families encoding
RT squalene monooxygenase homologues in Arabidopsis thaliana and Brassica
RT napus.";
RL Plant Mol. Biol. 39:721-728(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
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 IDENTIFICATION, TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=17426032; DOI=10.1074/jbc.m611831200;
RA Rasbery J.M., Shan H., LeClair R.J., Norman M., Matsuda S.P., Bartel B.;
RT "Arabidopsis thaliana squalene epoxidase 1 is essential for root and seed
RT development.";
RL J. Biol. Chem. 282:17002-17013(2007).
CC -!- FUNCTION: Catalyzes the stereospecific oxidation of squalene to (S)-
CC 2,3-epoxysqualene, and is considered to be a rate-limiting enzyme in
CC steroid biosynthesis. {ECO:0000250|UniProtKB:Q9SM02}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + reduced [NADPH--hemoprotein reductase] + squalene = (S)-
CC 2,3-epoxysqualene + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:25282, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:15440, ChEBI:CHEBI:15441, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210; EC=1.14.14.17;
CC Evidence={ECO:0000250|UniProtKB:Q9SM02};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q14534};
CC -!- PATHWAY: Terpene metabolism; lanosterol biosynthesis; lanosterol from
CC farnesyl diphosphate: step 2/3.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, leaves, stems,
CC inflorescences and siliques. {ECO:0000269|PubMed:17426032}.
CC -!- SIMILARITY: Belongs to the squalene monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; AJ005927; CAA06769.1; -; mRNA.
DR EMBL; AB016883; BAB08407.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93265.1; -; Genomic_DNA.
DR PIR; T51363; T51363.
DR RefSeq; NP_197804.1; NM_122321.5.
DR AlphaFoldDB; O65402; -.
DR SMR; O65402; -.
DR STRING; 3702.AT5G24160.1; -.
DR PaxDb; O65402; -.
DR PRIDE; O65402; -.
DR ProteomicsDB; 220572; -.
DR EnsemblPlants; AT5G24160.1; AT5G24160.1; AT5G24160.
DR GeneID; 832482; -.
DR Gramene; AT5G24160.1; AT5G24160.1; AT5G24160.
DR KEGG; ath:AT5G24160; -.
DR Araport; AT5G24160; -.
DR TAIR; locus:2151832; AT5G24160.
DR eggNOG; KOG1298; Eukaryota.
DR HOGENOM; CLU_026390_1_0_1; -.
DR InParanoid; O65402; -.
DR OMA; MEIFPGN; -.
DR OrthoDB; 583514at2759; -.
DR PhylomeDB; O65402; -.
DR BioCyc; ARA:AT5G24160-MON; -.
DR UniPathway; UPA00767; UER00752.
DR PRO; PR:O65402; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; O65402; baseline and differential.
DR Genevisible; O65402; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004506; F:squalene monooxygenase activity; IBA:GO_Central.
DR GO; GO:0016126; P:sterol biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR013698; Squalene_epoxidase.
DR InterPro; IPR040125; Squalene_monox.
DR PANTHER; PTHR10835; PTHR10835; 1.
DR Pfam; PF08491; SE; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 2: Evidence at transcript level;
KW FAD; Flavoprotein; Membrane; Oxidoreductase; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..517
FT /note="Squalene epoxidase 6"
FT /id="PRO_0000209842"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 447..467
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 55..56
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT BINDING 75..76
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT BINDING 83
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT BINDING 88
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT BINDING 156
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT BINDING 172
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT BINDING 336
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT BINDING 349
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
SQ SEQUENCE 517 AA; 56890 MW; 311429D335B0AC27 CRC64;
MAFTHVCLWT LVAFVLTWTV FYLTNMKKKA TDLADTVAED QKDGAADVII VGAGVGGSAL
AYALAKDGRR VHVIERDMRE PERMMGEFMQ PGGRLMLSKL GLQDCLEDID AQKATGLAVY
KDGKEADAPF PVDNNNFSYE PSARSFHNGR FVQQLRRKAF SLSNVRLEEG TVKSLLEEKG
VVKGVTYKNK EGEETTALAP LTVVCDGCYS NLRRSLNDDN NAEIMSYIVG YISKNCRLEE
PEKLHLILSK PSFTMVYQIS STDVRCGFEV LPENFPSIAN GEMSTFMKNT IVPQVPPKLR
KIFLKGIDEG AHIKVVPAKR MTSTLSKKKG VIVLGDAFNM RHPVVASGMM VLLSDILILR
RLLQPLSNLG DANKVSEVIN SFYDIRKPMS ATVNTLGNAF SQVLIGSTDE AKEAMRQGVY
DYLCSGGFRT SGMMALLGGM NPRPLSLVYH LCAITLSSIG QLLSPFPSPL RIWHSLKLFG
LAMKMLVPNL KAEGVSQMLF PANAAAYHKS YMAATTL
