ERG11_ARATH
ID ERG11_ARATH Reviewed; 516 AA.
AC O65404;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Squalene epoxidase 5;
DE Short=AtSQE5;
DE EC=1.14.14.17 {ECO:0000250|UniProtKB:Q9SM02};
DE AltName: Full=Squalene monooxygenase 1,1;
DE Short=SE 1,1;
GN Name=SQE5; Synonyms=SQP1,1; OrderedLocusNames=At5g24150; ORFNames=K12G2.2;
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-516.
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 [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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O65404-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, leaves, stems and
CC inflorescences. Detected in siliques. {ECO:0000269|PubMed:17426032}.
CC -!- MISCELLANEOUS: SEQ4 or SEQ5 are unable to complement seq1 mutants.
CC {ECO:0000305|PubMed:17426032}.
CC -!- SIMILARITY: Belongs to the squalene monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; AB016883; BAB08406.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93262.1; -; Genomic_DNA.
DR EMBL; AJ005930; CAA06772.1; -; mRNA.
DR PIR; T51365; T51365.
DR RefSeq; NP_197803.1; NM_122320.4. [O65404-1]
DR AlphaFoldDB; O65404; -.
DR SMR; O65404; -.
DR STRING; 3702.AT5G24150.1; -.
DR PaxDb; O65404; -.
DR PRIDE; O65404; -.
DR ProteomicsDB; 220571; -. [O65404-1]
DR EnsemblPlants; AT5G24150.1; AT5G24150.1; AT5G24150. [O65404-1]
DR GeneID; 832480; -.
DR Gramene; AT5G24150.1; AT5G24150.1; AT5G24150. [O65404-1]
DR KEGG; ath:AT5G24150; -.
DR Araport; AT5G24150; -.
DR TAIR; locus:2151857; AT5G24150.
DR eggNOG; KOG1298; Eukaryota.
DR HOGENOM; CLU_026390_1_0_1; -.
DR InParanoid; O65404; -.
DR OMA; FMEVFLW; -.
DR PhylomeDB; O65404; -.
DR BioCyc; ARA:AT5G24150-MON; -.
DR UniPathway; UPA00767; UER00752.
DR PRO; PR:O65404; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; O65404; baseline and differential.
DR Genevisible; O65404; 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; ISS:TAIR.
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 Alternative splicing; FAD; Flavoprotein; Membrane; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..516
FT /note="Squalene epoxidase 5"
FT /id="PRO_0000209841"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 446..466
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 335
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT BINDING 348
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
SQ SEQUENCE 516 AA; 56606 MW; 95613C5C207F46A6 CRC64;
MAFTNVCLWT LLAFMLTWTV FYVTNRGKKA TQLADAVVEE REDGATDVII VGAGVGGSAL
AYALAKDGRR VHVIERDLRE PERIMGEFMQ PGGRLMLSKL GLEDCLEGID AQKATGMTVY
KDGKEAVASF PVDNNNFPFD PSARSFHNGR FVQRLRQKAS SLPNVRLEEG TVKSLIEEKG
VIKGVTYKNS AGEETTALAP LTVVCDGCYS NLRRSLNDNN AEVLSYQVGF ISKNCQLEEP
EKLKLIMSKP SFTMLYQISS TDVRCVFEVL PNNIPSISNG EMATFVKNTI APQVPLKLRK
IFLKGIDEGE HIKAMPTKKM TATLSEKKGV ILLGDAFNMR HPAIASGMMV LLSDILILRR
LLQPLSNLGN AQKISQVIKS FYDIRKPMSA TVNTLGNAFS QVLVASTDEA KEAMRQGCYD
YLSSGGFRTS GMMALLGGMN PRPISLIYHL CAITLSSIGH LLSPFPSPLR IWHSLRLFGL
AMKMLVPHLK AEGVSQMLFP VNAAAYSKSY MAATAL
