ERG13_ARATH
ID ERG13_ARATH Reviewed; 516 AA.
AC O65403;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Squalene epoxidase 4;
DE Short=AtSQE4;
DE EC=1.14.14.17 {ECO:0000250|UniProtKB:Q9SM02};
DE AltName: Full=Squalene monooxygenase 2;
DE Short=SE 2;
GN Name=SQE4; Synonyms=SQP2; OrderedLocusNames=At5g24140; ORFNames=MLE8.6;
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=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
RN [3]
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 [4]
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 [5]
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 mainly in seedlings and inflorescences.
CC {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; AJ005929; CAA06771.1; -; mRNA.
DR EMBL; AB010696; BAB11574.1; -; Genomic_DNA.
DR EMBL; AB016883; BAB11574.1; JOINED; Genomic_DNA.
DR EMBL; CP002688; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; T51364; T51364.
DR AlphaFoldDB; O65403; -.
DR SMR; O65403; -.
DR STRING; 3702.AT5G24140.1; -.
DR PaxDb; O65403; -.
DR PRIDE; O65403; -.
DR EnsemblPlants; AT5G24140.1; AT5G24140.1; AT5G24140.
DR Gramene; AT5G24140.1; AT5G24140.1; AT5G24140.
DR Araport; AT5G24140; -.
DR TAIR; locus:2167423; AT5G24140.
DR eggNOG; KOG1298; Eukaryota.
DR HOGENOM; CLU_026390_1_0_1; -.
DR InParanoid; O65403; -.
DR PhylomeDB; O65403; -.
DR BioCyc; ARA:AT5G24140-MON; -.
DR BRENDA; 1.14.14.17; 399.
DR UniPathway; UPA00767; UER00752.
DR PRO; PR:O65403; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; O65403; baseline and differential.
DR Genevisible; O65403; 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; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR013698; Squalene_epoxidase.
DR InterPro; IPR040125; Squalene_monox.
DR PANTHER; PTHR10835; PTHR10835; 1.
DR Pfam; PF01266; DAO; 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..516
FT /note="Squalene epoxidase 4"
FT /id="PRO_0000209843"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 435..455
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 53..54
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT BINDING 73..74
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT BINDING 81
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT BINDING 153
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT BINDING 169
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; 57027 MW; D6B3BA803FC682A7 CRC64;
MTYAWLWTLL AFVLTWMVFH LIKMKKAATG DLEAEAEARR DGATDVIIVG AGVAGASLAY
ALAKDGRRVH VIERDLKEPQ RFMGELMQAG GRFMLAQLGL EDCLEDIDAQ EAKSLAIYKD
GKHATLPFPD DKSFPHEPVG RLLRNGRLVQ RLRQKAASLS NVQLEEGTVK SLIEEEGVVK
GVTYKNSAGE EITAFAPLTV VCDGCYSNLR RSLVDNTEEV LSYMVGYVTK NSRLEDPHSL
HLIFSKPLVC VIYQITSDEV RCVAEVPADS IPSISNGEMS TFLKKSMAPQ IPETGNLREI
FLKGIEEGLP EIKSTATKSM SSRLCDKRGV IVLGDAFNMR HPIIASGMMV ALSDICILRN
LLKPLPNLSN TKKVSDLVKS FYIIRKPMSA TVNTLASIFS QVLVATTDEA REGMRQGCFN
YLARGDFKTR GLMTILGGMN PHPLTLVLHL VAITLTSMGH LLSPFPSPRR FWHSLRILAW
ALQMLGAHLV DEGFKEMLIP TNAAAYRRNY IATTTV
