ERG15_ARATH
ID ERG15_ARATH Reviewed; 585 AA.
AC O81000;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Squalene epoxidase 2, mitochondrial;
DE Short=AtSQE2;
DE EC=1.14.14.17 {ECO:0000269|PubMed:17426032};
DE Flags: Precursor;
GN Name=SQE2; OrderedLocusNames=At2g22830; ORFNames=T20K9.4;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 IDENTIFICATION, FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, GENE
RP 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. Produces primarily oxidosqualene.
CC {ECO:0000269|PubMed:17426032}.
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:0000269|PubMed:17426032};
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: Mitochondrion membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed mainly in inflorescences. Detected in
CC seedlings, leaves, stems, and siliques. {ECO:0000269|PubMed:17426032}.
CC -!- SIMILARITY: Belongs to the squalene monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; AC004786; AAC32430.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07362.1; -; Genomic_DNA.
DR PIR; D84617; D84617.
DR RefSeq; NP_179868.1; NM_127848.4.
DR AlphaFoldDB; O81000; -.
DR SMR; O81000; -.
DR STRING; 3702.AT2G22830.1; -.
DR PaxDb; O81000; -.
DR PRIDE; O81000; -.
DR ProteomicsDB; 220574; -.
DR EnsemblPlants; AT2G22830.1; AT2G22830.1; AT2G22830.
DR GeneID; 816814; -.
DR Gramene; AT2G22830.1; AT2G22830.1; AT2G22830.
DR KEGG; ath:AT2G22830; -.
DR Araport; AT2G22830; -.
DR TAIR; locus:2059196; AT2G22830.
DR eggNOG; KOG1298; Eukaryota.
DR HOGENOM; CLU_026390_1_0_1; -.
DR InParanoid; O81000; -.
DR OMA; TYIRRWK; -.
DR OrthoDB; 583514at2759; -.
DR PhylomeDB; O81000; -.
DR BRENDA; 1.14.14.17; 399.
DR UniPathway; UPA00767; UER00752.
DR PRO; PR:O81000; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O81000; baseline and differential.
DR Genevisible; O81000; 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:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
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 1: Evidence at protein level;
KW FAD; Flavoprotein; Membrane; Mitochondrion; Oxidoreductase;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..45
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 46..585
FT /note="Squalene epoxidase 2, mitochondrial"
FT /id="PRO_0000422764"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 493..513
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 520..540
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 545..565
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 132..133
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT BINDING 152..153
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT BINDING 160
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT BINDING 231
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT BINDING 247
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT BINDING 409
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT BINDING 422
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
FT SITE 194
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000250|UniProtKB:Q14534"
SQ SEQUENCE 585 AA; 64792 MW; D2259095A99B8B3C CRC64;
MKPFVIRNLP RFQSTLRSSL LYTNHRPSSR FSLSTRRFTT GATYIRRWKA TAAQTLKLSA
VNSTVMMKPA KIALDQFIAS LFTFLLLYIL RRSSNKNKKN RGLVVSQNDT VSKNLETEVD
SGTDVIIVGA GVAGSALAHT LGKEGRRVHV IERDFSEQDR IVGELLQPGG YLKLIELGLE
DCVKKIDAQR VLGYVLFKDG KHTKLAYPLE TFDSDVAGRS FHNGRFVQRM REKALTLSNV
RLEQGTVTSL LEEHGTIKGV RYRTKEGNEF RSFAPLTIVC DGCFSNLRRS LCKPKVDVPS
TFVGLVLENC ELPFANHGHV VLGDPSPILM YPISSSEVRC LVDVPGQKLP PIANGEMAKY
LKTRVAPQVP TKVREAFITA VEKGNIRTMP NRSMPADPIP TPGALLLGDA FNMRHPLTGG
GMTVALADIV VLRDLLRPIR NLNDKEALSK YIESFYTLRK PVASTINTLA DALYKVFLAS
SDEARTEMRE ACFDYLSLGG VFSSGPVALL SGLNPRPLSL VLHFFAVAIY AVCRLMLPFP
SIESFWLGAR IISSASSIIF PIIKAEGVRQ MFFPRTIPAI YRAPP
