ID H3K2X4_9EURO Unreviewed; 415 AA. AC H3K2X4; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 10-FEB-2021, entry version 28. DE RecName: Full=Squalene monooxygenase {ECO:0000256|RuleBase:RU367121}; DE EC=1.14.14.17 {ECO:0000256|RuleBase:RU367121}; GN Name=erg1 {ECO:0000313|EMBL:BAL48859.1}; OS Trichophyton mentagrophytes. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton. OX NCBI_TaxID=523103 {ECO:0000313|EMBL:BAL48859.1}; RN [1] {ECO:0000313|EMBL:BAL48859.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TIMM2789 {ECO:0000313|EMBL:BAL48859.1}; RX PubMed=22610431; DOI=10.1128/AEM.00464-12; RA Iwata A., Alshahni M.M., Nishiyama Y., Makimura K., Abe S., Yamada T.; RT "Development of a tightly regulatable copper-mediated gene switch system in RT dermatophytes."; RL Appl. Environ. Microbiol. 78:5204-5211(2012). 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:0000256|ARBA:ARBA00002173, CC ECO:0000256|RuleBase:RU367121}. 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:0000256|RuleBase:RU367121}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|ARBA:ARBA00001974, CC ECO:0000256|RuleBase:RU367121}; CC -!- PATHWAY: Terpene metabolism; lanosterol biosynthesis; lanosterol from CC farnesyl diphosphate: step 2/3. {ECO:0000256|ARBA:ARBA00005018, CC ECO:0000256|RuleBase:RU367121}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000256|RuleBase:RU367121}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU367121}. Microsome membrane CC {ECO:0000256|ARBA:ARBA00004154}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004154}. CC -!- SIMILARITY: Belongs to the squalene monooxygenase family. CC {ECO:0000256|ARBA:ARBA00008802, ECO:0000256|RuleBase:RU367121}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB690298; BAL48859.1; -; Genomic_DNA. DR UniPathway; UPA00767; UER00752. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0004506; F:squalene monooxygenase activity; IEA:UniProtKB-EC. DR GO; GO:0016126; P:sterol biosynthetic process; IEA:InterPro. 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 3: Inferred from homology; KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU367121}; KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU367121}; KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, KW ECO:0000256|RuleBase:RU367121}; Microsome {ECO:0000256|ARBA:ARBA00022848}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU367121}. FT DOMAIN 40..70 FT /note="DAO" FT /evidence="ECO:0000259|Pfam:PF01266" FT DOMAIN 191..404 FT /note="SE" FT /evidence="ECO:0000259|Pfam:PF08491" FT REGION 1..31 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 415 AA; 45166 MW; D455371447E391B4 CRC64; MVVEAPPCPQ SGNGFANGSA KPKAYRDEAE RRRYEHHEAD VVIIGAGIAG CALAVALGNQ GRSVILLERS LKEPDRIVGE LLQPGGVRAL EQLGLRDCLE GIDAVRTYGY DVIYFGNGVK IPFPSDANDK ILEGRCFHHG RFIMRLREAA AANPNVTIVE TKAVSTIKST HTGDVLGVQC QTDGKQDFYF GPLTVVADGY ASTFRKEYLP IQPVAKSKFW GLELIDAKLP IPGHGHVVLG DFPPILIYQI GEHETRILID IPDNLPSASV ANGGVKGHMR NVVLPSLPEC IRPSFEAALE KGGFRSMPNS FLRPVTNRIP GLMFLGDSLN MRHPLTGGGM TVAFNDVVLL RNLLSPEAVP DLSDTKLVLK QLSKFHWQRK SLISVINILA QSLYSIFAAG GKHMFSLPLL LVSGY //