ID H3K2X4_9EURO Unreviewed; 415 AA. AC H3K2X4; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 03-MAY-2023, entry version 36. DE RecName: Full=Squalene monooxygenase {ECO:0000256|ARBA:ARBA00012312, ECO:0000256|RuleBase:RU367121}; DE EC=1.14.14.17 {ECO:0000256|ARBA:ARBA00012312, ECO:0000256|RuleBase:RU367121}; GN Name=erg1 {ECO:0000313|EMBL:BAL48859.1}; GN Synonyms=SQLE {ECO:0000313|EMBL:QOH97037.1}; 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). RN [2] {ECO:0000313|EMBL:QOH97037.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TMH1 {ECO:0000313|EMBL:QOH97037.1}, TMH2 RC {ECO:0000313|EMBL:QOH97038.1}, TMH3 {ECO:0000313|EMBL:QOH97039.1}, and RC TMH4 {ECO:0000313|EMBL:QOH97040.1}; RX PubMed=32770418; RA Lagowski D., Gnat S., Nowakiewicz A., Osinska M., Dylag M.; RT "Intrinsic resistance to terbinafine among human and animal isolates of RT Trichophyton mentagrophytes related to amino acid substitution in the RT squalene epoxidase."; RL Infection 0:0-0(2020). RN [3] {ECO:0000313|EMBL:QOH97048.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TMS23 {ECO:0000313|EMBL:QOH97048.1}; RA Gnat S.; RT "cat-SQLE-T. mentagrophytes."; RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:QOH97047.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TMS27 {ECO:0000313|EMBL:QOH97047.1}; RA Gnat S.; RT "SQLE gene in dogs T. mentagrophytes."; RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000313|EMBL:QOH97045.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TMA16 {ECO:0000313|EMBL:QOH97045.1}, and TMS24 RC {ECO:0000313|EMBL:QOH97046.1}; RA Gnat S.; RT "SQLE gene in T. mentagrophytes from guinea pigs."; RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000313|EMBL:QOH97041.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TMA11 {ECO:0000313|EMBL:QOH97041.1}, TMS20 RC {ECO:0000313|EMBL:QOH97042.1}, TMS21 {ECO:0000313|EMBL:QOH97043.1}, RC and TMS22 {ECO:0000313|EMBL:QOH97044.1}; RA Gnat S.; RT "T. mentagrophytes silver fox squalene epoxidase."; RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the stereospecific oxidation of squalene to CC (S)-2,3-epoxysqualene, and is considered to be a rate-limiting enzyme CC in steroid biosynthesis. {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 -!- 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 EMBL; MT130516; QOH97037.1; -; Genomic_DNA. DR EMBL; MT130517; QOH97038.1; -; Genomic_DNA. DR EMBL; MT130518; QOH97039.1; -; Genomic_DNA. DR EMBL; MT130519; QOH97040.1; -; Genomic_DNA. DR EMBL; MT130520; QOH97041.1; -; Genomic_DNA. DR EMBL; MT130521; QOH97042.1; -; Genomic_DNA. DR EMBL; MT130522; QOH97043.1; -; Genomic_DNA. DR EMBL; MT130523; QOH97044.1; -; Genomic_DNA. DR EMBL; MT130524; QOH97045.1; -; Genomic_DNA. DR EMBL; MT130525; QOH97046.1; -; Genomic_DNA. DR EMBL; MT130526; QOH97047.1; -; Genomic_DNA. DR EMBL; MT130527; QOH97048.1; -; Genomic_DNA. DR AlphaFoldDB; H3K2X4; -. DR SMR; H3K2X4; -. DR UniPathway; UPA00767; UER00752. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule. DR GO; GO:0004506; F:squalene monooxygenase activity; IEA:UniProtKB-UniRule. DR GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-UniRule. DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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; SQUALENE MONOOXYGENASE; 1. DR PANTHER; PTHR10835:SF0; SQUALENE MONOOXYGENASE; 1. DR Pfam; PF01266; DAO; 1. DR Pfam; PF08491; SE; 1. DR PRINTS; PR00420; RNGMNOXGNASE. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 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}; Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Microsome {ECO:0000256|ARBA:ARBA00022848}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU367121}. FT DOMAIN 40..70 FT /note="FAD dependent oxidoreductase" FT /evidence="ECO:0000259|Pfam:PF01266" FT DOMAIN 191..404 FT /note="Squalene epoxidase" 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 //