ID MSMO1_MOUSE Reviewed; 293 AA. AC Q9CRA4; Q543V8; DT 22-FEB-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 04-NOV-2026, entry version 161. DE RecName: Full=Methylsterol monooxygenase 1; DE EC=1.14.18.9 {ECO:0000250|UniProtKB:O35532}; DE AltName: Full=C-4 methylsterol oxidase; DE AltName: Full=Sterol-C4-methyl oxidase; GN Name=Msmo1; Synonyms=Sc4mol; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; RC TISSUE=Amnion, Bone marrow, Cerebellum, Embryo, Liver, and Placenta; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, and Liver; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). CC -!- FUNCTION: Catalyzes the three-step monooxygenation required for the CC demethylation of 4,4-dimethyl and 4alpha-methylsterols, which can be CC subsequently metabolized to cholesterol. CC {ECO:0000250|UniProtKB:Q15800}. CC -!- CATALYTIC ACTIVITY: CC Reaction=4,4-dimethyl-5alpha-cholest-7-en-3beta-ol + 6 Fe(II)- CC [cytochrome b5] + 3 O2 + 5 H(+) = 4alpha-carboxy-4beta-methyl-5alpha- CC cholest-7-ene-3beta-ol + 6 Fe(III)-[cytochrome b5] + 4 H2O; CC Xref=Rhea:RHEA:55220, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:16455, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, CC ChEBI:CHEBI:58387; EC=1.14.18.9; CC Evidence={ECO:0000250|UniProtKB:O35532}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55221; CC Evidence={ECO:0000250|UniProtKB:O35532}; CC -!- CATALYTIC ACTIVITY: CC Reaction=4,4-dimethyl-5alpha-cholesta-8,24-dien-3beta-ol + 6 Fe(II)- CC [cytochrome b5] + 3 O2 + 5 H(+) = 4beta-methylzymosterol-4alpha- CC carboxylate + 6 Fe(III)-[cytochrome b5] + 4 H2O; CC Xref=Rhea:RHEA:55244, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:18364, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, CC ChEBI:CHEBI:64925; Evidence={ECO:0000250|UniProtKB:Q15800}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55245; CC Evidence={ECO:0000250|UniProtKB:Q15800}; CC -!- CATALYTIC ACTIVITY: CC Reaction=4alpha-methylzymosterol + 6 Fe(II)-[cytochrome b5] + 3 O2 + 5 CC H(+) = 4alpha-carboxyzymosterol + 6 Fe(III)-[cytochrome b5] + 4 H2O; CC Xref=Rhea:RHEA:47056, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, CC ChEBI:CHEBI:1949, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, CC ChEBI:CHEBI:143575; Evidence={ECO:0000250|UniProtKB:Q15800}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47057; CC Evidence={ECO:0000250|UniProtKB:Q15800}; CC -!- CATALYTIC ACTIVITY: CC Reaction=4alpha-methyl-5alpha-cholest-7-en-3beta-ol + 6 Fe(II)- CC [cytochrome b5] + 3 O2 + 5 H(+) = 4alpha-carboxy-5alpha-cholest-7-en- CC 3beta-ol + 6 Fe(III)-[cytochrome b5] + 4 H2O; Xref=Rhea:RHEA:62768, CC Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:18378, CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:145943; CC Evidence={ECO:0000250|UniProtKB:Q15800}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62769; CC Evidence={ECO:0000250|UniProtKB:Q15800}; CC -!- CATALYTIC ACTIVITY: CC Reaction=4,4-dimethyl-5alpha-cholest-8-en-3beta-ol + 6 Fe(II)- CC [cytochrome b5] + 3 O2 + 5 H(+) = 4alpha-carboxy-4beta-methyl-5alpha- CC cholest-8-en-3beta-ol + 6 Fe(III)-[cytochrome b5] + 4 H2O; CC Xref=Rhea:RHEA:62776, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:87044, CC ChEBI:CHEBI:87047; Evidence={ECO:0000250|UniProtKB:Q15800}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62777; CC Evidence={ECO:0000250|UniProtKB:Q15800}; CC -!- CATALYTIC ACTIVITY: CC Reaction=4alpha-methyl-5alpha-cholest-8-en-3beta-ol + 6 Fe(II)- CC [cytochrome b5] + 3 O2 + 5 H(+) = 4alpha-carboxy-5alpha-cholest-8- CC ene-3beta-ol + 6 Fe(III)-[cytochrome b5] + 4 H2O; CC Xref=Rhea:RHEA:62780, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:87051, CC ChEBI:CHEBI:87055; Evidence={ECO:0000250|UniProtKB:Q15800}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62781; CC Evidence={ECO:0000250|UniProtKB:Q15800}; CC -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; CC Evidence={ECO:0000250|UniProtKB:Q15800}; CC -!- PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol from CC lanosterol: step 3/6. {ECO:0000250|UniProtKB:Q15800}. CC -!- PATHWAY: Steroid biosynthesis; cholesterol biosynthesis. CC {ECO:0000250|UniProtKB:Q15800}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000250|UniProtKB:Q15800}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:Q15800}. CC -!- DOMAIN: The histidine box domains may contain the active site and/or be CC involved in metal ion binding. CC -!- PTM: Ubiquitinated by MARCHF6, leading to proteasomal degradation. CC {ECO:0000250|UniProtKB:Q15800}. CC -!- SIMILARITY: Belongs to the sterol desaturase family. {ECO:0000305}. 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; AK005090; BAB23811.1; -; mRNA. DR EMBL; AK005441; BAB24035.1; -; mRNA. DR EMBL; AK045059; BAC32201.1; -; mRNA. DR EMBL; AK146684; BAE27358.1; -; mRNA. DR EMBL; AK151135; BAE30143.1; -; mRNA. DR EMBL; AK169017; BAE40814.1; -; mRNA. DR EMBL; BC006802; AAH06802.1; -; mRNA. DR CCDS; CCDS22328.1; -. DR RefSeq; NP_079712.1; NM_025436.3. DR RefSeq; XP_036010125.1; XM_036154232.1. DR AlphaFoldDB; Q9CRA4; -. DR SMR; Q9CRA4; -. DR BioGRID; 211315; 3. DR FunCoup; Q9CRA4; 360. DR STRING; 10090.ENSMUSP00000034015; -. DR iPTMnet; Q9CRA4; -. DR PhosphoSitePlus; Q9CRA4; -. DR SwissPalm; Q9CRA4; -. DR jPOST; Q9CRA4; -. DR PaxDb; 10090-ENSMUSP00000034015; -. DR PeptideAtlas; Q9CRA4; -. DR ProteomicsDB; 290101; -. DR Pumba; Q9CRA4; -. DR Antibodypedia; 28315; 138 antibodies from 22 providers. DR DNASU; 66234; -. DR Ensembl; ENSMUST00000034015.11; ENSMUSP00000034015.5; ENSMUSG00000031604.11. DR GeneID; 66234; -. DR KEGG; mmu:66234; -. DR UCSC; uc009lux.1; mouse. DR AGR; MGI:1913484; -. DR CTD; 6307; -. DR MGI; MGI:1913484; Msmo1. DR VEuPathDB; HostDB:ENSMUSG00000031604; -. DR eggNOG; KOG0873; Eukaryota. DR GeneTree; ENSGT00940000158012; -. DR HOGENOM; CLU_047036_5_2_1; -. DR InParanoid; Q9CRA4; -. DR OMA; AADQWKC; -. DR OrthoDB; 1658724at2759; -. DR PhylomeDB; Q9CRA4; -. DR Reactome; R-MMU-6807047; Cholesterol biosynthesis via desmosterol (Bloch pathway). DR UniPathway; UPA00063; -. DR UniPathway; UPA00770; UER00756. DR BioGRID-ORCS; 66234; 9 hits in 79 CRISPR screens. DR PRO; PR:Q9CRA4; -. DR Proteomes; UP000000589; Chromosome 8. DR RNAct; Q9CRA4; protein. DR Bgee; ENSMUSG00000031604; Expressed in tail skin and 285 other cell types or tissues. DR ExpressionAtlas; Q9CRA4; baseline and differential. DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB. DR GO; GO:0000254; F:C-4 methylsterol oxidase activity; IMP:MGI. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0006695; P:cholesterol biosynthetic process; IMP:MGI. DR GO; GO:0036197; P:zymosterol biosynthetic process; IMP:MGI. DR InterPro; IPR006694; Fatty_acid_hydroxylase. DR InterPro; IPR050307; Sterol_desaturase-rel. DR PANTHER; PTHR11863; STEROL DESATURASE; 1. DR Pfam; PF04116; FA_hydroxylase; 1. PE 1: Evidence at protein level; KW Cholesterol biosynthesis; Cholesterol metabolism; Endoplasmic reticulum; KW Iron; Lipid biosynthesis; Lipid metabolism; Membrane; NAD; Oxidoreductase; KW Reference proteome; Steroid biosynthesis; Steroid metabolism; KW Sterol biosynthesis; Sterol metabolism; Transmembrane; Transmembrane helix; KW Ubl conjugation. FT CHAIN 1..293 FT /note="Methylsterol monooxygenase 1" FT /id="PRO_0000117034" FT TRANSMEM 55..75 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 100..120 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 199..219 FT /note="Helical" FT /evidence="ECO:0000255" FT DOMAIN 144..274 FT /note="Fatty acid hydroxylase" FT /evidence="ECO:0000255" FT MOTIF 157..161 FT /note="Histidine box-1" FT MOTIF 170..174 FT /note="Histidine box-2" FT MOTIF 249..255 FT /note="Histidine box-3" SQ SEQUENCE 293 AA; 34772 MW; 0A275DE7B5D4DB52 CRC64; MATNKSVGVF SSASLAVEYV DSLLPENPLQ EPFKNAWVYM LDNYTKFQIA TWGSLIVHEA IYFLFSLPGF LFQFIPYMRK YKIQKDKPET FEGQWKCLKK ILFNHFFIQL PLICGTYYFT EFFNIPYDWE RMPRWYLTLA RCLGCAVIED TWHYFLHRLL HHKRIYKYIH KVHHEFQAPF GIEAEYAHPL ETLILGTGFF IGIVLLCDHV ILLWAWVTIR LLETIDVHSG YDIPLNPLNL VPFYTGARHH DFHHMNFIGN YASTFTWWDK LFGTDAQYHA YIEKSKKLGK KSD //