ID MSMO1_HUMAN Reviewed; 293 AA. AC Q15800; A8K8Q3; A8MYF6; D3DP32; Q32Q24; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 02-OCT-2024, entry version 198. DE RecName: Full=Methylsterol monooxygenase 1 {ECO:0000303|PubMed:23583456}; DE EC=1.14.18.9 {ECO:0000250|UniProtKB:O35532}; DE AltName: Full=C-4 methylsterol oxidase {ECO:0000303|PubMed:23583456}; DE AltName: Full=Sterol-C4-methyl oxidase {ECO:0000303|PubMed:21285510}; GN Name=MSMO1; Synonyms=DESP4, ERG25, SC4MOL; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND COFACTOR. RC TISSUE=Intestine; RX PubMed=8663358; DOI=10.1074/jbc.271.28.16927; RA Li L., Kaplan J.; RT "Characterization of yeast methyl sterol oxidase (ERG25) and identification RT of a human homologue."; RL J. Biol. Chem. 271:16927-16933(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Retina; RA Herrmann K.; RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Corpus callosum, and Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Eye; 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 [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [8] RP FUNCTION, AND PATHWAY. RX PubMed=23583456; DOI=10.1016/j.bcp.2013.03.021; RA Mazein A., Watterson S., Hsieh W.Y., Griffiths W.J., Ghazal P.; RT "A comprehensive machine-readable view of the mammalian cholesterol RT biosynthesis pathway."; RL Biochem. Pharmacol. 86:56-66(2013). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [10] RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY. RX PubMed=26114596; DOI=10.7554/elife.07999; RA Mitsche M.A., McDonald J.G., Hobbs H.H., Cohen J.C.; RT "Flux analysis of cholesterol biosynthesis in vivo reveals multiple tissue RT and cell-type specific pathways."; RL Elife 4:E07999-E07999(2015). RN [11] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=26038696; DOI=10.1002/prp2.120; RA Yasuda K., Iwanaga Y., Ogawa K., Mano H., Ueno S., Kimoto S., Ohta M., RA Kamakura M., Ikushiro S., Sakaki T.; RT "Human hepatic metabolism of the anti-osteoporosis drug eldecalcitol RT involves sterol C4-methyl oxidase."; RL Pharmacol. Res. Perspect. 3:e00120-e00120(2015). RN [12] RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY. RX PubMed=28673550; DOI=10.1016/j.ymgme.2017.06.013; RA Frisso G., Gelzo M., Procopio E., Sica C., Lenza M.P., Dello Russo A., RA Donati M.A., Salvatore F., Corso G.; RT "A rare case of sterol-C4-methyl oxidase deficiency in a young Italian RT male: Biochemical and molecular characterization."; RL Mol. Genet. Metab. 121:329-335(2017). RN [13] RP INVOLVEMENT IN MCCPD, VARIANTS MCCPD GLN-173 AND CYS-244, FUNCTION, RP CATALYTIC ACTIVITY, AND PATHWAY. RX PubMed=21285510; DOI=10.1172/jci42650; RA He M., Kratz L.E., Michel J.J., Vallejo A.N., Ferris L., Kelley R.I., RA Hoover J.J., Jukic D., Gibson K.M., Wolfe L.A., Ramachandran D., RA Zwick M.E., Vockley J.; RT "Mutations in the human SC4MOL gene encoding a methyl sterol oxidase cause RT psoriasiform dermatitis, microcephaly, and developmental delay."; RL J. Clin. Invest. 121:976-984(2011). RN [14] RP VARIANT MCCPD ARG-115. RX PubMed=24144731; DOI=10.1016/j.bbalip.2013.10.009; RA He M., Smith L.D., Chang R., Li X., Vockley J.; RT "The role of sterol-C4-methyl oxidase in epidermal biology."; RL Biochim. Biophys. Acta 1841:331-335(2014). 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 (PubMed:21285510, CC PubMed:23583456, PubMed:26114596, PubMed:28673550). Also involved in CC drug metabolism, as it can metabolize eldecalcitol (ED-71 or 1alpha,25- CC dihydroxy-2beta-(3-hydroxypropoxy)-cholecalciferol), a second- CC generation vitamin D analog, into 1alpha,2beta,25-trihydroxy vitamin CC D3; this reaction occurs via enzymatic hydroxylation and spontaneous O- CC dehydroxypropylation (PubMed:26038696). {ECO:0000269|PubMed:21285510, CC ECO:0000269|PubMed:26038696, ECO:0000269|PubMed:28673550, CC ECO:0000305|PubMed:23583456, ECO:0000305|PubMed:26114596}. CC -!- CATALYTIC ACTIVITY: CC Reaction=4,4-dimethyl-5alpha-cholest-7-en-3beta-ol + 6 Fe(II)- CC [cytochrome b5] + 5 H(+) + 3 O2 = 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] + 5 H(+) + 3 O2 = 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:0000269|PubMed:21285510, CC ECO:0000269|PubMed:28673550, ECO:0000305|PubMed:26114596}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55245; CC Evidence={ECO:0000269|PubMed:21285510, ECO:0000269|PubMed:28673550, CC ECO:0000305|PubMed:26114596}; CC -!- CATALYTIC ACTIVITY: CC Reaction=4alpha-methylzymosterol + 6 Fe(II)-[cytochrome b5] + 5 H(+) + CC 3 O2 = 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:0000305|PubMed:21285510, CC ECO:0000305|PubMed:26114596, ECO:0000305|PubMed:28673550}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47057; CC Evidence={ECO:0000305|PubMed:21285510, ECO:0000305|PubMed:26114596, CC ECO:0000305|PubMed:28673550}; CC -!- CATALYTIC ACTIVITY: CC Reaction=4alpha-methyl-5alpha-cholest-7-en-3beta-ol + 6 Fe(II)- CC [cytochrome b5] + 5 H(+) + 3 O2 = 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:0000269|PubMed:21285510, ECO:0000269|PubMed:28673550}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62769; CC Evidence={ECO:0000269|PubMed:21285510, ECO:0000269|PubMed:28673550}; CC -!- CATALYTIC ACTIVITY: CC Reaction=4,4-dimethyl-5alpha-cholest-8-en-3beta-ol + 6 Fe(II)- CC [cytochrome b5] + 5 H(+) + 3 O2 = 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:0000269|PubMed:21285510, CC ECO:0000269|PubMed:28673550}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62777; CC Evidence={ECO:0000269|PubMed:21285510, ECO:0000269|PubMed:28673550}; CC -!- CATALYTIC ACTIVITY: CC Reaction=4alpha-methyl-5alpha-cholest-8-en-3beta-ol + 6 Fe(II)- CC [cytochrome b5] + 5 H(+) + 3 O2 = 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:0000269|PubMed:21285510, CC ECO:0000269|PubMed:28673550}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62781; CC Evidence={ECO:0000269|PubMed:21285510, ECO:0000269|PubMed:28673550}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1alpha,25-dihydroxy-2beta-(3-hydroxypropoxy)-cholecalciferol + CC 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = 1alpha,25-dihydroxy-2beta- CC (1,3-dihydroxypropoxy)-cholecalciferol + 2 Fe(III)-[cytochrome b5] + CC H2O; Xref=Rhea:RHEA:62820, Rhea:RHEA-COMP:10438, Rhea:RHEA- CC COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:73927, CC ChEBI:CHEBI:146141; Evidence={ECO:0000269|PubMed:26038696}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62821; CC Evidence={ECO:0000269|PubMed:26038696}; CC -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; CC Evidence={ECO:0000305|PubMed:8663358}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=19.5 uM for 1alpha,25-dihydroxy-2beta-(3-hydroxypropoxy)- CC cholecalciferol {ECO:0000269|PubMed:26038696}; CC Vmax=19 pmol/min/mg enzyme with 1alpha,25-dihydroxy-2beta-(3- CC hydroxypropoxy)-cholecalciferol as substrate CC {ECO:0000269|PubMed:26038696}; CC -!- PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol from CC lanosterol: step 3/6. {ECO:0000305|PubMed:23583456, CC ECO:0000305|PubMed:26114596}. CC -!- PATHWAY: Steroid biosynthesis; cholesterol biosynthesis. CC {ECO:0000305|PubMed:21285510, ECO:0000305|PubMed:23583456, CC ECO:0000305|PubMed:26114596, ECO:0000305|PubMed:28673550}. CC -!- INTERACTION: CC Q15800; Q6NT55: CYP4F22; NbExp=3; IntAct=EBI-949102, EBI-17509525; CC Q15800; Q96LL9: DNAJC30; NbExp=3; IntAct=EBI-949102, EBI-8639143; CC Q15800; Q9UKR5: ERG28; NbExp=3; IntAct=EBI-949102, EBI-711490; CC Q15800; Q6ZVE7: GOLT1A; NbExp=3; IntAct=EBI-949102, EBI-17231387; CC Q15800; P09601: HMOX1; NbExp=3; IntAct=EBI-949102, EBI-2806151; CC Q15800; P50281: MMP14; NbExp=3; IntAct=EBI-949102, EBI-992788; CC Q15800; P0DN84: STRIT1; NbExp=3; IntAct=EBI-949102, EBI-12200293; CC Q15800; Q13277: STX3; NbExp=3; IntAct=EBI-949102, EBI-1394295; CC Q15800; P17152: TMEM11; NbExp=3; IntAct=EBI-949102, EBI-723946; CC Q15800; Q9NV12: TMEM140; NbExp=3; IntAct=EBI-949102, EBI-2844246; CC Q15800; Q9NWH2: TMEM242; NbExp=3; IntAct=EBI-949102, EBI-10315004; CC Q15800; Q6PI78: TMEM65; NbExp=3; IntAct=EBI-949102, EBI-6656213; CC Q15800; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-949102, EBI-2548832; CC Q15800; O95070: YIF1A; NbExp=3; IntAct=EBI-949102, EBI-2799703; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; CC Multi-pass membrane protein {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q15800-1; Sequence=Displayed; CC Name=2; CC IsoId=Q15800-2; Sequence=VSP_044585; CC -!- DOMAIN: The histidine box domains may contain the active site and/or be CC involved in metal ion binding. CC -!- DISEASE: Microcephaly, congenital cataract, and psoriasiform dermatitis CC (MCCPD) [MIM:616834]: An autosomal recessive inborn error of CC cholesterol metabolism characterized by accumulation of a large amount CC of methylsterols, particularly dimethylsterols, in affected CC individuals. Patients manifest psoriasiform dermatitis, arthralgias, CC congenital cataracts, microcephaly, and developmental delay. CC {ECO:0000269|PubMed:21285510, ECO:0000269|PubMed:24144731}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. 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; U60205; AAC50587.1; -; mRNA. DR EMBL; U93162; AAB81566.1; -; mRNA. DR EMBL; AK292418; BAF85107.1; -; mRNA. DR EMBL; AK295432; BAH12066.1; -; mRNA. DR EMBL; AC012504; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471056; EAX04820.1; -; Genomic_DNA. DR EMBL; CH471056; EAX04821.1; -; Genomic_DNA. DR EMBL; BC010653; AAH10653.1; -; mRNA. DR EMBL; BC107879; AAI07880.1; -; mRNA. DR CCDS; CCDS3809.1; -. [Q15800-1] DR CCDS; CCDS43280.1; -. [Q15800-2] DR RefSeq; NP_001017369.1; NM_001017369.2. [Q15800-2] DR RefSeq; NP_006736.1; NM_006745.4. [Q15800-1] DR RefSeq; XP_005263233.1; XM_005263176.2. [Q15800-1] DR AlphaFoldDB; Q15800; -. DR BioGRID; 112214; 108. DR IntAct; Q15800; 68. DR MINT; Q15800; -. DR STRING; 9606.ENSP00000261507; -. DR DrugBank; DB00157; NADH. DR SwissLipids; SLP:000001244; -. DR GlyGen; Q15800; 2 sites. DR iPTMnet; Q15800; -. DR PhosphoSitePlus; Q15800; -. DR SwissPalm; Q15800; -. DR BioMuta; MSMO1; -. DR DMDM; 2498340; -. DR jPOST; Q15800; -. DR MassIVE; Q15800; -. DR PaxDb; 9606-ENSP00000261507; -. DR PeptideAtlas; Q15800; -. DR ProteomicsDB; 2398; -. DR ProteomicsDB; 60767; -. [Q15800-1] DR Pumba; Q15800; -. DR Antibodypedia; 28315; 144 antibodies from 20 providers. DR DNASU; 6307; -. DR Ensembl; ENST00000261507.11; ENSP00000261507.6; ENSG00000052802.13. [Q15800-1] DR Ensembl; ENST00000393766.6; ENSP00000377361.2; ENSG00000052802.13. [Q15800-2] DR GeneID; 6307; -. DR KEGG; hsa:6307; -. DR MANE-Select; ENST00000261507.11; ENSP00000261507.6; NM_006745.5; NP_006736.1. DR UCSC; uc003ire.4; human. [Q15800-1] DR AGR; HGNC:10545; -. DR CTD; 6307; -. DR DisGeNET; 6307; -. DR GeneCards; MSMO1; -. DR HGNC; HGNC:10545; MSMO1. DR HPA; ENSG00000052802; Tissue enhanced (liver). DR MalaCards; MSMO1; -. DR MIM; 607545; gene. DR MIM; 616834; phenotype. DR neXtProt; NX_Q15800; -. DR OpenTargets; ENSG00000052802; -. DR Orphanet; 488168; Microcephaly-congenital cataract-psoriasiform dermatitis syndrome. DR PharmGKB; PA34955; -. DR VEuPathDB; HostDB:ENSG00000052802; -. DR eggNOG; KOG0873; Eukaryota. DR GeneTree; ENSGT00940000158012; -. DR HOGENOM; CLU_047036_5_3_1; -. DR InParanoid; Q15800; -. DR OMA; IHHEFQA; -. DR OrthoDB; 179215at2759; -. DR PhylomeDB; Q15800; -. DR TreeFam; TF354294; -. DR BioCyc; MetaCyc:HS00650-MONOMER; -. DR BRENDA; 1.14.18.9; 2681. DR PathwayCommons; Q15800; -. DR Reactome; R-HSA-191273; Cholesterol biosynthesis. DR SignaLink; Q15800; -. DR UniPathway; UPA00063; -. DR UniPathway; UPA00770; UER00756. DR BioGRID-ORCS; 6307; 31 hits in 1159 CRISPR screens. DR ChiTaRS; MSMO1; human. DR GenomeRNAi; 6307; -. DR Pharos; Q15800; Tbio. DR PRO; PR:Q15800; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; Q15800; protein. DR Bgee; ENSG00000052802; Expressed in adrenal tissue and 213 other cell types or tissues. DR ExpressionAtlas; Q15800; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central. DR GO; GO:0016020; C:membrane; TAS:ProtInc. DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc. DR GO; GO:0000254; F:C-4 methylsterol oxidase activity; IBA:GO_Central. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0006695; P:cholesterol biosynthetic process; TAS:Reactome. DR GO; GO:0006631; P:fatty acid metabolic process; TAS:ProtInc. DR GO; GO:0008202; P:steroid metabolic process; TAS:ProtInc. DR GO; GO:0016126; P:sterol biosynthetic process; IBA:GO_Central. DR InterPro; IPR006694; Fatty_acid_hydroxylase. DR InterPro; IPR050307; Sterol_Desaturase_Related. DR PANTHER; PTHR11863:SF226; LATHOSTEROL OXIDASE-RELATED; 1. DR PANTHER; PTHR11863; STEROL DESATURASE; 1. DR Pfam; PF04116; FA_hydroxylase; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cataract; Cholesterol biosynthesis; KW Cholesterol metabolism; Disease variant; Endoplasmic reticulum; Iron; KW Lipid biosynthesis; Lipid metabolism; Membrane; NAD; Oxidoreductase; KW Proteomics identification; Reference proteome; Steroid biosynthesis; KW Steroid metabolism; Sterol biosynthesis; Sterol metabolism; Transmembrane; KW Transmembrane helix. FT CHAIN 1..293 FT /note="Methylsterol monooxygenase 1" FT /id="PRO_0000117033" 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 145..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" FT VAR_SEQ 1..131 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044585" FT VARIANT 115 FT /note="G -> R (in MCCPD; uncertain significance; FT dbSNP:rs1310714454)" FT /evidence="ECO:0000269|PubMed:24144731" FT /id="VAR_076531" FT VARIANT 124 FT /note="N -> S (in dbSNP:rs34499452)" FT /id="VAR_048898" FT VARIANT 173 FT /note="H -> Q (in MCCPD; dbSNP:rs869025576)" FT /evidence="ECO:0000269|PubMed:21285510" FT /id="VAR_076532" FT VARIANT 244 FT /note="Y -> C (in MCCPD; dbSNP:rs760048191)" FT /evidence="ECO:0000269|PubMed:21285510" FT /id="VAR_076533" SQ SEQUENCE 293 AA; 35216 MW; D88E0DDBE85DE0BF CRC64; MATNESVSIF SSASLAVEYV DSLLPENPLQ EPFKNAWNYM LNNYTKFQIA TWGSLIVHEA LYFLFCLPGF LFQFIPYMKK YKIQKDKPET WENQWKCFKV LLFNHFCIQL PLICGTYYFT EYFNIPYDWE RMPRWYFLLA RCFGCAVIED TWHYFLHRLL HHKRIYKYIH KVHHEFQAPF GMEAEYAHPL ETLILGTGFF IGIVLLCDHV ILLWAWVTIR LLETIDVHSG YDIPLNPLNL IPFYAGSRHH DFHHMNFIGN YASTFTWWDR IFGTDSQYNA YNEKRKKFEK KTE //