ID   MSMO1_DANRE             Reviewed;         291 AA.
AC   Q7ZW77;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Methylsterol monooxygenase 1;
DE            EC=1.14.18.9 {ECO:0000250|UniProtKB:P53045};
DE   AltName: Full=C-4 methylsterol oxidase;
GN   Name=msmo1; Synonyms=sc4mol; ORFNames=zgc:56437;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=SJD;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the first step in the removal of the two C-4 methyl
CC       groups of 4,4-dimethylzymosterol. {ECO:0000250|UniProtKB:P53045}.
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:P53045};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000250|UniProtKB:P53045};
CC   -!- PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol from
CC       lanosterol: step 3/6.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC       Multi-pass membrane protein {ECO:0000305}.
CC   -!- DOMAIN: The histidine box domains may contain the active site and/or be
CC       involved in metal ion binding.
CC   -!- SIMILARITY: Belongs to the sterol desaturase family. {ECO:0000305}.
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DR   EMBL; BC050163; AAH50163.1; -; mRNA.
DR   RefSeq; NP_998518.1; NM_213353.1.
DR   AlphaFoldDB; Q7ZW77; -.
DR   STRING; 7955.ENSDARP00000091590; -.
DR   PaxDb; Q7ZW77; -.
DR   GeneID; 406662; -.
DR   KEGG; dre:406662; -.
DR   CTD; 6307; -.
DR   ZFIN; ZDB-GENE-040426-2670; msmo1.
DR   eggNOG; KOG0873; Eukaryota.
DR   InParanoid; Q7ZW77; -.
DR   OrthoDB; 1493916at2759; -.
DR   PhylomeDB; Q7ZW77; -.
DR   Reactome; R-DRE-191273; Cholesterol biosynthesis.
DR   UniPathway; UPA00770; UER00756.
DR   PRO; PR:Q7ZW77; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
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:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0016126; P:sterol biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR006694; Fatty_acid_hydroxylase.
DR   Pfam; PF04116; FA_hydroxylase; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Iron; Lipid biosynthesis; Lipid metabolism;
KW   Membrane; NAD; Oxidoreductase; Reference proteome; Steroid biosynthesis;
KW   Steroid metabolism; Sterol biosynthesis; Sterol metabolism; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..291
FT                   /note="Methylsterol monooxygenase 1"
FT                   /id="PRO_0000249853"
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                   /evidence="ECO:0000250"
FT   MOTIF           170..174
FT                   /note="Histidine box-2"
FT                   /evidence="ECO:0000250"
FT   MOTIF           249..255
FT                   /note="Histidine box-3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   291 AA;  34807 MW;  67A435866F99E116 CRC64;
     MEVNGTANIL SSAFLAVEFV DSFLPQNPLQ EPFKHAWNHM LQNYTKFQIA TWGSLIVHEL
     IYFLFCLPGF IFQFLPFMQK YKIQPDKPET WEKQWKCFKM LLFNHFCIQL PLICGTYYFT
     EFFSIPYDWD TMPRWPFLLA QCFGCAVIED TWHYFLHRAL HHRRIYKYIH KVHHDFTSPF
     GMQAEYAHPL ETLILGAGFF IGTMVFCNHM ILLWAWVTFR LLETIDVHSG YDIPLNPLHL
     IPFYAGARFH DFHHMNFVGN YGSTFTWWDR LFDTDSQFNK HYSHHKTAKS D