MSMO1_MACFA
ID MSMO1_MACFA Reviewed; 293 AA.
AC Q4R4Q4;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 59.
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; ORFNames=QtrA-11285;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Temporal cortex;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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] + 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: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] + 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: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] + 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: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] + 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: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] + 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: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. {ECO:0000250|UniProtKB:Q15800}.
CC -!- SIMILARITY: Belongs to the sterol desaturase family. {ECO:0000305}.
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DR EMBL; AB169840; BAE01921.1; -; mRNA.
DR AlphaFoldDB; Q4R4Q4; -.
DR STRING; 9541.XP_005556297.1; -.
DR eggNOG; KOG0873; Eukaryota.
DR UniPathway; UPA00063; -.
DR UniPathway; UPA00770; UER00756.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000254; F:C-4 methylsterol oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR006694; Fatty_acid_hydroxylase.
DR Pfam; PF04116; FA_hydroxylase; 1.
PE 2: Evidence at transcript 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.
FT CHAIN 1..293
FT /note="Methylsterol monooxygenase 1"
FT /id="PRO_0000249850"
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"
SQ SEQUENCE 293 AA; 35252 MW; 584AF62E7F3CC698 CRC64;
MATNESVSIF SSASLAVEYV DSLLPENPLQ EPFKNAWNYM LNNYTKFQIA TWGSLIVHEA
LYFSFCLPGF LFQFIPYMKK YKIQKDKPET WENQWKCFKV LLFNHFCIQL PLICGTYYFT
EYFNIPYDWE RMPRWYFLLA RCFGCAVIED TWHYFMHRLL HHKRIYKYIH KVHHEFQAPF
GMEAEYAHPL ETLILGTGFF IGIVLLCDHV ILLWAWVTIR LLETIDVHSG YDIPLNPLNL
IPFYAGSRHH DFHHMNFIGN YASTFTWWDR IFGTDSQYHA YYEKKKKFEK KTE
