MSMO1_PIG
ID MSMO1_PIG Reviewed; 293 AA.
AC Q6UGB2;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 81.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RA Hwang K.-C., Ok D.-W., Kwon D.-N., Choi Y.-J., Lee S.-Y., Kim J.-H.;
RL Submitted (AUG-2003) 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}.
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; AY370690; AAQ67416.1; -; mRNA.
DR RefSeq; NP_998917.1; NM_213752.1.
DR AlphaFoldDB; Q6UGB2; -.
DR STRING; 9823.ENSSSCP00000009448; -.
DR PaxDb; Q6UGB2; -.
DR PeptideAtlas; Q6UGB2; -.
DR GeneID; 396590; -.
DR KEGG; ssc:396590; -.
DR CTD; 6307; -.
DR eggNOG; KOG0873; Eukaryota.
DR InParanoid; Q6UGB2; -.
DR OrthoDB; 1493916at2759; -.
DR UniPathway; UPA00063; -.
DR UniPathway; UPA00770; UER00756.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-UniPathway.
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 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_0000249851"
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; 35102 MW; 02B4733E8049F0ED CRC64;
MATNQSISIF SSASLAVEYV DSLLPENPLQ EPFKNAWNYM LNNYTKFQIA TWGSLIVHEA
LYFFFCLPGF LFQFIPYMKK YKIQKDKPET WENQWKCFKV LLFNHFCIQF PLICGTYYFT
EYFSIPYDWE TMPRWYIALA RCFGCAVIED TWHYFLHRLL HHKRIYKYIH KIHHEFQAPF
GMEAEYAHPL ETLILGTGFF IGIMLLCDHV ILLWAWVTVR LIETIDVHSG YDIPLNPLHL
IPFYAGSRHH DFHHMNFIGN YASTFTWWDR IFGTDAQYNA YNEKRKKAEK KTE
