Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Methylsterol monooxygenase 1

Gene

MSMO1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the first step in the removal of the two C-4 methyl groups of 4,4-dimethylzymosterol.By similarity

Catalytic activityi

4,4-dimethyl-5-alpha-cholest-7-en-3-beta-ol + NAD(P)H + O2 = 4-beta-hydroxymethyl-4-alpha-methyl-5-alpha-cholest-7-en-3-beta-ol + NAD(P)+ + H2O.By similarity
4-beta-hydroxymethyl-4-alpha-methyl-5-alpha-cholest-7-en-3-beta-ol + NAD(P)H + O2 = 3-beta-hydroxy-4-beta-methyl-5-alpha-cholest-7-ene-4-alpha-carbaldehyde + NAD(P)+ + 2 H2O.By similarity
3-beta-hydroxy-4-beta-methyl-5-alpha-cholest-7-ene-4-alpha-carbaldehyde + NAD(P)H + O2 = 3-beta-hydroxy-4-beta-methyl-5-alpha-cholest-7-ene-4-alpha-carboxylate + NAD(P)+ + H2O.By similarity

Cofactori

Fe cationBy similarity

Pathwayi: zymosterol biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes zymosterol from lanosterol.
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. Lanosterol 14-alpha demethylase (CYP51A1)
  2. no protein annotated in this organism
  3. Methylsterol monooxygenase 1 (MSMO1)
  4. Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating (NSDHL)
  5. 3-keto-steroid reductase (HSD17B7)
  6. no protein annotated in this organism
This subpathway is part of the pathway zymosterol biosynthesis, which is itself part of Steroid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes zymosterol from lanosterol, the pathway zymosterol biosynthesis and in Steroid biosynthesis.

GO - Molecular functioni

GO - Biological processi

  • cholesterol biosynthetic process Source: Reactome
  • fatty acid biosynthetic process Source: InterPro
  • fatty acid metabolic process Source: ProtInc
  • steroid metabolic process Source: ProtInc
  • sterol biosynthetic process Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism

Keywords - Ligandi

Iron, NAD

Enzyme and pathway databases

BioCyciMetaCyc:HS00650-MONOMER.
BRENDAi1.14.13.72. 2681.
ReactomeiR-HSA-191273. Cholesterol biosynthesis.
UniPathwayiUPA00770; UER00756.

Chemistry databases

SwissLipidsiSLP:000001244.

Names & Taxonomyi

Protein namesi
Recommended name:
Methylsterol monooxygenase 1 (EC:1.14.13.72By similarity)
Alternative name(s):
C-4 methylsterol oxidase
Gene namesi
Name:MSMO1
Synonyms:DESP4, ERG25, SC4MOL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:10545. MSMO1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei55 – 75HelicalSequence analysisAdd BLAST21
Transmembranei100 – 120HelicalSequence analysisAdd BLAST21
Transmembranei199 – 219HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

  • endoplasmic reticulum Source: ProtInc
  • endoplasmic reticulum membrane Source: GO_Central
  • integral component of membrane Source: ProtInc
  • plasma membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Microcephaly, congenital cataract, and psoriasiform dermatitis (MCCPD)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive inborn error of cholesterol metabolism characterized by accumulation of a large amount of methylsterols, particularly dimethylsterols, in affected individuals. Patients manifest psoriasiform dermatitis, arthralgias, congenital cataracts, microcephaly, and developmental delay.
See also OMIM:616834
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_076531115G → R in MCCPD; unknown pathological significance. 1 Publication1
Natural variantiVAR_076532173H → Q in MCCPD. 1 Publication1
Natural variantiVAR_076533244Y → C in MCCPD. 1 PublicationCorresponds to variant rs760048191dbSNPEnsembl.1

Keywords - Diseasei

Cataract, Disease mutation

Organism-specific databases

DisGeNETi6307.
MIMi616834. phenotype.
OpenTargetsiENSG00000052802.
PharmGKBiPA34955.

Polymorphism and mutation databases

BioMutaiMSMO1.
DMDMi2498340.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001170331 – 293Methylsterol monooxygenase 1Add BLAST293

Proteomic databases

EPDiQ15800.
MaxQBiQ15800.
PaxDbiQ15800.
PeptideAtlasiQ15800.
PRIDEiQ15800.

PTM databases

iPTMnetiQ15800.
PhosphoSitePlusiQ15800.
SwissPalmiQ15800.

Expressioni

Gene expression databases

BgeeiENSG00000052802.
CleanExiHS_SC4MOL.
ExpressionAtlasiQ15800. baseline and differential.
GenevisibleiQ15800. HS.

Organism-specific databases

HPAiHPA056127.

Interactioni

Protein-protein interaction databases

BioGridi112214. 12 interactors.
IntActiQ15800. 2 interactors.
MINTiMINT-2862749.
STRINGi9606.ENSP00000261507.

Structurei

3D structure databases

ProteinModelPortaliQ15800.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi157 – 161Histidine box-15
Motifi170 – 174Histidine box-25
Motifi249 – 255Histidine box-37

Domaini

The histidine box domains may contain the active site and/or be involved in metal ion binding.

Sequence similaritiesi

Belongs to the sterol desaturase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0873. Eukaryota.
COG3000. LUCA.
GeneTreeiENSGT00530000063017.
HOGENOMiHOG000162289.
HOVERGENiHBG051504.
InParanoidiQ15800.
KOiK07750.
OMAiDSQYVAY.
OrthoDBiEOG091G0BM3.
PhylomeDBiQ15800.
TreeFamiTF354294.

Family and domain databases

InterProiIPR006694. Fatty_acid_hydroxylase.
[Graphical view]
PfamiPF04116. FA_hydroxylase. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q15800-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MATNESVSIF SSASLAVEYV DSLLPENPLQ EPFKNAWNYM LNNYTKFQIA
60 70 80 90 100
TWGSLIVHEA LYFLFCLPGF LFQFIPYMKK YKIQKDKPET WENQWKCFKV
110 120 130 140 150
LLFNHFCIQL PLICGTYYFT EYFNIPYDWE RMPRWYFLLA RCFGCAVIED
160 170 180 190 200
TWHYFLHRLL HHKRIYKYIH KVHHEFQAPF GMEAEYAHPL ETLILGTGFF
210 220 230 240 250
IGIVLLCDHV ILLWAWVTIR LLETIDVHSG YDIPLNPLNL IPFYAGSRHH
260 270 280 290
DFHHMNFIGN YASTFTWWDR IFGTDSQYNA YNEKRKKFEK KTE
Length:293
Mass (Da):35,216
Last modified:November 1, 1997 - v1
Checksum:iD88E0DDBE85DE0BF
GO
Isoform 2 (identifier: Q15800-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-131: Missing.

Show »
Length:162
Mass (Da):19,470
Checksum:iEFA578AF15EDB678
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_076531115G → R in MCCPD; unknown pathological significance. 1 Publication1
Natural variantiVAR_048898124N → S.Corresponds to variant rs34499452dbSNPEnsembl.1
Natural variantiVAR_076532173H → Q in MCCPD. 1 Publication1
Natural variantiVAR_076533244Y → C in MCCPD. 1 PublicationCorresponds to variant rs760048191dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0445851 – 131Missing in isoform 2. 1 PublicationAdd BLAST131

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U60205 mRNA. Translation: AAC50587.1.
U93162 mRNA. Translation: AAB81566.1.
AK292418 mRNA. Translation: BAF85107.1.
AK295432 mRNA. Translation: BAH12066.1.
AC012504 Genomic DNA. No translation available.
CH471056 Genomic DNA. Translation: EAX04820.1.
CH471056 Genomic DNA. Translation: EAX04821.1.
BC010653 mRNA. Translation: AAH10653.1.
BC107879 mRNA. Translation: AAI07880.1.
CCDSiCCDS3809.1. [Q15800-1]
CCDS43280.1. [Q15800-2]
RefSeqiNP_001017369.1. NM_001017369.2. [Q15800-2]
NP_006736.1. NM_006745.4. [Q15800-1]
XP_005263233.1. XM_005263176.2. [Q15800-1]
UniGeneiHs.105269.

Genome annotation databases

EnsembliENST00000261507; ENSP00000261507; ENSG00000052802. [Q15800-1]
ENST00000393766; ENSP00000377361; ENSG00000052802. [Q15800-2]
GeneIDi6307.
KEGGihsa:6307.
UCSCiuc003ire.4. human. [Q15800-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U60205 mRNA. Translation: AAC50587.1.
U93162 mRNA. Translation: AAB81566.1.
AK292418 mRNA. Translation: BAF85107.1.
AK295432 mRNA. Translation: BAH12066.1.
AC012504 Genomic DNA. No translation available.
CH471056 Genomic DNA. Translation: EAX04820.1.
CH471056 Genomic DNA. Translation: EAX04821.1.
BC010653 mRNA. Translation: AAH10653.1.
BC107879 mRNA. Translation: AAI07880.1.
CCDSiCCDS3809.1. [Q15800-1]
CCDS43280.1. [Q15800-2]
RefSeqiNP_001017369.1. NM_001017369.2. [Q15800-2]
NP_006736.1. NM_006745.4. [Q15800-1]
XP_005263233.1. XM_005263176.2. [Q15800-1]
UniGeneiHs.105269.

3D structure databases

ProteinModelPortaliQ15800.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112214. 12 interactors.
IntActiQ15800. 2 interactors.
MINTiMINT-2862749.
STRINGi9606.ENSP00000261507.

Chemistry databases

SwissLipidsiSLP:000001244.

PTM databases

iPTMnetiQ15800.
PhosphoSitePlusiQ15800.
SwissPalmiQ15800.

Polymorphism and mutation databases

BioMutaiMSMO1.
DMDMi2498340.

Proteomic databases

EPDiQ15800.
MaxQBiQ15800.
PaxDbiQ15800.
PeptideAtlasiQ15800.
PRIDEiQ15800.

Protocols and materials databases

DNASUi6307.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261507; ENSP00000261507; ENSG00000052802. [Q15800-1]
ENST00000393766; ENSP00000377361; ENSG00000052802. [Q15800-2]
GeneIDi6307.
KEGGihsa:6307.
UCSCiuc003ire.4. human. [Q15800-1]

Organism-specific databases

CTDi6307.
DisGeNETi6307.
GeneCardsiMSMO1.
HGNCiHGNC:10545. MSMO1.
HPAiHPA056127.
MIMi607545. gene.
616834. phenotype.
neXtProtiNX_Q15800.
OpenTargetsiENSG00000052802.
PharmGKBiPA34955.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0873. Eukaryota.
COG3000. LUCA.
GeneTreeiENSGT00530000063017.
HOGENOMiHOG000162289.
HOVERGENiHBG051504.
InParanoidiQ15800.
KOiK07750.
OMAiDSQYVAY.
OrthoDBiEOG091G0BM3.
PhylomeDBiQ15800.
TreeFamiTF354294.

Enzyme and pathway databases

UniPathwayiUPA00770; UER00756.
BioCyciMetaCyc:HS00650-MONOMER.
BRENDAi1.14.13.72. 2681.
ReactomeiR-HSA-191273. Cholesterol biosynthesis.

Miscellaneous databases

ChiTaRSiMSMO1. human.
GenomeRNAii6307.
PROiQ15800.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000052802.
CleanExiHS_SC4MOL.
ExpressionAtlasiQ15800. baseline and differential.
GenevisibleiQ15800. HS.

Family and domain databases

InterProiIPR006694. Fatty_acid_hydroxylase.
[Graphical view]
PfamiPF04116. FA_hydroxylase. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMSMO1_HUMAN
AccessioniPrimary (citable) accession number: Q15800
Secondary accession number(s): A8K8Q3
, A8MYF6, D3DP32, Q32Q24
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 2, 2016
This is version 151 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.