[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Intestine; DOI=10.1074/jbc.271.28.16927; PubMed=8663358 [NCBI, ExPASy, EBI, Israel, Japan] Li L., Kaplan J.; "Characterization of yeast methyl sterol oxidase (ERG25) and identification of a human homologue."; J. Biol. Chem. 271:16927-16933(1996).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Retina; Herrmann K.; Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Eye; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).

Comments

CATALYTIC ACTIVITY: 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.
CATALYTIC ACTIVITY: 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.
CATALYTIC ACTIVITY: 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.
COFACTOR: Iron (Probable).
PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol from lanosterol: step 3/6 .
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein (Probable).
DOMAIN: The histidine box domains may contain the active site and/or be involved in metal ion binding.
SIMILARITY: Belongs to the sterol desaturase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U60205; AAC50587.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U93162; AAB81566.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC010653; AAH10653.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC107879; AAI07880.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001017369.1; -.
NP_006736.1; -.

UniGene

Hs.105269

3D structure databases

ModBase

Q15800.

Protein-protein interaction databases

IntAct

Q15800; -.

Enzyme and pathway databases

Reactome

REACT_602; Lipid and lipoprotein metabolism.

Organism-specific databases

HIX0004617; -.

HGNC:10545; SC4MOL.

607545; gene. [NCBI / EBI]

PharmGKB

PA34955; -.

GeneCards

Q15800.

Gene expression databases

ArrayExpress

Q15800; -.

CleanEx

HS_SC4MOL; -.

GermOnline

ENSG00000052802; Homo sapiens.

Ontologies

GO:0005789;	Cellular component: endoplasmic reticulum membrane (inferred from experiment from Reactome).
GO:0016021;	Cellular component: integral to membrane (traceable author statement from ProtInc).
GO:0005886;	Cellular component: plasma membrane (traceable author statement from ProtInc).
GO:0000254;	Molecular function: C-4 methylsterol oxidase activity (traceable author statement from ProtInc).
GO:0006631;	Biological process: fatty acid metabolic process (traceable author statement from ProtInc).
GO:0008202;	Biological process: steroid metabolic process (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR006088; Sterol_desatur.
Graphical view of domain structure.

Pfam

PF01598; Sterol_desat; 1.
Pfam graphical view of domain structure.

Genome annotation databases

Ensembl

ENSG00000052802; Homo sapiens. [Contig view]

GeneID

6307; -.

KEGG

hsa:6307; -.

Phylogenomic databases

HOGENOM

Q15800; -.

HOVERGEN

Q15800; -.

Other

DB00157; NADH.

Q15800; -.

24483; -.

SC4MOL; Homo sapiens.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Endoplasmic reticulum; Iron; Lipid synthesis; Membrane; NAD; Oxidoreductase; Steroid biosynthesis; Sterol biosynthesis; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 293`	`293`	`C-4 methylsterol oxidase.`	`PRO_0000117033`
`TRANSMEM`	`55 75`	`21`	`Potential.`
`TRANSMEM`	`100 120`	`21`	`Potential.`
`TRANSMEM`	`199 219`	`21`	`Potential.`
`MOTIF`	`157 161`	`5`	`Histidine box-1.`
`MOTIF`	`170 174`	`5`	`Histidine box-2.`
`MOTIF`	`249 255`	`7`	`Histidine box-3.`

Sequence information

Length: 293 AA [This is the length of the unprocessed precursor]

Molecular weight: 35216 Da [This is the MW of the unprocessed precursor]

CRC64: D88E0DDBE85DE0BF [This is a checksum on the sequence]

        10         20         30         40         50         60 
MATNESVSIF SSASLAVEYV DSLLPENPLQ EPFKNAWNYM LNNYTKFQIA TWGSLIVHEA 

        70         80         90        100        110        120 
LYFLFCLPGF LFQFIPYMKK YKIQKDKPET WENQWKCFKV LLFNHFCIQL PLICGTYYFT 

       130        140        150        160        170        180 
EYFNIPYDWE RMPRWYFLLA RCFGCAVIED TWHYFLHRLL HHKRIYKYIH KVHHEFQAPF 

       190        200        210        220        230        240 
GMEAEYAHPL ETLILGTGFF IGIVLLCDHV ILLWAWVTIR LLETIDVHSG YDIPLNPLNL 

       250        260        270        280        290 
IPFYAGSRHH DFHHMNFIGN YASTFTWWDR IFGTDSQYNA YNEKRKKFEK KTE

Q15800 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools