C-4 methylsterol oxidase - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot Q15800 (ERG25_HUMAN)

Last modified January 19, 2010. Version 86. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    C-4 methylsterol oxidase
    EC=1.14.13.72
Alternative name(s):
    Methylsterol monooxygenase

Gene names

Name:	SC4MOL
Synonyms:	DESP4, ERG25

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	293 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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General annotation (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. 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. 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.
Sequence similarities	Belongs to the sterol desaturase family.

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Ontologies

Keywords
Biological process	Lipid synthesis Steroid biosynthesis Sterol biosynthesis
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Polymorphism
Domain	Transmembrane
Ligand	Iron NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW sterol biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum membrane Ref.1 Inferred from Experiment. Source: Reactome integral to membrane Ref.1 Traceable author statement. Source: ProtInc plasma membrane Ref.1 Traceable author statement. Source: ProtInc
Molecular function	C-4 methylsterol oxidase activity Ref.1 Inferred from Experiment. Source: Reactome iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 293

293

C-4 methylsterol oxidase

PRO_0000117033

Regions

Transmembrane

55 – 75

Potential

Transmembrane

100 – 120

Potential

Transmembrane

199 – 219

Potential

Motif

157 – 161

Histidine box-1

Motif

170 – 174

Histidine box-2

Motif

249 – 255

Histidine box-3

Natural variations

Natural variant

124

N → S: dbSNP rs34499452.

VAR_048898

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Sequences

Sequence

Length

Mass (Da)

Tools

Q15800-1 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: D88E0DDBE85DE0BF
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FASTA

293

35,216

        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

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of yeast methyl sterol oxidase (ERG25) and identification of a human homologue." Li L., Kaplan J. J. Biol. Chem. 271:16927-16933(1996) [PubMed: 8663358] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Intestine.
[2]	Herrmann K. Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Retina.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Eye.
[6]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	U60205 mRNA. Translation: AAC50587.1. U93162 mRNA. Translation: AAB81566.1. AK292418 mRNA. Translation: BAF85107.1. CH471056 Genomic DNA. Translation: EAX04820.1. BC010653 mRNA. Translation: AAH10653.1. BC107879 mRNA. Translation: AAI07880.1.
IPI	IPI00019899.
RefSeq	NP_001017369.1. NP_006736.1.
UniGene	Hs.105269 Hs.593050
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q15800. 1 interaction.
STRING	Q15800.
Proteomic databases
PRIDE	Q15800.
Genome annotation databases
Ensembl	ENST00000261507; ENSP00000261507; ENSG00000052802; Homo sapiens. [Genome view]
GeneID	6307.
KEGG	hsa:6307.
UCSC	uc003ire.1. human.
Organism-specific databases
CTD	6307.
GeneCards	GC04P166468.
H-InvDB	HIX0004617.
HGNC	HGNC:10545. SC4MOL.
MIM	607545. gene.
PharmGKB	PA34955.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG10938.
HOGENOM	HBG325679.
HOVERGEN	Q15800.
InParanoid	Q15800.
OMA	PLNPLHL.
PhylomeDB	Q15800.
Enzyme and pathway databases
BRENDA	1.14.13.72. 247.
Reactome	REACT_602. Metabolism of lipids and lipoproteins.
Gene expression databases
ArrayExpress	Q15800.
Bgee	Q15800.
CleanEx	HS_SC4MOL.
Genevestigator	Q15800.
GermOnline	ENSG00000052802. Homo sapiens.
Family and domain databases
InterPro	IPR006694. Fatty_acid_hydroxylase. [Graphical view]
Pfam	PF04116. FA_hydroxylase. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
DrugBank	DB00157. NADH.
NextBio	24483.
SOURCE	Search...

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Entry information

Entry name

ERG25_HUMAN

Accession

Primary (citable) accession number: Q15800
Secondary accession number(s): A8K8Q3, Q32Q24

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	January 19, 2010
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.

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