Reviewed, UniProtKB/Swiss-Prot Q9CRA4 (ERG25_MOUSE)

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

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	293 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

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.

Ontologies

Keywords
Biological process	Lipid synthesis Steroid biosynthesis Sterol biosynthesis
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane
Ligand	Iron NAD
Molecular function	Oxidoreductase
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 Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	C-4 methylsterol oxidase activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 293	293	C-4 methylsterol oxidase		PRO_0000117034
Regions
	Transmembrane	55 – 75	21	Potential
	Transmembrane	100 – 120	21	Potential
	Transmembrane	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

Sequences

	Sequence		Length	Mass (Da)
	Q9CRA4-1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 0A275DE7B5D4DB52	FASTA	293	34,772
	10 20 30 40 50 60 MATNKSVGVF SSASLAVEYV DSLLPENPLQ EPFKNAWVYM LDNYTKFQIA TWGSLIVHEA 70 80 90 100 110 120 IYFLFSLPGF LFQFIPYMRK YKIQKDKPET FEGQWKCLKK ILFNHFFIQL PLICGTYYFT 130 140 150 160 170 180 EFFNIPYDWE RMPRWYLTLA RCLGCAVIED TWHYFLHRLL HHKRIYKYIH KVHHEFQAPF 190 200 210 220 230 240 GIEAEYAHPL ETLILGTGFF IGIVLLCDHV ILLWAWVTIR LLETIDVHSG YDIPLNPLNL 250 260 270 280 290 VPFYTGARHH DFHHMNFIGN YASTFTWWDK LFGTDAQYHA YIEKSKKLGK KSD

References

[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Amnion, Bone marrow, Cerebellum, Embryo, Liver and Placenta.
[2]	"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: Mammary tumor.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AK005090 mRNA. Translation: BAB23811.1. AK005441 mRNA. Translation: BAB24035.1. AK045059 mRNA. Translation: BAC32201.1. AK146684 mRNA. Translation: BAE27358.1. AK151135 mRNA. Translation: BAE30143.1. AK169017 mRNA. Translation: BAE40814.1. BC006802 mRNA. Translation: AAH06802.1.
IPI	IPI00133526.
RefSeq	NP_079712.1.
UniGene	Mm.30119
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q9CRA4.
Proteomic databases
PRIDE	Q9CRA4.
Genome annotation databases
Ensembl	ENSMUST00000034015; ENSMUSP00000034015; ENSMUSG00000031604; Mus musculus. [Genome view]
GeneID	66234.
KEGG	mmu:66234.
UCSC	uc009lux.1. mouse.
Organism-specific databases
CTD	66234.
MGI	MGI:1913484. Sc4mol.
Phylogenomic databases
HOGENOM	Q9CRA4.
HOVERGEN	Q9CRA4.
OMA	NPLHLIP.
Enzyme and pathway databases
BRENDA	1.14.13.72. 244.
Gene expression databases
ArrayExpress	Q9CRA4.
Bgee	Q9CRA4.
CleanEx	MM_SC4MOL.
Genevestigator	Q9CRA4.
GermOnline	ENSMUSG00000031604. Mus musculus.
Family and domain databases
InterPro	IPR006694. Fatty_acid_hydroxylase. [Graphical view]
Pfam	PF04116. FA_hydroxylase. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	321041.
SOURCE	Search...

Entry information

Entry name

ERG25_MOUSE

Accession

Primary (citable) accession number: Q9CRA4
Secondary accession number(s): Q543V8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 22, 2003
Last sequence update:	June 1, 2001
Last modified:	November 3, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)