Reviewed, UniProtKB/Swiss-Prot Q71KT5 (ERG24_MOUSE)

Names and origin

Protein names

Recommended name:
    Delta(14)-sterol reductase
      Short name=Delta-14-SR
    EC=1.3.1.70
Alternative name(s):
    C-14 sterol reductase
    Sterol C14-reductase
    Transmembrane 7 superfamily member 2

Gene names

Name:

Tm7sf2

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	418 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Involved in the conversion of lanosterol to cholesterol.
Catalytic activity	4,4-dimethyl-5-alpha-cholesta-8,24-dien-3-beta-ol + NADP+ = 4,4-dimethyl-5-alpha-cholesta-8,14,24-trien-3-beta-ol + NADPH.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.
Sequence similarities	Belongs to the ERG4/ERG24 family.

Ontologies

Keywords
Biological process	Cholesterol biosynthesis Lipid synthesis Steroid biosynthesis Sterol biosynthesis
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane
Ligand	NADP
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	cholesterol biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction 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	delta14-sterol reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 418	418	Delta(14)-sterol reductase		PRO_0000331121
Regions
	Transmembrane	13 – 35	23	Potential
	Transmembrane	62 – 81	20	Potential
	Transmembrane	102 – 124	23	Potential
	Transmembrane	129 – 148	20	Potential
	Transmembrane	255 – 277	23	Potential
	Transmembrane	287 – 304	18	Potential
	Transmembrane	355 – 377	23	Potential

Sequences

	Sequence		Length	Mass (Da)
	Q71KT5-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 05DCB3E4B9422D31	FASTA	418	46,493
	10 20 30 40 50 60 MTSREASQAP LEFGGPLGVA ALLILLPATM FHLLLAARSG PARLLALPAY LPGLEELWSP 70 80 90 100 110 120 WALLLLFIWL GLQVALYLLP ARKVAEGLEL KDKSRLRYPI NGFQALVLTA LLMGLGVSVG 130 140 150 160 170 180 LPLGALPGML LPLAFATTLT SFIFSLLLYA KALVAPASAL APGGNSGNSM YDFFLGRELN 190 200 210 220 230 240 PRLGSFDFKY FCELRPGLIG WVFINLALLM QEAELRGSPS LAMWLVNGFQ LLYVGDALWY 250 260 270 280 290 300 EESVLTTMDI IHDGFGFMLV FGDLAWVPFT YSLQAQFLLY HPQPLGLPMA LLICLLKAIG 310 320 330 340 350 360 YYIFRGANSQ KNTFRKNPSD PSVAGLETIP TATGRQLLVS GWWGMVRHPN YLGDLIMALA 370 380 390 400 410 WSLPCGLSHL LPYFYVLYFT ALLVHREARD EQQCLQKYGR AWQEYCKRVP YRIIPYVY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning and expression of the gene encoding the mouse C-14 sterol reductase." Roberti R., Bennati A.M. Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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: NOD.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF480070 mRNA. Translation: AAQ05836.1. AK155475 mRNA. Translation: BAE33285.1.
IPI	IPI00751362.
RefSeq	NP_082730.2.
UniGene	Mm.478278
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q71KT5.
Genome annotation databases
Ensembl	ENSMUST00000025713; ENSMUSP00000025713; ENSMUSG00000024799; Mus musculus. [Genome view]
GeneID	73166.
KEGG	mmu:73166.
UCSC	uc008ggw.1. mouse.
Organism-specific databases
CTD	73166.
MGI	MGI:1920416. Tm7sf2.
Phylogenomic databases
HOGENOM	HBG592488.
HOVERGEN	Q71KT5.
InParanoid	Q71KT5.
PhylomeDB	Q71KT5.
Gene expression databases
ArrayExpress	Q71KT5.
Bgee	Q71KT5.
Genevestigator	Q71KT5.
Family and domain databases
InterPro	IPR001171. Ergosterol_biosynth_ERG4_ERG24. IPR018083. Sterol_reductase_CS. [Graphical view]
Pfam	PF01222. ERG4_ERG24. 1 hit. [Graphical view]
PROSITE	PS01017. STEROL_REDUCT_1. 1 hit. PS01018. STEROL_REDUCT_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
SOURCE	Search...

Entry information

Entry name

ERG24_MOUSE

Accession

Primary (citable) accession number: Q71KT5

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	July 5, 2004
Last modified:	January 19, 2010
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)