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Q71KT5 (ERG24_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Delta(14)-sterol reductase

Short name=Delta-14-SR
EC=1.3.1.70
Alternative name(s):
C-14 sterol reductase
Short name=C14SR
Sterol C14-reductase
Transmembrane 7 superfamily member 2
Gene names
Name:Tm7sf2
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length418 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Involved in the conversion of lanosterol to cholesterol. Ref.2

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. Microsome membrane; Multi-pass membrane protein Ref.2.

Tissue specificity

Strongly expressed in liver, weaker in ovary, testis, kidney and brain. Ref.2

Disruption phenotype

mice develop normally, appear healthy and are fertile. Ref.2

Sequence similarities

Belongs to the ERG4/ERG24 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 418418Delta(14)-sterol reductase
PRO_0000331121

Regions

Transmembrane13 – 3523Helical; Potential
Transmembrane62 – 8120Helical; Potential
Transmembrane102 – 12423Helical; Potential
Transmembrane129 – 14820Helical; Potential
Transmembrane255 – 27723Helical; Potential
Transmembrane287 – 30418Helical; Potential
Transmembrane355 – 37723Helical; Potential

Experimental info

Sequence conflict2981V → A in AAQ05836. Ref.1
Sequence conflict2981V → A in BAE33285. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q71KT5 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 0DCCA4E4B9423A31

FASTA41846,521
        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 LLICLLKVIG 

       310        320        330        340        350        360 
YYIFRGANSQ KNTFRKNPSD PSVAGLETIP TATGRQLLVS GWWGMVRHPN YLGDLIMALA 

       370        380        390        400        410 
WSLPCGLSHL LPYFYVLYFT ALLVHREARD EQQCLQKYGR AWQEYCKRVP YRIIPYVY 

« Hide

References

« Hide '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]"Disruption of the gene encoding 3beta-hydroxysterol Delta14-reductase (Tm7sf2) in mice does not impair cholesterol biosynthesis."
Bennati A.M., Schiavoni G., Franken S., Piobbico D., Della Fazia M.A., Caruso D., De Fabiani E., Benedetti L., Cusella De Angelis M.G., Gieselmann V., Servillo G., Beccari T., Roberti R.
FEBS J. 275:5034-5047(2008)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
Strain: 129/SvJ.
[3]"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. expand/collapse author list , 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.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF480070 mRNA. Translation: AAQ05836.1.
EU672836 Genomic DNA. Translation: ACF94776.1.
AK155475 mRNA. Translation: BAE33285.1.
CH466612 Genomic DNA. Translation: EDL33202.1.
IPIIPI00751362.
RefSeqNP_082730.2. NM_028454.2.
UniGeneMm.227361.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ71KT5.

Proteomic databases

PRIDEQ71KT5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025713; ENSMUSP00000025713; ENSMUSG00000024799.
GeneID73166.
KEGGmmu:73166.

Organism-specific databases

CTD7108.
MGIMGI:1920416. Tm7sf2.

Phylogenomic databases

GeneTreeENSGT00390000000417.
HOGENOMHBG592488.
HOVERGENHBG007825.
InParanoidQ71KT5.
OrthoDBEOG4FBHT3.
PhylomeDBQ71KT5.

Gene expression databases

ArrayExpressQ71KT5.
BgeeQ71KT5.
GenevestigatorQ71KT5.

Family and domain databases

InterProIPR001171. Ergosterol_biosynth_ERG4_ERG24.
IPR018083. Sterol_reductase_CS.
[Graphical view]
KOK00222.
PfamPF01222. ERG4_ERG24. 1 hit.
[Graphical view]
PROSITEPS01017. STEROL_REDUCT_1. 1 hit.
PS01018. STEROL_REDUCT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

SOURCESearch...

Entry information

Entry nameERG24_MOUSE
AccessionPrimary (citable) accession number: Q71KT5
Secondary accession number(s): B5LBK0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: July 27, 2011
Last modified: November 16, 2011
This is version 57 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families