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UniProtKB/Swiss-Prot entry Q71KT5


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ERG24_MOUSE
Primary accession number Q71KT5
Secondary accession numbers None
Integrated into Swiss-Prot on April 29, 2008
Sequence was last modified on July 5, 2004 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 32)
Name and origin of the protein
Protein name Delta(14)-sterol reductase
Synonyms Delta-14-SR
EC 1.3.1.70
C-14 sterol reductase
Sterol C14-reductase
Transmembrane 7 superfamily member 2
Gene name
Name: Tm7sf2
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Roberti R., Bennati A.M.;
"cDNA cloning and expression of the gene encoding the mouse C-14 sterol reductase.";
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=NOD;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
Comments
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
AF480070; AAQ05836.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK155475; BAE33285.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
UniGene Mm.458077
3D structure databases
ModBase Q71KT5.
Organism-specific databases
MGI MGI:1920416; Tm7sf2.
Ontologies
GO
GO:0005789; Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0050613; Molecular function: delta14-sterol reductase activity (inferred from electronic annotation from EC).
GO:0006695; Biological process: cholesterol biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001171; ERG4_ERG24.
Graphical view of domain structure.
Pfam PF01222; ERG4_ERG24; 1.
Pfam graphical view of domain structure.
PROSITE PS01017; STEROL_REDUCT_1; 1.
PS01018; STEROL_REDUCT_2; 1.
BLOCKS Q71KT5.
ProtoNet Q71KT5.
Genome annotation databases
Ensembl ENSMUSG00000024799; Mus musculus. [Contig view]
Phylogenomic databases
HOGENOM Q71KT5; -.
HOVERGEN Q71KT5; -.
Other
SOURCE Tm7sf2; Mus musculus.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cholesterol biosynthesis; Endoplasmic reticulum; Lipid synthesis; Membrane; NADP; Oxidoreductase; Steroid biosynthesis; Sterol biosynthesis; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   418  418     Delta(14)-sterol reductase. PRO_0000331121
TRANSMEM   13    35  23     Potential. 
TRANSMEM   62    81  20     Potential. 
TRANSMEM   102   124  23     Potential. 
TRANSMEM   129   148  20     Potential. 
TRANSMEM   255   277  23     Potential. 
TRANSMEM   287   304  18     Potential. 
TRANSMEM   355   377  23     Potential. 
Sequence information
Length: 418 AA [This is the length of the unprocessed precursor] Molecular weight: 46493 Da [This is the MW of the unprocessed precursor] CRC64: 05DCB3E4B9422D31 [This is a checksum on the sequence]
        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 

Q71KT5 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

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