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UniProtKB/Swiss-Prot entry Q64FW2


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

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Entry information
Entry name RETST_MOUSE
Primary accession number Q64FW2
Secondary accession numbers Q3UNN9 Q78JX8 Q8VHE7 Q9CW85
Integrated into Swiss-Prot on March 7, 2006
Sequence was last modified on March 7, 2006 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 34)
Name and origin of the protein
Protein name All-trans-retinol 13,14-reductase [Precursor]
Synonyms EC 1.3.99.23
All-trans-13,14-dihydroretinol saturase
RetSat
Gene name
Name: Retsat
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 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
STRAIN=C57BL/6;
TISSUE=Retina;
DOI=10.1074/jbc.M409130200; PubMed=15358783 [NCBI, ExPASy, EBI, Israel, Japan]
Moise A.R., Kuksa V., Imanishi Y., Palczewski K.;
"Identification of all-trans-retinol: all-trans-13,14-dihydroretinol saturase.";
J. Biol. Chem. 279:50230-50242(2004).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=A/J;
DOI=10.1038/sj.onc.1204941; PubMed=11753649 [NCBI, ExPASy, EBI, Israel, Japan]
Wang Y., Hu L., Yao R., Wang M., Crist K.A., Grubbs C.J., Johanning G.L., Lubet R.A., You M.;
"Altered gene expression profile in chemically induced rat mammary adenocarcinomas and its modulation by an aromatase inhibitor.";
Oncogene 20:7710-7721(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C3H, and C57BL/6J;
TISSUE=Brain, and Kidney;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 274-609.
STRAIN=FVB/N;
TISSUE=Salivary gland;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
Comments
  • FUNCTION: Retinol saturase carrying out the saturation of the 13-14 double bond of all-trans-retinol to produce all-trans-13,14-dihydroretinol. Has activity toward all-trans-retinol as substrate. Does not use all-trans-retinoic acid nor 9-cis, 11-cis or 13-cis-retinol isomers as substrates. May play a role in the metabolism of vitamin A.
  • CATALYTIC ACTIVITY: All-trans-13,14-dihydroretinol + acceptor = all-trans-retinol + reduced acceptor.
  • COFACTOR: NAD, NADP, or FAD (By similarity).
  • SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein.
  • TISSUE SPECIFICITY: Predominantly expressed in the liver and kidney. Also expressed in intestine. Weakly expressed in other tissues.
  • SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family. CrtISO subfamily.
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
AY704159; AAU25836.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF466400; AAL73986.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK002851; BAB22406.2; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK144115; BAE25708.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC011203; AAH11203.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_080435.3; -.
UniGene Mm.305108
3D structure databases
ModBase Q64FW2.
Organism-specific databases
MGI MGI:1914692; Retsat.
Gene expression databases
GermOnline ENSMUSG00000056666; Mus musculus.
Ontologies
GO
GO:0005789; Cellular component: endoplasmic reticulum membrane (inferred from direct assay from HGNC).
GO:0005640; Cellular component: nuclear outer membrane (inferred from direct assay from HGNC).
GO:0051786; Molecular function: all-trans-retinol 13,14-reductase activity (inferred from direct assay from HGNC).
GO:0055114; Biological process: oxidation reduction (inferred from direct assay from HGNC).
GO:0042572; Biological process: retinol metabolic process (inferred from direct assay from HGNC).
QuickGo view.
Family and domain databases
InterPro IPR003953; FAD_bind2_N.
Graphical view of domain structure.
Pfam PF00890; FAD_binding_2; 1.
Pfam graphical view of domain structure.
ProDom PD139017; Phytn_dehydro; 1.
[Domain structure / List of seq. sharing at least 1 domain]
BLOCKS Q64FW2.
Genome annotation databases
Ensembl ENSMUSG00000056666; Mus musculus. [Contig view]
GeneID 67442; -.
KEGG mmu:67442; -.
Phylogenomic databases
HOGENOM Q64FW2; -.
HOVERGEN Q64FW2; -.
Other
SOURCE Retsat; Mus musculus.
ProtoNet Q64FW2.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Endoplasmic reticulum; FAD; Flavoprotein; Membrane; NAD; NADP; Oxidoreductase; Signal.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    25  25     Potential. 
CHAIN   26   609  584     All-trans-retinol 13,14-reductase. PRO_0000225667
NP_BIND   69    97  29     FAD or NAD or NADP (Potential). 
CONFLICT   273   273        T -> A (in Ref. 1; AAU25836 and 3; BAB22406). 
CONFLICT   293   293        R -> G (in Ref. 1, 3; BAB22406 and 4; AAH11203). 
CONFLICT   306   306        I -> V (in Ref. 4; AAH11203). 
CONFLICT   451   451        E -> D (in Ref. 3; BAE25708). 
CONFLICT   495   495        A -> V (in Ref. 3; BAB22406). 
Sequence information
Length: 609 AA [This is the length of the unprocessed precursor] Molecular weight: 67464 Da [This is the MW of the unprocessed precursor] CRC64: 09B6EB440E52145D [This is a checksum on the sequence]
        10         20         30         40         50         60 
MWITALLLAV LLLVILHRVY VGLYAASSPN PFAEDVKRPP EPLVTDKEAR KKVLKQAFSV 

        70         80         90        100        110        120 
SRVPEKLDAV VIGSGIGGLA SAAVLAKAGK RVLVLEQHTK AGGCCHTFGE NGLEFDTGIH 

       130        140        150        160        170        180 
YIGRMREGNI GRFILDQITE GQLDWAPMAS PFDLMILEGP NGRKEFPMYS GRKEYIQGLK 

       190        200        210        220        230        240 
KKFPKEEAVI DKYMELVKVV ARGVSHAVLL KFLPLPLTQL LSKFGLLTRF SPFCRASTQS 

       250        260        270        280        290        300 
LAEVLQQLGA SRELQAVLSY IFPTYGVTPS HTTFSLHALL VDHYIQGAYY PRRGSSEIAF 

       310        320        330        340        350        360 
HTIPLIQRAG GAVLTRATVQ SVLLDSAGRA CGVSVKKGQE LVNIYCPVVI SNAGMFNTYQ 

       370        380        390        400        410        420 
HLLPETVRHL PDVKKQLAMV RPGLSMLSIF ICLKGTKEDL KLQSTNYYVY FDTDMDKAME 

       430        440        450        460        470        480 
RYVSMPKEKA PEHIPLLFIA FPSSKDPTWE ERFPDRSTMT ALVPMAFEWF EEWQEEPKGK 

       490        500        510        520        530        540 
RGVDYETLKN AFVEASMSVI MKLFPQLEGK VESVTGGSPL TNQYYLAAPR GATYGADHDL 

       550        560        570        580        590        600 
ARLHPHAMAS IRAQTPIPNL YLTGQDIFTC GLMGALQGAL LCSSAILKRN LYSDLQALGS 


KVKAQKKKM 

Q64FW2 in FASTA format

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