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Reviewed, UniProtKB/Swiss-Prot Q64FW2 (RETST_MOUSE)

Last modified November 25, 2008. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    All-trans-retinol 13,14-reductase
    EC=1.3.99.23
Alternative name(s):
    All-trans-13,14-dihydroretinol saturase
      Short name=RetSat
Gene names
Name: Retsat
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length609 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (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.

Sequence similarities

Belongs to the carotenoid/retinoid oxidoreductase family. CrtISO subfamily.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 609584All-trans-retinol 13,14-reductase
PRO_0000225667

Regions

Nucleotide binding69 – 9729FAD or NAD or NADP Potential

Experimental info

Sequence conflict2731T → A in AAU25836. Ref.1
Sequence conflict2731T → A in BAB22406. Ref.3
Sequence conflict2931R → G in BAB22406. Ref.1 Ref.3
Sequence conflict2931R → G in AAH11203. Ref.4
Sequence conflict3061I → V in AAH11203. Ref.4
Sequence conflict4511E → D in BAE25708. Ref.3
Sequence conflict4951A → V in BAB22406. Ref.3

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Sequences

Sequence LengthMass (Da)Tools
Q64FW2-1 [UniParc].

Last modified March 7, 2006. Version 2.
Checksum: 09B6EB440E52145D

FASTA60967,464
        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

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References

« Hide 'large scale' references
[1]"Identification of all-trans-retinol: all-trans-13,14-dihydroretinol saturase."
Moise A.R., Kuksa V., Imanishi Y., Palczewski K.
J. Biol. Chem. 279:50230-50242(2004) [PubMed: 15358783] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Strain: C57BL/6.
Tissue: Retina.
[2]"Altered gene expression profile in chemically induced rat mammary adenocarcinomas and its modulation by an aromatase inhibitor."
Wang Y., Hu L., Yao R., Wang M., Crist K.A., Grubbs C.J., Johanning G.L., Lubet R.A., You M.
Oncogene 20:7710-7721(2001) [PubMed: 11753649] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: A/J.
[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: C3H and C57BL/6J.
Tissue: Brain and Kidney.
[4]"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] OF 274-609.
Strain: FVB/N.
Tissue: Salivary gland.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AY704159 mRNA. Translation: AAU25836.1.
AF466400 Genomic DNA. Translation: AAL73986.1.
AK002851 mRNA. Translation: BAB22406.2. Different initiation.
AK144115 mRNA. Translation: BAE25708.1.
BC011203 mRNA. Translation: AAH11203.1. Different initiation.
RefSeqNP_080435.3.
UniGeneMm.305108

3D structure databases

ModBaseSearch...

PTM databases

PhosphoSiteQ64FW2.

Genome annotation databases

EnsemblENSMUSG00000056666. Mus musculus. [Contig view]
GeneID67442.
KEGGmmu:67442.

Organism-specific databases

MGIMGI:1914692. Retsat.

Phylogenomic databases

HOGENOMQ64FW2.
HOVERGENQ64FW2.

Gene expression databases

GermOnlineENSMUSG00000056666. Mus musculus.

Family and domain databases

InterProIPR003953. FAD_bind2_N.
[Graphical view]
PfamPF00890. FAD_binding_2. 1 hit.
[Graphical view]
ProDomPD139017. Phytn_dehydro. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Other Resources

NextBio324578.
SOURCESearch...

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Entry information

Entry nameRETST_MOUSE
AccessionPrimary (citable) accession number: Q64FW2
Secondary accession number(s): Q3UNN9 expand/collapse secondary AC list , Q78JX8, Q8VHE7, Q9CW85
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: March 7, 2006
Last modified: November 25, 2008
This is version 36 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

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

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents