NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
STRAIN=Sprague-Dawley;
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).

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 (By similarity).
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 (By similarity).
TISSUE SPECIFICITY: Highly expressed in liver, kidney and heart.
INDUCTION: Down-regulated in mammary adenocarcinomas.
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

AF465614; AAL73494.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_659552.1; -.

UniGene

Rn.55275

3D structure databases

ModBase

Q8VHE9.

Organism-specific databases

RGD

628802; Retsat.

Gene expression databases

ArrayExpress

Q8VHE9; -.

GermOnline

ENSRNOG00000014090; Rattus norvegicus.

Ontologies

GO:0005789;	Cellular component: endoplasmic reticulum membrane (inferred from sequence or structural similarity from HGNC).
GO:0005640;	Cellular component: nuclear outer membrane (inferred from sequence or structural similarity from HGNC).
GO:0051786;	Molecular function: all-trans-retinol 13,14-reductase activity (inferred from sequence or structural similarity from HGNC).
GO:0055114;	Biological process: oxidation reduction (inferred from sequence or structural similarity from HGNC).
GO:0042572;	Biological process: retinol metabolic process (inferred from sequence or structural similarity 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

Q8VHE9.

Genome annotation databases

Ensembl

ENSRNOG00000014090; Rattus norvegicus. [Contig view]

GeneID

246298; -.

KEGG

rno:246298; -.

Phylogenomic databases

HOVERGEN

Q8VHE9; -.

Other

ProtoNet

Q8VHE9.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Endoplasmic reticulum; FAD; Flavoprotein; Membrane; NAD; NADP; Oxidoreductase; Signal.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 21`	`21`	`Potential.`
`CHAIN`	`22 609`	`588`	`All-trans-retinol 13,14-reductase.`	`PRO_0000225668`
`NP_BIND`	`69 97`	`29`	`FAD or NAD or NADP (Potential).`

Sequence information

Length: 609 AA [This is the length of the unprocessed precursor]

Molecular weight: 67531 Da [This is the MW of the unprocessed precursor]

CRC64: D492DC98E8D23963 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MWITALLLVV LLLVVVHRVY VGLFTGSSPN 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 
EKFPKEEAVI DKYMELVKVV AHGVSHAILL KFLPLPLTQL LNKFGLLTRF SPFCRASTQS 

       250        260        270        280        290        300 
LAEVLKQLGA SPELQAVLSY ILPTYGVTPS HTTFSLHALL VDHYIQGAYY PRRGSSEIAF 

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

       370        380        390        400        410        420 
HLLPESVRYL PDVKKQLTMV KPGLSMLSIF ICLKGTKEEL KLQSTNYYVY FDTDMDKAME 

       430        440        450        460        470        480 
CYVSMPKEKA PEHIPLLFIP FPSSKDPTWE DRFPDRSTMT VLVPTAFEWF EEWQEEPKGK 

       490        500        510        520        530        540 
RGVDYETLKN TFREASMSVI MKLFPQLEGK VESVTGGSPL TNQYYLAAHR GATYGADHDL 

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


KVRAQKKKK

Q8VHE9 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools