[1]	NUCLEOTIDE SEQUENCE [MRNA]. 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).

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).
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

AY707524; AAU34019.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

Q64FG0.

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

IPR000759; Adrndx_reductase.
IPR003953; FAD_bind2_N.
Graphical view of domain structure.

Pfam

PF00890; FAD_binding_2; 1.
Pfam graphical view of domain structure.

PRINTS

PR00419; ADXRDTASE.

ProDom

PD139017; Phytn_dehydro; 1.
[Domain structure / List of seq. sharing at least 1 domain]

BLOCKS

Q64FG0.

Phylogenomic databases

HOVERGEN

Q64FG0; -.

Other

ProtoNet

Q64FG0.

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 18`	`18`	`Potential.`
`CHAIN`	`19 610`	`592`	`All-trans-retinol 13,14-reductase.`	`PRO_0000225666`
`NP_BIND`	`70 98`	`29`	`FAD or NAD or NADP (Potential).`

Sequence information

Length: 610 AA [This is the length of the unprocessed precursor]

Molecular weight: 66918 Da [This is the MW of the unprocessed precursor]

CRC64: FD74D22F28129FB1 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MWLPLVLFLA VLLLAVVCKV YLGLFSGKSP NPFSEDVKRP PAPLVTDKEA RKKVLKQAFS 

        70         80         90        100        110        120 
ASRVPEKLDV VVIGSGFGGL AAAAILAKAG KRVLVLEQHT KAGGACHTFG ENGLEFDTGI 

       130        140        150        160        170        180 
HYIGRMEEGS IGRFILDQIT EGQLDWVPMS SPFDIMVLEG PNGRKEYPMY SGEKAYIQGL 

       190        200        210        220        230        240 
KEKFPQEEAI IDKYIKLVKV VSNGVAHAIL LKFLPLPVIQ LLDRCGLLTR FSPFLHASTQ 

       250        260        270        280        290        300 
SLAEVLQQLG ASSELQAVLS YIFPTYGVTP RHSAFSMHAL LVNHYLKGAF YPRGGSSEIA 

       310        320        330        340        350        360 
FHTIPVIQRA GGAVLTRATV QSVLLDSAGK ACGVSVKKGH ELVNIYCPVV VSNAGLFNTY 

       370        380        390        400        410        420 
EHLLPGNARC LPGVKQQLGM VRPGLGMMSV FICLQGTKED LHLPSTNYYV YHDTDMDQAM 

       430        440        450        460        470        480 
ERYVSMPREK AAEHIPLLFI AFPSAKDPTW EDRFPGRSSM IMLIPSAYEW FEEWQAELKG 

       490        500        510        520        530        540 
KRGSDYETYK NSFVEASMSV AMKLFPQLEG KVESVTAGSP LTNQFYLAAP RGACYGADHD 

       550        560        570        580        590        600 
LGRLHPRVMA SLRAQSPIPN LYLTGQDIFT CGLVGALQGA LLCSSAILKR NLYSDLKDLG 

       610 
SRIQAQKKKN

Q64FG0 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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