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O55240 (RDH1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
11-cis retinol dehydrogenase

Short name=11-cis RDH
Short name=11-cis RoDH
EC=1.1.1.315
Alternative name(s):
9-cis retinol dehydrogenase
Cis-retinol dehydrogenase
Retinol dehydrogenase 5
Gene names
Name:Rdh5
Synonyms:cRDH, rdh, RDH4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length318 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Stereospecific 11-cis retinol dehydrogenase, which catalyzes the final step in the biosynthesis of 11-cis retinaldehyde, the universal chromophore of visual pigments. Also able to oxidize 9-cis-retinol and 13-cis-retinol, but not all-trans-retinol. Active in the presence of NAD as cofactor but not in the presence of NADP. Ref.2 Ref.3

Catalytic activity

11-cis-retinol-[retinal-binding-protein] + NAD+ = 11-cis-retinal-[retinol-binding-protein] + NADH. Ref.2 Ref.3

Enzyme regulation

Inhibited by 9-cis-, 13-cis- and all-trans-retinoic acids, with the most potent inhibitor being 13-cis-retinoic acid. Weakly inhibited by oleic acid. Ref.3

Pathway

Cofactor metabolism; retinol metabolism. Ref.2

Subcellular location

Membrane; Peripheral membrane protein By similarity. Endoplasmic reticulum lumen Ref.8 UniProtKB Q27979.

Tissue specificity

Expressed in eye, liver, kidney, brain, intestine, placenta, epididymus and submaxillary gland. In eye, strongly expressed in the retinal pigment epithelium, with lower expression levels detected in the inner segment of the photoreceptor cells and in the outer plexiform layer. In kidney, strong expression detected in the distal tubules and the transitional epithelium in the renal pelvis, with weaker expression detected in the epithelium of the outer stripe of the outer zone of the medulla. In liver, detected in hepatocytes in the centrilobular area. In lung, present in Clara cells in the epithelium of the bronchiole, in parenchyma and in cartilage surrounding the secondary bronchi. In skin, expressed in epidermis, hair follicles and mast cells in the dermis. Expressed in heart (Ref.3 and Ref.8). Not detected in heart (Ref.2). Not detected in lung, spleen, skeletal muscle and testis. Ref.1 Ref.2 Ref.3 Ref.8

Developmental stage

Abundantly expressed during embryonic development, especially in the developing central nervous system and sensory organs, cranial and spinal ganglia and endoderm of foregut and hindgut. At E10, detected along the entire neural tube, the mid- and hindbrain floor, the central canal of the brain vesicles, spinal cord, lung mesenchyme, the trabecular layer of the heart ventricles, endoderm and endodermally-derived structures such as tracheal epithelium and liver. At E11, expressed in the brain vesicles, along the spinal cord, myotome, migrating muscle progenitor cells in the body wall, cells of the genital ridge, spinal ganglion, liver, cerebellar primordium, basal cells of the neuroepithelium of the mesenchephalic flexure, collections of cells in the pons, Rathke's pouch, spinal and cranial ganglia and the floor plate, retina, lens, optic stalks and the neural crest-derived mesenchyme in the anterior eye segment. During eye development, expression restricted to the retinal pigment epithelium of the posterior hemisphere at E18, with expression levels increasing postnatally to P16. Ref.2 Ref.8

Disruption phenotype

Mutant mice develop normally and are fertile. No abnormalities can be found in the retinal structure, rhodopsin content and fundus appearance of their eyes. Mice display a mild visual phenotype of impaired dark adaptation and accumulation of 11-cis- and 13-cis-retinols and 11-cis- and 13-cis-retinyl esters in the eyes. Ref.9

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Ontologies

Keywords
   Biological processSensory transduction
Vision
   Cellular componentEndoplasmic reticulum
Membrane
   DomainSignal
   LigandNAD
   Molecular functionOxidoreductase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processresponse to stimulus

Inferred from electronic annotation. Source: UniProtKB-KW

retinol metabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

visual perception

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcell body

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum lumen

Inferred from direct assay PubMed 16223484. Source: MGI

membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionoxidoreductase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 31829511-cis retinol dehydrogenase
PRO_0000419633

Regions

Nucleotide binding32 – 5625NADP By similarity

Sites

Active site1751Proton acceptor By similarity
Binding site1631Substrate By similarity

Amino acid modifications

Glycosylation1601N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
O55240 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: AA8DB76CD0BF7DFC

FASTA31834,826
        10         20         30         40         50         60 
MWLPLLLGAL LWAVLWLLRD RQSLPASDAF IFITGCDSGF GRLLALQLDQ KGFQVLAGCL 

        70         80         90        100        110        120 
TPSGAEDLQQ MASSRLHTTL LDITDPQNVQ QVAKWVKTRV GETGLFGLVN NAGVAGIIGP 

       130        140        150        160        170        180 
TPWLTQDDFQ RVLSVNTLGP IGVTLALLPL LQQARGRVVN ITSVLGRIAA NGGGYCVSKF 

       190        200        210        220        230        240 
GLEAFSDSLR RDMAPFGVQV SIVEPGFFRT PVTNLESLES TLKACWARLP PAIQAHYGEA 

       250        260        270        280        290        300 
FLDTYLRVQR RIMNLICDPE LTKVTSCLEH ALTARHPRTR YSPGWDAKLL WLPASYLPAR 

       310 
VVDAVLTWIL PRPAQSVS 

« Hide

References

« Hide 'large scale' references
[1]"The visual cycle retinol dehydrogenase: possible involvement in the 9-cis retinoic acid biosynthetic pathway."
Driessen C.A., Winkens H.J., Kuhlmann E.D., Janssen A.P., van Vugt A.H., Deutman A.F., Janssen J.J.
FEBS Lett. 428:135-140(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
Strain: 129/SvJ.
Tissue: Liver.
[2]"The identification of a 9-cis retinol dehydrogenase in the mouse embryo reveals a pathway for synthesis of 9-cis retinoic acid."
Romert A., Tuvendal P., Simon A., Dencker L., Eriksson U.
Proc. Natl. Acad. Sci. U.S.A. 95:4404-4409(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Tissue: Liver.
[3]"Biochemical properties, tissue expression, and gene structure of a short chain dehydrogenase/reductase able to catalyze cis-retinol oxidation."
Gamble M.V., Shang E., Zott R.P., Mertz J.R., Wolgemuth D.J., Blaner W.S.
J. Lipid Res. 40:2279-2292(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, TISSUE SPECIFICITY.
Strain: 129/SvJ, BALB/c and C57BL/6J.
Tissue: Kidney and Liver.
[4]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Cerebellum.
[5]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[6]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Kidney.
[8]"Gene structure, expression analysis, and membrane topology of RDH4."
Romert A., Tuvendal P., Tryggvason K., Dencker L., Eriksson U.
Exp. Cell Res. 256:338-345(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[9]"Disruption of the 11-cis-retinol dehydrogenase gene leads to accumulation of cis-retinols and cis-retinyl esters."
Driessen C.A., Winkens H.J., Hoffmann K., Kuhlmann L.D., Janssen B.P., Van Vugt A.H., Van Hooser J.P., Wieringa B.E., Deutman A.F., Palczewski K., Ruether K., Janssen J.J.
Mol. Cell. Biol. 20:4275-4287(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X97752 Genomic DNA. Translation: CAA66347.1.
AF013288 mRNA. Translation: AAC25951.1.
AF033195 mRNA. Translation: AAC00491.1.
AF033196 mRNA. Translation: AAC00492.1.
AK135139 mRNA. Translation: BAE22435.1.
AC122380 Genomic DNA. No translation available.
CH466578 Genomic DNA. Translation: EDL24632.1.
BC021372 mRNA. Translation: AAH21372.1.
CCDSCCDS24298.1.
RefSeqNP_598767.1. NM_134006.4.
XP_006513450.1. XM_006513387.1.
UniGeneMm.439856.

3D structure databases

ProteinModelPortalO55240.
SMRO55240. Positions 25-284.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEO55240.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000026406; ENSMUSP00000026406; ENSMUSG00000025350.
GeneID19682.
KEGGmmu:19682.
UCSCuc007how.1. mouse.

Organism-specific databases

CTD5959.
MGIMGI:1201412. Rdh5.

Phylogenomic databases

GeneTreeENSGT00620000087655.
HOVERGENHBG005482.
InParanoidO55240.
KOK00061.
OMAGPTPWLT.
OrthoDBEOG7FXZZX.
PhylomeDBO55240.
TreeFamTF325617.

Enzyme and pathway databases

BRENDA1.1.1.105. 244.
UniPathwayUPA00912.

Gene expression databases

BgeeO55240.
GenevestigatorO55240.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
ProtoNetSearch...

Other

NextBio297004.
PROO55240.
SOURCESearch...

Entry information

Entry nameRDH1_MOUSE
AccessionPrimary (citable) accession number: O55240
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2012
Last sequence update: June 1, 1998
Last modified: July 9, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

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