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Q92781 (RDH1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·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
Short name=9cRDH
Gene names
Name:RDH5
Synonyms:RDH1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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.5

Catalytic activity

11-cis-retinol-[retinal-binding-protein] + NAD+ = 11-cis-retinal-[retinol-binding-protein] + NADH. Ref.2 Ref.5

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.5

Pathway

Cofactor metabolism; retinol metabolism. Ref.2

Subunit structure

Homodimer. Ref.6

Subcellular location

Membrane; Peripheral membrane protein. Endoplasmic reticulum lumen Ref.6.

Tissue specificity

Abundant in the retinal pigment epithelium. Expressed at high levels in mammary tissue, kidney and testis, and at lower levels in liver, heart, adrenal gland, lung, pancreas and skeletal muscle. Ref.2

Involvement in disease

Retinitis punctata albescens (RPA) [MIM:136880]: Rare form of stationary night blindness characterized by a delay in the regeneration of cone and rod photopigments.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13

Sequence similarities

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

Biophysicochemical properties

pH dependence:

Optimum pH is 7.5-8.0 for 9-cis retinol dehydrogenase activity. Ref.2

Ontologies

Keywords
   Biological processSensory transduction
Vision
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainSignal
   LigandNAD
   Molecular functionOxidoreductase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processphototransduction, visible light

Traceable author statement. Source: Reactome

retinoid metabolic process

Traceable author statement. Source: Reactome

retinol metabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

visual perception

Traceable author statement Ref.8. Source: ProtInc

   Cellular_componentcell body

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

   Molecular_functionretinol dehydrogenase activity

Traceable author statement Ref.2. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 31829511-cis retinol dehydrogenase
PRO_0000054758

Regions

Nucleotide binding32 – 5625NADP By similarity

Sites

Active site1751Proton acceptor By similarity
Binding site1631Substrate By similarity

Amino acid modifications

Glycosylation1601N-linked (GlcNAc...) Potential

Natural variations

Natural variant211R → Q.
Corresponds to variant rs3138143 [ dbSNP | Ensembl ].
VAR_052321
Natural variant331I → V. Ref.8
Corresponds to variant rs62638195 [ dbSNP | Ensembl ].
VAR_009272
Natural variant351G → S in RPA; decreased stability. Ref.6 Ref.10
VAR_016814
Natural variant701R → G. Ref.2
Corresponds to variant rs1058635 [ dbSNP | Ensembl ].
VAR_052322
Natural variant731S → F in RPA; decreased stability; loss of enzymatic activity; accumulates in the perinuclear region. Ref.6 Ref.8
VAR_009273
Natural variant1051L → I in RPA; decreased stability. Ref.6
VAR_068716
Natural variant1071G → R in RPA; associated with macular dystrophy. Ref.10 Ref.12
VAR_016815
Natural variant1281D → N in RPA; decreased stability. Ref.6
VAR_068717
Natural variant1321V → M in RPA. Ref.10
Corresponds to variant rs62638187 [ dbSNP | Ensembl ].
VAR_016816
Natural variant1571R → W in RPA; decreased stability. Ref.6
VAR_068718
Natural variant1641V → F in RPA. Ref.13
VAR_016817
Natural variant1771V → G in RPA. Ref.9
VAR_016818
Natural variant2381G → W in RPA; decreased stability; loss of enzymatic activity; accumulates in the perinuclear region. Ref.6 Ref.7 Ref.8
Corresponds to variant rs62638191 [ dbSNP | Ensembl ].
VAR_009274
Natural variant2641V → G in RPA; decreased stability. Ref.6
VAR_068719
Natural variant2671C → W in RPA. Ref.11
VAR_016819
Natural variant2801R → H in RPA; decreased stability; loss of enzymatic activity. Ref.6 Ref.7 Ref.9 Ref.10
VAR_016820
Natural variant2811Y → H in RPA. Ref.10
VAR_016821
Natural variant2941A → P in RPA; associated with H-280; no effect on enzymatic activity; accumulates in the perinuclear region. Ref.6 Ref.7
VAR_016822
Natural variant3101L → EV in RPA; loss of enzymatic activity; accumulates in the perinuclear region.
VAR_016823

Experimental info

Sequence conflict301F → L in AAH28298. Ref.4
Sequence conflict51 – 522RG → KS in AAB93668. Ref.2
Sequence conflict75 – 773RLH → GFN in AAB93668. Ref.2
Sequence conflict891V → F in AAB93668. Ref.2
Sequence conflict2001V → E in AAB93668. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q92781 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 2CE24343F2EEA4B7

FASTA31834,979
        10         20         30         40         50         60 
MWLPLLLGAL LWAVLWLLRD RQSLPASNAF VFITGCDSGF GRLLALQLDQ RGFRVLASCL 

        70         80         90        100        110        120 
TPSGAEDLQR VASSRLHTTL LDITDPQSVQ QAAKWVEMHV KEAGLFGLVN NAGVAGIIGP 

       130        140        150        160        170        180 
TPWLTRDDFQ RVLNVNTMGP IGVTLALLPL LQQARGRVIN ITSVLGRLAA NGGGYCVSKF 

       190        200        210        220        230        240 
GLEAFSDSLR RDVAHFGIRV SIVEPGFFRT PVTNLESLEK TLQACWARLP PATQAHYGGA 

       250        260        270        280        290        300 
FLTKYLKMQQ RIMNLICDPD LTKVSRCLEH ALTARHPRTR YSPGWDAKLL WLPASYLPAS 

       310 
LVDAVLTWVL PKPAQAVY 

« Hide

References

« Hide 'large scale' references
[1]"Primary structure of human 11-cis retinol dehydrogenase and organization and chromosomal localization of the corresponding gene."
Simon A., Lagercrantz J., Bajalica-Lagercrantz S., Eriksson U.
Genomics 36:424-430(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Identification and characterization of a stereospecific human enzyme that catalyzes 9-cis-retinol oxidation. A possible role in 9-cis-retinoic acid formation."
Mertz J.R., Shang E., Piantedosi R., Wei S., Wolgemuth D.J., Blaner W.S.
J. Biol. Chem. 272:11744-11749(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, VARIANT GLY-70.
Tissue: Mammary gland.
[3]"Retinol dehydrogenase: complete genomic sequence and its relationship to retinitis pigmentosa."
Gu S., Jablonka S., Gal A.
Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Blood.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[5]"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: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION.
[6]"Biochemical defects in 11-cis-retinol dehydrogenase mutants associated with fundus albipunctatus."
Liden M., Romert A., Tryggvason K., Persson B., Eriksson U.
J. Biol. Chem. 276:49251-49257(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS RPA SER-35; PHE-73; ILE-105; ASN-128; TRP-157; TRP-238; GLY-264; HIS-280; PRO-294 AND 309-GLU-VAL-310 DELINS.
[7]"11-cis retinol dehydrogenase mutations as a major cause of the congenital night-blindness disorder known as fundus albipunctatus."
Gonzalez-Fernandez F., Kurz D., Bao Y., Newman S., Conway B.P., Young J.E., Han D.P., Khani S.C.
Mol. Vis. 5:41-41(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RPA TRP-238; HIS-280 AND PRO-294.
[8]"Mutations in the gene encoding 11-cis retinol dehydrogenase cause delayed dark adaptation and fundus albipunctatus."
Yamamoto H., Simon A., Eriksson U., Harris E., Berson E.L., Dryja T.P.
Nat. Genet. 22:188-191(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RPA PHE-73 AND TRP-238, VARIANT VAL-33.
[9]"A novel compound heterozygous mutation in the RDH5 gene in a patient with fundus albipunctatus."
Kuroiwa S., Kikuchi T., Yoshimura N.
Am. J. Ophthalmol. 130:672-675(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RPA GLY-177 AND HIS-280.
[10]"A high association with cone dystrophy in Fundus albipunctatus caused by mutations of the RDH5 gene."
Nakamura M., Hotta Y., Tanikawa A., Terasaki H., Miyake Y.
Invest. Ophthalmol. Vis. Sci. 41:3925-3932(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RPA SER-35; ARG-107; MET-132; HIS-280; HIS-281 AND 309-GLU-VAL-310 DELINS.
[11]"Null mutation in the human 11-cis retinol dehydrogenase gene associated with fundus albipunctatus."
Driessen C.A., Janssen B.P., Winkens H.J., Kuhlmann L.D., Van Vugt A.H., Pinckers A.J., Deutman A.F., Janssen J.J.
Ophthalmology 108:1479-1484(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT RPA TRP-267.
[12]"Macular dystrophy in a Japanese family with fundus albipunctatus."
Hotta K., Nakamura M., Kondo M., Ito S., Terasaki H., Miyake Y., Hida T.
Am. J. Ophthalmol. 135:917-919(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT RPA ARG-107.
[13]"A novel RDH5 gene mutation in a patient with fundus albipunctatus presenting with macular atrophy and fading white dots."
Yamamoto H., Yakushijin K., Kusuhara S., Escano M.F., Nagai A., Negi A.
Am. J. Ophthalmol. 136:572-574(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT RPA PHE-164.
+Additional computationally mapped references.

Web resources

Mutations of the RDH5 gene

Retina International's Scientific Newsletter

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U43559 mRNA. Translation: AAC50725.1.
U89717 mRNA. Translation: AAB93668.1.
AF037062 Genomic DNA. Translation: AAC09250.1.
BC028298 mRNA. Translation: AAH28298.1.
CCDSCCDS31829.1.
RefSeqNP_001186700.1. NM_001199771.1.
NP_002896.2. NM_002905.3.
UniGeneHs.600940.

3D structure databases

ProteinModelPortalQ92781.
SMRQ92781. Positions 25-273.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111892. 2 interactions.
STRING9606.ENSP00000257895.

Chemistry

DrugBankDB00157. NADH.
DB00162. Vitamin A.

PTM databases

PhosphoSiteQ92781.

Polymorphism databases

DMDM2492753.

Proteomic databases

PaxDbQ92781.
PRIDEQ92781.

Protocols and materials databases

DNASU5959.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000257895; ENSP00000257895; ENSG00000135437.
ENST00000548082; ENSP00000447128; ENSG00000135437.
GeneID5959.
KEGGhsa:5959.
UCSCuc001shk.3. human.

Organism-specific databases

CTD5959.
GeneCardsGC12P056121.
HGNCHGNC:9940. RDH5.
MIM136880. phenotype.
601617. gene.
neXtProtNX_Q92781.
Orphanet227796. Fundus albipunctatus.
52427. Retinitis punctata albescens.
PharmGKBPA34308.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1028.
HOVERGENHBG005482.
InParanoidQ92781.
KOK00061.
OMAGPTPWLT.
PhylomeDBQ92781.
TreeFamTF325617.

Enzyme and pathway databases

BioCycMetaCyc:HS06003-MONOMER.
BRENDA1.1.1.105. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
UniPathwayUPA00912.

Gene expression databases

BgeeQ92781.
CleanExHS_RDH5.
GenevestigatorQ92781.

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

ChiTaRSRDH5. human.
GeneWikiRDH5.
GenomeRNAi5959.
NextBio23204.
PROQ92781.
SOURCESearch...

Entry information

Entry nameRDH1_HUMAN
AccessionPrimary (citable) accession number: Q92781
Secondary accession number(s): O00179, Q8TAI2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: July 9, 2014
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM