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Q92781

- RDH1_HUMAN

UniProt

Q92781 - RDH1_HUMAN

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Protein

11-cis retinol dehydrogenase

Gene

RDH5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

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

Enzyme regulationi

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.1 Publication

pH dependencei

Optimum pH is 7.5-8.0 for 9-cis retinol dehydrogenase activity.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei163 – 1631SubstrateBy similarity
Active sitei175 – 1751Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi32 – 5625NADPBy similarityAdd
BLAST

GO - Molecular functioni

  1. retinol dehydrogenase activity Source: ProtInc

GO - Biological processi

  1. phototransduction, visible light Source: Reactome
  2. retinoid metabolic process Source: Reactome
  3. retinol metabolic process Source: UniProtKB-UniPathway
  4. visual perception Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Sensory transduction, Vision

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciMetaCyc:HS06003-MONOMER.
BRENDAi1.1.1.105. 2681.
ReactomeiREACT_160156. The canonical retinoid cycle in rods (twilight vision).
UniPathwayiUPA00912.

Names & Taxonomyi

Protein namesi
Recommended name:
11-cis retinol dehydrogenase (EC:1.1.1.315)
Short name:
11-cis RDH
Short name:
11-cis RoDH
Alternative name(s):
9-cis retinol dehydrogenase
Short name:
9cRDH
Gene namesi
Name:RDH5
Synonyms:RDH1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:9940. RDH5.

Subcellular locationi

Membrane 1 Publication; Peripheral membrane protein 1 Publication. Endoplasmic reticulum lumen 1 Publication

GO - Cellular componenti

  1. cell body Source: Ensembl
  2. endoplasmic reticulum lumen Source: Ensembl
  3. endoplasmic reticulum membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Retinitis punctata albescens (RPA) [MIM:136880]: Rare form of stationary night blindness characterized by a delay in the regeneration of cone and rod photopigments.7 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti35 – 351G → S in RPA; decreased stability. 1 Publication
VAR_016814
Natural varianti73 – 731S → F in RPA; decreased stability; loss of enzymatic activity; accumulates in the perinuclear region. 1 Publication
VAR_009273
Natural varianti105 – 1051L → I in RPA; decreased stability.
VAR_068716
Natural varianti107 – 1071G → R in RPA; associated with macular dystrophy. 2 Publications
VAR_016815
Natural varianti128 – 1281D → N in RPA; decreased stability.
VAR_068717
Natural varianti132 – 1321V → M in RPA. 1 Publication
Corresponds to variant rs62638187 [ dbSNP | Ensembl ].
VAR_016816
Natural varianti157 – 1571R → W in RPA; decreased stability.
VAR_068718
Natural varianti164 – 1641V → F in RPA. 1 Publication
VAR_016817
Natural varianti177 – 1771V → G in RPA. 1 Publication
VAR_016818
Natural varianti238 – 2381G → W in RPA; decreased stability; loss of enzymatic activity; accumulates in the perinuclear region. 2 Publications
Corresponds to variant rs62638191 [ dbSNP | Ensembl ].
VAR_009274
Natural varianti264 – 2641V → G in RPA; decreased stability.
VAR_068719
Natural varianti267 – 2671C → W in RPA. 1 Publication
VAR_016819
Natural varianti280 – 2801R → H in RPA; decreased stability; loss of enzymatic activity. 3 Publications
VAR_016820
Natural varianti281 – 2811Y → H in RPA. 1 Publication
VAR_016821
Natural varianti294 – 2941A → P in RPA; associated with H-280; no effect on enzymatic activity; accumulates in the perinuclear region. 1 Publication
VAR_016822
Natural varianti310 – 3101L → EV in RPA; loss of enzymatic activity; accumulates in the perinuclear region.
VAR_016823

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi136880. phenotype.
Orphaneti227796. Fundus albipunctatus.
52427. Retinitis punctata albescens.
PharmGKBiPA34308.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 31829511-cis retinol dehydrogenasePRO_0000054758Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi160 – 1601N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ92781.
PRIDEiQ92781.

PTM databases

PhosphoSiteiQ92781.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

BgeeiQ92781.
CleanExiHS_RDH5.
ExpressionAtlasiQ92781. baseline.
GenevestigatoriQ92781.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi111892. 6 interactions.
STRINGi9606.ENSP00000257895.

Structurei

3D structure databases

ProteinModelPortaliQ92781.
SMRiQ92781. Positions 25-273.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG1028.
GeneTreeiENSGT00770000120485.
HOVERGENiHBG005482.
InParanoidiQ92781.
KOiK00061.
OMAiGPTPWLT.
PhylomeDBiQ92781.
TreeFamiTF325617.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q92781-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MWLPLLLGAL LWAVLWLLRD RQSLPASNAF VFITGCDSGF GRLLALQLDQ
60 70 80 90 100
RGFRVLASCL TPSGAEDLQR VASSRLHTTL LDITDPQSVQ QAAKWVEMHV
110 120 130 140 150
KEAGLFGLVN NAGVAGIIGP TPWLTRDDFQ RVLNVNTMGP IGVTLALLPL
160 170 180 190 200
LQQARGRVIN ITSVLGRLAA NGGGYCVSKF GLEAFSDSLR RDVAHFGIRV
210 220 230 240 250
SIVEPGFFRT PVTNLESLEK TLQACWARLP PATQAHYGGA FLTKYLKMQQ
260 270 280 290 300
RIMNLICDPD LTKVSRCLEH ALTARHPRTR YSPGWDAKLL WLPASYLPAS
310
LVDAVLTWVL PKPAQAVY
Length:318
Mass (Da):34,979
Last modified:February 1, 1997 - v1
Checksum:i2CE24343F2EEA4B7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 301F → L in AAH28298. (PubMed:15489334)Curated
Sequence conflicti51 – 522RG → KS in AAB93668. (PubMed:9115228)Curated
Sequence conflicti75 – 773RLH → GFN in AAB93668. (PubMed:9115228)Curated
Sequence conflicti89 – 891V → F in AAB93668. (PubMed:9115228)Curated
Sequence conflicti200 – 2001V → E in AAB93668. (PubMed:9115228)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti21 – 211R → Q.
Corresponds to variant rs3138143 [ dbSNP | Ensembl ].
VAR_052321
Natural varianti33 – 331I → V.1 Publication
Corresponds to variant rs62638195 [ dbSNP | Ensembl ].
VAR_009272
Natural varianti35 – 351G → S in RPA; decreased stability. 1 Publication
VAR_016814
Natural varianti70 – 701R → G.1 Publication
Corresponds to variant rs1058635 [ dbSNP | Ensembl ].
VAR_052322
Natural varianti73 – 731S → F in RPA; decreased stability; loss of enzymatic activity; accumulates in the perinuclear region. 1 Publication
VAR_009273
Natural varianti105 – 1051L → I in RPA; decreased stability.
VAR_068716
Natural varianti107 – 1071G → R in RPA; associated with macular dystrophy. 2 Publications
VAR_016815
Natural varianti128 – 1281D → N in RPA; decreased stability.
VAR_068717
Natural varianti132 – 1321V → M in RPA. 1 Publication
Corresponds to variant rs62638187 [ dbSNP | Ensembl ].
VAR_016816
Natural varianti157 – 1571R → W in RPA; decreased stability.
VAR_068718
Natural varianti164 – 1641V → F in RPA. 1 Publication
VAR_016817
Natural varianti177 – 1771V → G in RPA. 1 Publication
VAR_016818
Natural varianti238 – 2381G → W in RPA; decreased stability; loss of enzymatic activity; accumulates in the perinuclear region. 2 Publications
Corresponds to variant rs62638191 [ dbSNP | Ensembl ].
VAR_009274
Natural varianti264 – 2641V → G in RPA; decreased stability.
VAR_068719
Natural varianti267 – 2671C → W in RPA. 1 Publication
VAR_016819
Natural varianti280 – 2801R → H in RPA; decreased stability; loss of enzymatic activity. 3 Publications
VAR_016820
Natural varianti281 – 2811Y → H in RPA. 1 Publication
VAR_016821
Natural varianti294 – 2941A → P in RPA; associated with H-280; no effect on enzymatic activity; accumulates in the perinuclear region. 1 Publication
VAR_016822
Natural varianti310 – 3101L → EV in RPA; loss of enzymatic activity; accumulates in the perinuclear region.
VAR_016823

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43559 mRNA. Translation: AAC50725.1.
U89717 mRNA. Translation: AAB93668.1.
AF037062 Genomic DNA. Translation: AAC09250.1.
BC028298 mRNA. Translation: AAH28298.1.
CCDSiCCDS31829.1.
RefSeqiNP_001186700.1. NM_001199771.1.
NP_002896.2. NM_002905.3.
UniGeneiHs.600940.

Genome annotation databases

EnsembliENST00000257895; ENSP00000257895; ENSG00000135437.
ENST00000548082; ENSP00000447128; ENSG00000135437.
GeneIDi5959.
KEGGihsa:5959.
UCSCiuc001shk.3. human.

Polymorphism databases

DMDMi2492753.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Mutations of the RDH5 gene

Retina International's Scientific Newsletter

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43559 mRNA. Translation: AAC50725.1 .
U89717 mRNA. Translation: AAB93668.1 .
AF037062 Genomic DNA. Translation: AAC09250.1 .
BC028298 mRNA. Translation: AAH28298.1 .
CCDSi CCDS31829.1.
RefSeqi NP_001186700.1. NM_001199771.1.
NP_002896.2. NM_002905.3.
UniGenei Hs.600940.

3D structure databases

ProteinModelPortali Q92781.
SMRi Q92781. Positions 25-273.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111892. 6 interactions.
STRINGi 9606.ENSP00000257895.

Chemistry

DrugBanki DB00162. Vitamin A.

PTM databases

PhosphoSitei Q92781.

Polymorphism databases

DMDMi 2492753.

Proteomic databases

PaxDbi Q92781.
PRIDEi Q92781.

Protocols and materials databases

DNASUi 5959.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000257895 ; ENSP00000257895 ; ENSG00000135437 .
ENST00000548082 ; ENSP00000447128 ; ENSG00000135437 .
GeneIDi 5959.
KEGGi hsa:5959.
UCSCi uc001shk.3. human.

Organism-specific databases

CTDi 5959.
GeneCardsi GC12P056132.
HGNCi HGNC:9940. RDH5.
MIMi 136880. phenotype.
601617. gene.
neXtProti NX_Q92781.
Orphaneti 227796. Fundus albipunctatus.
52427. Retinitis punctata albescens.
PharmGKBi PA34308.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1028.
GeneTreei ENSGT00770000120485.
HOVERGENi HBG005482.
InParanoidi Q92781.
KOi K00061.
OMAi GPTPWLT.
PhylomeDBi Q92781.
TreeFami TF325617.

Enzyme and pathway databases

UniPathwayi UPA00912 .
BioCyci MetaCyc:HS06003-MONOMER.
BRENDAi 1.1.1.105. 2681.
Reactomei REACT_160156. The canonical retinoid cycle in rods (twilight vision).

Miscellaneous databases

ChiTaRSi RDH5. human.
GeneWikii RDH5.
GenomeRNAii 5959.
NextBioi 23204.
PROi Q92781.
SOURCEi Search...

Gene expression databases

Bgeei Q92781.
CleanExi HS_RDH5.
ExpressionAtlasi Q92781. baseline.
Genevestigatori Q92781.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
InterProi IPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
Pfami PF00106. adh_short. 1 hit.
[Graphical view ]
PRINTSi PR00081. GDHRDH.
PR00080. SDRFAMILY.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiRDH1_HUMAN
AccessioniPrimary (citable) accession number: Q92781
Secondary accession number(s): O00179, Q8TAI2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: November 26, 2014
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3