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UniProtKB - Q92781 (RDH1_HUMAN)

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Protein

11-cis retinol dehydrogenase

Gene

RDH5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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: retinol metabolism

This protein is involved in the pathway retinol metabolism, which is part of Cofactor metabolism.1 Publication
View all proteins of this organism that are known to be involved in the pathway retinol metabolism and in Cofactor metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei163SubstrateBy similarity1
Active sitei175Proton acceptorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi32 – 56NADPBy similarityAdd BLAST25

GO - Molecular functioni

Complete GO annotation...

GO - Biological processi

  • response to stimulus Source: UniProtKB-KW
  • retinoid metabolic process Source: Reactome
  • retinol metabolic process Source: UniProtKB-UniPathway
  • visual perception Source: ProtInc
Complete GO annotation...

Keywordsi

Molecular functionOxidoreductase
Biological processSensory transduction, Vision
LigandNAD

Enzyme and pathway databases

BioCyciMetaCyc:HS06003-MONOMER.
BRENDAi1.1.1.300. 2681.
1.1.1.315. 2681.
ReactomeiR-HSA-2453902. The canonical retinoid cycle in rods (twilight vision).
R-HSA-5365859. RA biosynthesis pathway.
UniPathwayiUPA00912.

Chemistry databases

SwissLipidsiSLP:000000797.

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
Retinol dehydrogenase 5
Short chain dehydrogenase/reductase family 9C member 5
Gene namesi
Name:RDH5
Synonyms:HSD17B9, RDH1, SDR9C5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:9940. RDH5.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Fundus albipunctatus (FALBI)10 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of fleck retina disease characterized by discrete uniform white dots over the entire fundus with greatest density in the mid-periphery and no macular involvement. Night blindness occurs. Inheritance can be autosomal dominant or autosomal recessive.
See also OMIM:136880
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01681435G → S in FALBI; decreased stability. 2 PublicationsCorresponds to variant dbSNP:rs759359491Ensembl.1
Natural variantiVAR_00927373S → F in FALBI; decreased stability; loss of enzymatic activity; accumulates in the perinuclear region. 2 PublicationsCorresponds to variant dbSNP:rs62638185Ensembl.1
Natural variantiVAR_068716105L → I in FALBI; decreased stability. 1 Publication1
Natural variantiVAR_016815107G → R in FALBI; associated with macular dystrophy. 2 Publications1
Natural variantiVAR_068717128D → N in FALBI; decreased stability. 1 PublicationCorresponds to variant dbSNP:rs377029071Ensembl.1
Natural variantiVAR_016816132V → M in FALBI. 1 PublicationCorresponds to variant dbSNP:rs62638187Ensembl.1
Natural variantiVAR_068718157R → W in FALBI; decreased stability. 1 PublicationCorresponds to variant dbSNP:rs104894374Ensembl.1
Natural variantiVAR_016817164V → F in FALBI. 1 Publication1
Natural variantiVAR_075309175Y → F in FALBI. 1 PublicationCorresponds to variant dbSNP:rs758411232Ensembl.1
Natural variantiVAR_016818177V → G in FALBI. 1 PublicationCorresponds to variant dbSNP:rs104894373Ensembl.1
Natural variantiVAR_009274238G → W in FALBI; decreased stability; loss of enzymatic activity; accumulates in the perinuclear region. 3 PublicationsCorresponds to variant dbSNP:rs62638191Ensembl.1
Natural variantiVAR_068719264V → G in FALBI; decreased stability. 2 Publications1
Natural variantiVAR_016819267C → W in FALBI. 1 Publication1
Natural variantiVAR_016820280R → H in FALBI; decreased stability; loss of enzymatic activity. 4 PublicationsCorresponds to variant dbSNP:rs62638193Ensembl.1
Natural variantiVAR_016821281Y → H in FALBI. 1 PublicationCorresponds to variant dbSNP:rs62638194Ensembl.1
Natural variantiVAR_016822294A → P in FALBI; no effect on enzymatic activity; accumulates in the perinuclear region. 2 PublicationsCorresponds to variant dbSNP:rs111033593Ensembl.1
Natural variantiVAR_016823310L → EV in FALBI; loss of enzymatic activity; accumulates in the perinuclear region. 2 Publications1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi5959.
MalaCardsiRDH5.
MIMi136880. phenotype.
OpenTargetsiENSG00000135437.
Orphaneti227796. Fundus albipunctatus.
52427. Retinitis punctata albescens.
PharmGKBiPA34308.

Chemistry databases

DrugBankiDB00157. NADH.
DB00162. Vitamin A.

Polymorphism and mutation databases

BioMutaiRDH5.
DMDMi2492753.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Sequence analysisAdd BLAST23
ChainiPRO_000005475824 – 31811-cis retinol dehydrogenaseAdd BLAST295

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi160N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ92781.
PeptideAtlasiQ92781.
PRIDEiQ92781.

PTM databases

iPTMnetiQ92781.
PhosphoSitePlusiQ92781.

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

BgeeiENSG00000135437.
CleanExiHS_RDH5.
ExpressionAtlasiQ92781. baseline and differential.
GenevisibleiQ92781. HS.

Organism-specific databases

HPAiHPA063345.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi111892. 7 interactors.
IntActiQ92781. 1 interactor.
STRINGi9606.ENSP00000257895.

Structurei

3D structure databases

ProteinModelPortaliQ92781.
SMRiQ92781.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1610. Eukaryota.
ENOG410Y7FK. LUCA.
GeneTreeiENSGT00880000137848.
HOVERGENiHBG005482.
InParanoidiQ92781.
KOiK00061.
OMAiIIGPTPW.
OrthoDBiEOG091G0LMI.
PhylomeDBiQ92781.
TreeFamiTF325617.

Family and domain databases

InterProiView protein in InterPro
IPR016040. NAD(P)-bd_dom.
IPR032968. RDH5.
IPR002347. SDR_fam.
PANTHERiPTHR43313:SF5. PTHR43313:SF5. 1 hit.
PfamiView protein in Pfam
PF00106. adh_short. 1 hit.
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.

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)DescriptionActionsGraphical viewLength
Sequence conflicti30F → L in AAH28298 (PubMed:15489334).Curated1
Sequence conflicti51 – 52RG → KS in AAB93668 (PubMed:9115228).Curated2
Sequence conflicti75 – 77RLH → GFN in AAB93668 (PubMed:9115228).Curated3
Sequence conflicti89V → F in AAB93668 (PubMed:9115228).Curated1
Sequence conflicti200V → E in AAB93668 (PubMed:9115228).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05232121R → Q. Corresponds to variant dbSNP:rs3138143Ensembl.1
Natural variantiVAR_00927233I → V1 PublicationCorresponds to variant dbSNP:rs62638195Ensembl.1
Natural variantiVAR_01681435G → S in FALBI; decreased stability. 2 PublicationsCorresponds to variant dbSNP:rs759359491Ensembl.1
Natural variantiVAR_05232270R → G1 PublicationCorresponds to variant dbSNP:rs1058635Ensembl.1
Natural variantiVAR_00927373S → F in FALBI; decreased stability; loss of enzymatic activity; accumulates in the perinuclear region. 2 PublicationsCorresponds to variant dbSNP:rs62638185Ensembl.1
Natural variantiVAR_068716105L → I in FALBI; decreased stability. 1 Publication1
Natural variantiVAR_016815107G → R in FALBI; associated with macular dystrophy. 2 Publications1
Natural variantiVAR_068717128D → N in FALBI; decreased stability. 1 PublicationCorresponds to variant dbSNP:rs377029071Ensembl.1
Natural variantiVAR_016816132V → M in FALBI. 1 PublicationCorresponds to variant dbSNP:rs62638187Ensembl.1
Natural variantiVAR_068718157R → W in FALBI; decreased stability. 1 PublicationCorresponds to variant dbSNP:rs104894374Ensembl.1
Natural variantiVAR_016817164V → F in FALBI. 1 Publication1
Natural variantiVAR_075309175Y → F in FALBI. 1 PublicationCorresponds to variant dbSNP:rs758411232Ensembl.1
Natural variantiVAR_016818177V → G in FALBI. 1 PublicationCorresponds to variant dbSNP:rs104894373Ensembl.1
Natural variantiVAR_009274238G → W in FALBI; decreased stability; loss of enzymatic activity; accumulates in the perinuclear region. 3 PublicationsCorresponds to variant dbSNP:rs62638191Ensembl.1
Natural variantiVAR_068719264V → G in FALBI; decreased stability. 2 Publications1
Natural variantiVAR_016819267C → W in FALBI. 1 Publication1
Natural variantiVAR_016820280R → H in FALBI; decreased stability; loss of enzymatic activity. 4 PublicationsCorresponds to variant dbSNP:rs62638193Ensembl.1
Natural variantiVAR_016821281Y → H in FALBI. 1 PublicationCorresponds to variant dbSNP:rs62638194Ensembl.1
Natural variantiVAR_016822294A → P in FALBI; no effect on enzymatic activity; accumulates in the perinuclear region. 2 PublicationsCorresponds to variant dbSNP:rs111033593Ensembl.1
Natural variantiVAR_016823310L → EV in FALBI; loss of enzymatic activity; accumulates in the perinuclear region. 2 Publications1

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.4. human.

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.
CCDSiCCDS31829.1.
RefSeqiNP_001186700.1. NM_001199771.1.
NP_002896.2. NM_002905.3.
UniGeneiHs.600940.

3D structure databases

ProteinModelPortaliQ92781.
SMRiQ92781.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111892. 7 interactors.
IntActiQ92781. 1 interactor.
STRINGi9606.ENSP00000257895.

Chemistry databases

DrugBankiDB00157. NADH.
DB00162. Vitamin A.
SwissLipidsiSLP:000000797.

PTM databases

iPTMnetiQ92781.
PhosphoSitePlusiQ92781.

Polymorphism and mutation databases

BioMutaiRDH5.
DMDMi2492753.

Proteomic databases

PaxDbiQ92781.
PeptideAtlasiQ92781.
PRIDEiQ92781.

Protocols and materials databases

DNASUi5959.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000257895; ENSP00000257895; ENSG00000135437.
ENST00000548082; ENSP00000447128; ENSG00000135437.
GeneIDi5959.
KEGGihsa:5959.
UCSCiuc001shk.4. human.

Organism-specific databases

CTDi5959.
DisGeNETi5959.
GeneCardsiRDH5.
HGNCiHGNC:9940. RDH5.
HPAiHPA063345.
MalaCardsiRDH5.
MIMi136880. phenotype.
601617. gene.
neXtProtiNX_Q92781.
OpenTargetsiENSG00000135437.
Orphaneti227796. Fundus albipunctatus.
52427. Retinitis punctata albescens.
PharmGKBiPA34308.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1610. Eukaryota.
ENOG410Y7FK. LUCA.
GeneTreeiENSGT00880000137848.
HOVERGENiHBG005482.
InParanoidiQ92781.
KOiK00061.
OMAiIIGPTPW.
OrthoDBiEOG091G0LMI.
PhylomeDBiQ92781.
TreeFamiTF325617.

Enzyme and pathway databases

UniPathwayiUPA00912.
BioCyciMetaCyc:HS06003-MONOMER.
BRENDAi1.1.1.300. 2681.
1.1.1.315. 2681.
ReactomeiR-HSA-2453902. The canonical retinoid cycle in rods (twilight vision).
R-HSA-5365859. RA biosynthesis pathway.

Miscellaneous databases

ChiTaRSiRDH5. human.
GeneWikiiRDH5.
GenomeRNAii5959.
PROiPR:Q92781.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000135437.
CleanExiHS_RDH5.
ExpressionAtlasiQ92781. baseline and differential.
GenevisibleiQ92781. HS.

Family and domain databases

InterProiView protein in InterPro
IPR016040. NAD(P)-bd_dom.
IPR032968. RDH5.
IPR002347. SDR_fam.
PANTHERiPTHR43313:SF5. PTHR43313:SF5. 1 hit.
PfamiView protein in Pfam
PF00106. adh_short. 1 hit.
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRDH1_HUMAN
AccessioniPrimary (citable) accession number: Q92781
Secondary accession number(s): O00179, Q8TAI2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: June 7, 2017
This is version 159 of the entry and version 1 of the sequence. See 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.