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Q92781

- RDH1_HUMAN

UniProt

Q92781 - RDH1_HUMAN

Protein

11-cis retinol dehydrogenase

Gene

RDH5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 1 (01 Feb 1997)
      Previous versions | rss
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    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

    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: UniProtKB-SubCell
    3. endoplasmic reticulum membrane Source: Reactome

    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.
    GenevestigatoriQ92781.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi111892. 2 interactions.
    STRINGi9606.ENSP00000257895.

    Structurei

    3D structure databases

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

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG1028.
    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

    MWLPLLLGAL LWAVLWLLRD RQSLPASNAF VFITGCDSGF GRLLALQLDQ    50
    RGFRVLASCL TPSGAEDLQR VASSRLHTTL LDITDPQSVQ QAAKWVEMHV 100
    KEAGLFGLVN NAGVAGIIGP TPWLTRDDFQ RVLNVNTMGP IGVTLALLPL 150
    LQQARGRVIN ITSVLGRLAA NGGGYCVSKF GLEAFSDSLR RDVAHFGIRV 200
    SIVEPGFFRT PVTNLESLEK TLQACWARLP PATQAHYGGA FLTKYLKMQQ 250
    RIMNLICDPD LTKVSRCLEH ALTARHPRTR YSPGWDAKLL WLPASYLPAS 300
    LVDAVLTWVL PKPAQAVY 318
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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. 2 interactions.
    STRINGi 9606.ENSP00000257895.

    Chemistry

    DrugBanki DB00157. NADH.
    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 GC12P056121.
    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.
    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.
    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

    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: October 1, 2014
    This is version 131 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