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Protein

Retinol dehydrogenase 16

Gene

RDH16

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

Functioni

Oxidoreductase with a preference for NAD. Oxidizes all-trans-retinol and 13-cis-retinol to the corresponding aldehydes. Has higher activity towards CRBP-bound retinol than with free retinol. Oxidizes 3-alpha-hydroxysteroids. Oxidizes androstanediol and androsterone to dihydrotestosterone and androstanedione. Can also catalyze the reverse reaction.3 Publications

Enzyme regulationi

Inhibited by citral, perillyl alcohol, geraniol, farnesol and geranyl geraniol.1 Publication

Kineticsi

  1. KM=0.14 µM for androsterone1 Publication
  2. KM=0.22 µM for androstanediol1 Publication
  3. KM=0.80 µM for dihydrotestosterone1 Publication
  4. KM=0.13 µM for NAD1 Publication
  5. KM=190 µM for NADP1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei164 – 1641SubstrateBy similarity
    Active sitei176 – 1761Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi33 – 5725NADBy similarityAdd
    BLAST

    GO - Molecular functioni

    • electron carrier activity Source: UniProtKB
    • retinol dehydrogenase activity Source: ProtInc

    GO - Biological processi

    • lipid metabolic process Source: ProtInc
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciMetaCyc:ENSG00000139547-MONOMER.
    BRENDAi1.1.1.105. 2681.
    ReactomeiREACT_160156. The canonical retinoid cycle in rods (twilight vision).
    REACT_268561. RA biosynthesis pathway.
    SABIO-RKO75452.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Retinol dehydrogenase 16 (EC:1.1.-.-)
    Alternative name(s):
    Microsomal NAD(+)-dependent retinol dehydrogenase 4
    Short name:
    RoDH-4
    Short chain dehydrogenase/reductase family 9C member 8
    Sterol/retinol dehydrogenase
    Gene namesi
    Name:RDH16
    Synonyms:RODH4, SDR9C8
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:29674. RDH16.

    Subcellular locationi

    Topology

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 288288CytoplasmicSequence AnalysisAdd
    BLAST
    Transmembranei289 – 30921Helical; Anchor for type IV membrane proteinSequence AnalysisAdd
    BLAST
    Topological domaini310 – 3178LumenalSequence Analysis

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Microsome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA142671089.

    Polymorphism and mutation databases

    BioMutaiRDH16.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 317317Retinol dehydrogenase 16PRO_0000307693Add
    BLAST

    Post-translational modificationi

    Not N-glycosylated.

    Proteomic databases

    PaxDbiO75452.
    PRIDEiO75452.

    PTM databases

    PhosphoSiteiO75452.

    Expressioni

    Tissue specificityi

    Highly expressed in adult liver (at protein level). Detected in endometrium, liver and foreskin. Detected in the spineous layers of adult skin, and at lower levels in basal and granular skin layers. Detected in fetal liver and lung.3 Publications

    Inductioni

    Transiently up-regulated by retinoic acid.1 Publication

    Gene expression databases

    BgeeiO75452.
    CleanExiHS_RDH16.
    GenevisibleiO75452. HS.

    Organism-specific databases

    HPAiHPA038518.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000381206.

    Structurei

    3D structure databases

    ProteinModelPortaliO75452.
    SMRiO75452. Positions 32-281.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1028.
    GeneTreeiENSGT00800000124016.
    HOVERGENiHBG005482.
    InParanoidiO75452.
    KOiK11154.
    OMAiKSFLEIW.
    OrthoDBiEOG7FXZZX.
    PhylomeDBiO75452.
    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.
    IPR020904. Sc_DH/Rdtase_CS.
    [Graphical view]
    PfamiPF00106. adh_short. 1 hit.
    [Graphical view]
    PRINTSiPR00081. GDHRDH.
    PR00080. SDRFAMILY.
    PROSITEiPS00061. ADH_SHORT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O75452-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MWLYLAVFVG LYYLLHWYRE RQVLSHLRDK YVFITGCDSG FGKLLARQLD
    60 70 80 90 100
    ARGLRVLAAC LTEKGAEQLR GQTSDRLETV TLDVTKTESV AAAAQWVKEC
    110 120 130 140 150
    VRDKGLWGLV NNAGISLPTA PNELLTKQDF VTILDVNLLG VIDVTLSLLP
    160 170 180 190 200
    LVRRARGRVV NVSSVMGRVS LFGGGYCISK YGVEAFSDSL RRELSYFGVK
    210 220 230 240 250
    VAMIEPGYFK TAVTSKERFL KSFLEIWDRS SPEVKEAYGE KFVADYKKSA
    260 270 280 290 300
    EQMEQKCTQD LSLVTNCMEH ALIACHPRTR YSAGWDAKLL YLPMSYMPTF
    310
    LVDAIMYWVS PSPAKAL
    Length:317
    Mass (Da):35,673
    Last modified:October 23, 2007 - v2
    Checksum:iF9208C22B0515CFD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti130 – 1312FV → LL in AAC72923 (PubMed:10329026).Curated
    Sequence conflicti147 – 1471S → N in AAC72923 (PubMed:10329026).Curated
    Sequence conflicti154 – 1541R → K in AAC39922 (PubMed:9677409).Curated
    Sequence conflicti163 – 1631S → F in AAC72923 (PubMed:10329026).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF057034 mRNA. Translation: AAC39922.1.
    AF086735 mRNA. Translation: AAC72923.1.
    CCDSiCCDS41797.1.
    RefSeqiNP_003699.3. NM_003708.3.
    UniGeneiHs.134958.

    Genome annotation databases

    EnsembliENST00000398138; ENSP00000381206; ENSG00000139547.
    GeneIDi8608.
    KEGGihsa:8608.
    UCSCiuc001smi.4. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF057034 mRNA. Translation: AAC39922.1.
    AF086735 mRNA. Translation: AAC72923.1.
    CCDSiCCDS41797.1.
    RefSeqiNP_003699.3. NM_003708.3.
    UniGeneiHs.134958.

    3D structure databases

    ProteinModelPortaliO75452.
    SMRiO75452. Positions 32-281.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi9606.ENSP00000381206.

    PTM databases

    PhosphoSiteiO75452.

    Polymorphism and mutation databases

    BioMutaiRDH16.

    Proteomic databases

    PaxDbiO75452.
    PRIDEiO75452.

    Protocols and materials databases

    DNASUi8608.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000398138; ENSP00000381206; ENSG00000139547.
    GeneIDi8608.
    KEGGihsa:8608.
    UCSCiuc001smi.4. human.

    Organism-specific databases

    CTDi8608.
    GeneCardsiGC12M057346.
    H-InvDBHIX0036688.
    HGNCiHGNC:29674. RDH16.
    HPAiHPA038518.
    neXtProtiNX_O75452.
    PharmGKBiPA142671089.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG1028.
    GeneTreeiENSGT00800000124016.
    HOVERGENiHBG005482.
    InParanoidiO75452.
    KOiK11154.
    OMAiKSFLEIW.
    OrthoDBiEOG7FXZZX.
    PhylomeDBiO75452.
    TreeFamiTF325617.

    Enzyme and pathway databases

    BioCyciMetaCyc:ENSG00000139547-MONOMER.
    BRENDAi1.1.1.105. 2681.
    ReactomeiREACT_160156. The canonical retinoid cycle in rods (twilight vision).
    REACT_268561. RA biosynthesis pathway.
    SABIO-RKO75452.

    Miscellaneous databases

    GenomeRNAii8608.
    NextBioi32255.
    PROiO75452.

    Gene expression databases

    BgeeiO75452.
    CleanExiHS_RDH16.
    GenevisibleiO75452. HS.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR002198. DH_sc/Rdtase_SDR.
    IPR002347. Glc/ribitol_DH.
    IPR016040. NAD(P)-bd_dom.
    IPR020904. Sc_DH/Rdtase_CS.
    [Graphical view]
    PfamiPF00106. adh_short. 1 hit.
    [Graphical view]
    PRINTSiPR00081. GDHRDH.
    PR00080. SDRFAMILY.
    PROSITEiPS00061. ADH_SHORT. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "cDNA cloning and characterization of a new human microsomal NAD+-dependent dehydrogenase that oxidizes all-trans-retinol and 3alpha-hydroxysteroids."
      Gough W.H., VanOoteghem S., Sint T., Kedishvili N.Y.
      J. Biol. Chem. 273:19778-19785(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Liver.
    2. "Cloning and characterization of retinol dehydrogenase transcripts expressed in human epidermal keratinocytes."
      Jurukovski V., Markova N.G., Karaman-Jurukovska N., Randolph R.K., Su J., Napoli J.L., Simon M.
      Mol. Genet. Metab. 67:62-73(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INDUCTION, TISSUE SPECIFICITY.
      Tissue: Keratinocyte.
    3. "Expression of a retinol dehydrogenase (hRoDH-4), a member of the retinol/steroid dehydrogenase family implicated in retinoic acid biosynthesis, in normal and neoplastic endometria."
      Cain J.M., Zaino R., Shearer D., Bennett R.A., Olt G., Weisz J.
      Am. J. Obstet. Gynecol. 186:675-683(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    4. "Differential recognition of the free versus bound retinol by human microsomal retinol/sterol dehydrogenases: characterization of the holo-CRBP dehydrogenase activity of RoDH-4."
      Lapshina E.A., Belyaeva O.V., Chumakova O.V., Kedishvili N.Y.
      Biochemistry 42:776-784(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, LACK OF GLYCOSYLATION, SUBCELLULAR LOCATION.
    5. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiRDH16_HUMAN
    AccessioniPrimary (citable) accession number: O75452
    Secondary accession number(s): Q9UNV2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 23, 2007
    Last sequence update: October 23, 2007
    Last modified: July 22, 2015
    This is version 105 of the entry and version 2 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    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 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.