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Protein

Retinol dehydrogenase 16

Gene

RDH16

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
    Binding sitei164SubstrateBy similarity1
    Active sitei176Proton acceptorPROSITE-ProRule annotation1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi33 – 57NADBy similarityAdd BLAST25

    GO - Molecular functioni

    • electron transfer activity Source: UniProtKB
    • retinol dehydrogenase activity Source: Reactome

    GO - Biological processi

    • lipid metabolic process Source: ProtInc

    Keywordsi

    Molecular functionOxidoreductase
    LigandNAD

    Enzyme and pathway databases

    BioCyciMetaCyc:ENSG00000139547-MONOMER
    BRENDAi1.1.1.105 2681
    ReactomeiR-HSA-2453902 The canonical retinoid cycle in rods (twilight vision)
    R-HSA-5365859 RA biosynthesis pathway
    SABIO-RKO75452

    Chemistry databases

    SwissLipidsiSLP:000000801

    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
    Proteomesi
    • UP000005640 Componenti: Chromosome 12

    Organism-specific databases

    EuPathDBiHostDB:ENSG00000139547.7
    HGNCiHGNC:29674 RDH16
    neXtProtiNX_O75452

    Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Topology

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Topological domaini1 – 288CytoplasmicSequence analysisAdd BLAST288
    Transmembranei289 – 309Helical; Anchor for type IV membrane proteinSequence analysisAdd BLAST21
    Topological domaini310 – 317LumenalSequence analysis8

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Microsome

    Pathology & Biotechi

    Organism-specific databases

    DisGeNETi8608
    OpenTargetsiENSG00000139547
    PharmGKBiPA142671089

    Polymorphism and mutation databases

    BioMutaiRDH16

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00003076931 – 317Retinol dehydrogenase 16Add BLAST317

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei189PhosphoserineBy similarity1

    Post-translational modificationi

    Not N-glycosylated.

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiO75452
    PeptideAtlasiO75452
    PRIDEiO75452

    PTM databases

    iPTMnetiO75452
    PhosphoSitePlusiO75452

    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

    BgeeiENSG00000139547
    CleanExiHS_RDH16
    GenevisibleiO75452 HS

    Organism-specific databases

    HPAiHPA038518

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000381206

    Structurei

    3D structure databases

    ProteinModelPortaliO75452
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiKOG1610 Eukaryota
    ENOG410Y7FK LUCA
    GeneTreeiENSGT00910000144025
    HOVERGENiHBG005482
    InParanoidiO75452
    KOiK11154
    OMAiVDAIMYW
    OrthoDBiEOG091G0LMI
    PhylomeDBiO75452
    TreeFamiTF325617

    Family and domain databases

    InterProiView protein in InterPro
    IPR036291 NAD(P)-bd_dom_sf
    IPR020904 Sc_DH/Rdtase_CS
    IPR002347 SDR_fam
    PfamiView protein in Pfam
    PF00106 adh_short, 1 hit
    PRINTSiPR00081 GDHRDH
    PR00080 SDRFAMILY
    SUPFAMiSSF51735 SSF51735, 1 hit
    PROSITEiView protein in PROSITE
    PS00061 ADH_SHORT, 1 hit

    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)DescriptionActionsGraphical viewLength
    Sequence conflicti130 – 131FV → LL in AAC72923 (PubMed:10329026).Curated2
    Sequence conflicti147S → N in AAC72923 (PubMed:10329026).Curated1
    Sequence conflicti154R → K in AAC39922 (PubMed:9677409).Curated1
    Sequence conflicti163S → F in AAC72923 (PubMed:10329026).Curated1

    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_003708.4
    UniGeneiHs.134958

    Genome annotation databases

    EnsembliENST00000398138; ENSP00000381206; ENSG00000139547
    GeneIDi8608
    KEGGihsa:8608
    UCSCiuc001smi.6 human

    Similar proteinsi

    Entry informationi

    Entry nameiRDH16_HUMAN
    AccessioniPrimary (citable) accession number: O75452
    Secondary accession number(s): Q9UNV2
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 23, 2007
    Last sequence update: October 23, 2007
    Last modified: March 28, 2018
    This is version 129 of the entry and version 2 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

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