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Entry version 162 (22 Apr 2020)
Sequence version 3 (17 Oct 2006)
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Protein

Retinol dehydrogenase 12

Gene

RDH12

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

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Retinoids dehydrogenase/reductase with a clear preference for NADP. Displays high activity towards 9-cis, 11-cis and all-trans-retinal. Shows very weak activity towards 13-cis-retinol (PubMed:15865448, PubMed:12226107). Also exhibits activity, albeit with lower affinity than for retinaldehydes, towards lipid peroxidation products (C9 aldehydes) such as 4-hydroxynonenal and trans-2-nonenal (PubMed:19686838, PubMed:15865448). May play an important function in photoreceptor cells to detoxify 4-hydroxynonenal and potentially other toxic aldehyde products resulting from lipid peroxidation (PubMed:19686838). Has no dehydrogenase activity towards steroids (PubMed:15865448, PubMed:12226107).3 Publications

Miscellaneous

Shows clear specificity for the pro-S hydrogen on C4 of NADPH and the pro-R hydrogen on C15 of retinols.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 36 min(-1) for all-trans-retinal as substrate. kcat is 45 min(-1) for 11-cis-retinal as substrate. kcat is 14 min(-1) for 9-cis-retinal as substrate. kcat is 27 min(-1) for all-trans-retinol as substrate. kcat is 7 min(-1) for 11-cis-retinol as substrate. kcat is 7 min(-1) for 9-cis-retinol as substrate. kcat is 56 min(-1) for nonanal as substrate. kcat is 45 min(-1) for (Z)-non-6-enal as substrate. kcat is 28 min(-1) for (E)-non-2-enal.1 Publication
  1. KM=1.2 µM for NADPH1 Publication
  2. KM=2200 µM for NADH1 Publication
  3. KM=0.04 µM for all-trans-retinal1 Publication
  4. KM=0.10 µM for 11-cis-retinal1 Publication
  5. KM=0.14 µM for 9-cis-retinal1 Publication
  6. KM=0.16 µM for 11-cis-retinol1 Publication
  7. KM=0.16 µM for 9-cis-retinol1 Publication
  8. KM=0.4 µM for all-trans-retinol1 Publication
  9. KM=3.1 µM for nonanal1 Publication
  10. KM=20 µM for (E)-non-2-enal1 Publication
  11. KM=1 µM for (Z)-non-6-enal1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>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
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei175SubstrateBy similarity1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei200Proton acceptorBy similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi46 – 52NADPBy similarity7

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionOxidoreductase
    Biological processSensory transduction, Vision
    LigandNADP

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:ENSG00000139988-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    1.1.1.105 2681
    1.1.1.300 2681

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-HSA-2453864 Retinoid cycle disease events
    R-HSA-2453902 The canonical retinoid cycle in rods (twilight vision)

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...
    UniPathwayi
    UPA00912

    Chemistry databases

    SwissLipids knowledge resource for lipid biology

    More...
    SwissLipidsi
    SLP:000001789

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Retinol dehydrogenase 12 (EC:1.1.1.3002 Publications)
    Alternative name(s):
    All-trans and 9-cis retinol dehydrogenase
    Short chain dehydrogenase/reductase family 7C member 2
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:RDH12
    Synonyms:SDR7C2
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 14

    Organism-specific databases

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:19977 RDH12

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    608830 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_Q96NR8

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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 & Seán O’Donoghue; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    <p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

    Leber congenital amaurosis 13 (LCA13)2 Publications
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionA severe dystrophy of the retina, typically becoming evident in the first years of life. Visual function is usually poor and often accompanied by nystagmus, sluggish or near-absent pupillary responses, photophobia, high hyperopia and keratoconus.
    Related information in OMIM
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_02085849T → M in LCA13; aberrant activity in interconverting isomers of retinol and retinal; abolishes protection against the toxicity of 4-hydroxynonenal in the retina; there is differing activity profiles associated with each of the alleles of the R-161-Q polymorphism; genetic background may act as a modifier of mutation effect. 2 PublicationsCorresponds to variant dbSNP:rs28940314EnsemblClinVar.1
    Natural variantiVAR_02085951I → N in LCA13. 1 PublicationCorresponds to variant dbSNP:rs104894473EnsemblClinVar.1
    Natural variantiVAR_02086099L → I in LCA13; exhibits a profound loss of catalytic activity. 2 PublicationsCorresponds to variant dbSNP:rs28940315EnsemblClinVar.1
    Natural variantiVAR_020861151H → D in LCA13; exhibits a profound loss of catalytic activity. 2 PublicationsCorresponds to variant dbSNP:rs104894475EnsemblClinVar.1
    Natural variantiVAR_020862151H → N in LCA13. 1 PublicationCorresponds to variant dbSNP:rs104894475EnsemblClinVar.1
    Natural variantiVAR_020863175S → P in LCA13. 1 PublicationCorresponds to variant dbSNP:rs104894472EnsemblClinVar.1
    Natural variantiVAR_020864226Y → C in LCA13; diminished activity in interconverting isomers of retinol and retinal. 1 PublicationCorresponds to variant dbSNP:rs28940313EnsemblClinVar.1
    Natural variantiVAR_020865230P → A in LCA13. 1 PublicationCorresponds to variant dbSNP:rs104894476EnsemblClinVar.1
    Retinitis pigmentosa 53 (RP53)3 Publications
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionA retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. RP53 inheritance is autosomal dominant or autosomal recessive.
    Related information in OMIM
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_06416676G → R in RP53. 1 PublicationCorresponds to variant dbSNP:rs368489658Ensembl.1
    Natural variantiVAR_064169126A → V in RP53. 1 PublicationCorresponds to variant dbSNP:rs202126574EnsemblClinVar.1
    Natural variantiVAR_081222146V → D in RP53; early onset; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs116649873Ensembl.1

    Keywords - Diseasei

    Disease mutation, Leber congenital amaurosis, Retinitis pigmentosa

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    145226

    GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

    More...
    GeneReviewsi
    RDH12

    MalaCards human disease database

    More...
    MalaCardsi
    RDH12
    MIMi612712 phenotype

    Open Targets

    More...
    OpenTargetsi
    ENSG00000139988

    Orphanet; a database dedicated to information on rare diseases and orphan drugs

    More...
    Orphaneti
    65 Leber congenital amaurosis
    791 Retinitis pigmentosa

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA134864793

    Miscellaneous databases

    Pharos NIH Druggable Genome Knowledgebase

    More...
    Pharosi
    Q96NR8 Tbio

    Chemistry databases

    Drug and drug target database

    More...
    DrugBanki
    DB00162 Vitamin A

    DrugCentral

    More...
    DrugCentrali
    Q96NR8

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    RDH12

    Domain mapping of disease mutations (DMDM)

    More...
    DMDMi
    116242750

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000547661 – 316Retinol dehydrogenase 12Add BLAST316

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    Q96NR8

    MassIVE - Mass Spectrometry Interactive Virtual Environment

    More...
    MassIVEi
    Q96NR8

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    Q96NR8

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    Q96NR8

    PeptideAtlas

    More...
    PeptideAtlasi
    Q96NR8

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q96NR8

    ProteomicsDB: a multi-organism proteome resource

    More...
    ProteomicsDBi
    77549

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    Q96NR8

    Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

    More...
    PhosphoSitePlusi
    Q96NR8

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

    Widely expressed, mostly in retina, kidney, brain, skeletal muscle, pancreas and stomach.1 Publication

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSG00000139988 Expressed in skin of leg and 116 other tissues

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    Q96NR8 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    Q96NR8 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    ENSG00000139988 Tissue enhanced (skin)

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    Show more details

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    126895, 30 interactors

    Protein interaction database and analysis system

    More...
    IntActi
    Q96NR8, 19 interactors

    Molecular INTeraction database

    More...
    MINTi
    Q96NR8

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000449079

    Miscellaneous databases

    RNAct, Protein-RNA interaction predictions for model organisms.

    More...
    RNActi
    Q96NR8 protein

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    Q96NR8

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    <p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG1208 Eukaryota
    COG1028 LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000161505

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_010194_44_5_1

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q96NR8

    KEGG Orthology (KO)

    More...
    KOi
    K11153

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    DCKRAWV

    Database of Orthologous Groups

    More...
    OrthoDBi
    1032903at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    Q96NR8

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF105429

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR036291 NAD(P)-bd_dom_sf
    IPR002347 SDR_fam

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00106 adh_short, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00081 GDHRDH
    PR00080 SDRFAMILY

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51735 SSF51735, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    Q96NR8-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MLVTLGLLTS FFSFLYMVAP SIRKFFAGGV CRTNVQLPGK VVVITGANTG
    60 70 80 90 100
    IGKETARELA SRGARVYIAC RDVLKGESAA SEIRVDTKNS QVLVRKLDLS
    110 120 130 140 150
    DTKSIRAFAE GFLAEEKQLH ILINNAGVMM CPYSKTADGF ETHLGVNHLG
    160 170 180 190 200
    HFLLTYLLLE RLKVSAPARV VNVSSVAHHI GKIPFHDLQS EKRYSRGFAY
    210 220 230 240 250
    CHSKLANVLF TRELAKRLQG TGVTTYAVHP GVVRSELVRH SSLLCLLWRL
    260 270 280 290 300
    FSPFVKTARE GAQTSLHCAL AEGLEPLSGK YFSDCKRTWV SPRARNNKTA
    310
    ERLWNVSCEL LGIRWE
    Length:316
    Mass (Da):35,094
    Last modified:October 17, 2006 - v3
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iEA0915E1E484879B
    GO

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_06416347A → T in retinal dystrophy; exhibits a profound loss of catalytic activity. 1 PublicationCorresponds to variant dbSNP:rs761231974Ensembl.1
    Natural variantiVAR_02085849T → M in LCA13; aberrant activity in interconverting isomers of retinol and retinal; abolishes protection against the toxicity of 4-hydroxynonenal in the retina; there is differing activity profiles associated with each of the alleles of the R-161-Q polymorphism; genetic background may act as a modifier of mutation effect. 2 PublicationsCorresponds to variant dbSNP:rs28940314EnsemblClinVar.1
    Natural variantiVAR_02085951I → N in LCA13. 1 PublicationCorresponds to variant dbSNP:rs104894473EnsemblClinVar.1
    Natural variantiVAR_06416455T → M in retinal dystrophy; exhibits a profound loss of catalytic activity. 1 PublicationCorresponds to variant dbSNP:rs766631462Ensembl.1
    Natural variantiVAR_06416565R → Q1 PublicationCorresponds to variant dbSNP:rs745471670Ensembl.1
    Natural variantiVAR_06416676G → R in RP53. 1 PublicationCorresponds to variant dbSNP:rs368489658Ensembl.1
    Natural variantiVAR_06719379A → V Found in a patient with LCA13. 1 PublicationCorresponds to variant dbSNP:rs763414313Ensembl.1
    Natural variantiVAR_02086099L → I in LCA13; exhibits a profound loss of catalytic activity. 2 PublicationsCorresponds to variant dbSNP:rs28940315EnsemblClinVar.1
    Natural variantiVAR_064167101D → N1 PublicationCorresponds to variant dbSNP:rs148334092Ensembl.1
    Natural variantiVAR_064168125N → K in retinal dystrophy; exhibits a profound loss of catalytic activity. 1 Publication1
    Natural variantiVAR_064169126A → V in RP53. 1 PublicationCorresponds to variant dbSNP:rs202126574EnsemblClinVar.1
    Natural variantiVAR_064170145G → E in retinal dystrophy; exhibits a profound loss of catalytic activity. 1 PublicationCorresponds to variant dbSNP:rs907600014Ensembl.1
    Natural variantiVAR_081222146V → D in RP53; early onset; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs116649873Ensembl.1
    Natural variantiVAR_020861151H → D in LCA13; exhibits a profound loss of catalytic activity. 2 PublicationsCorresponds to variant dbSNP:rs104894475EnsemblClinVar.1
    Natural variantiVAR_020862151H → N in LCA13. 1 PublicationCorresponds to variant dbSNP:rs104894475EnsemblClinVar.1
    Natural variantiVAR_064171155T → I in retinal dystrophy; exhibits a profound loss of catalytic activity. 1 PublicationCorresponds to variant dbSNP:rs121434337EnsemblClinVar.1
    Natural variantiVAR_028281161R → Q Does not affect the protection against the toxicity of 4-hydroxynonenal in the retina. 4 PublicationsCorresponds to variant dbSNP:rs17852293EnsemblClinVar.1
    Natural variantiVAR_020863175S → P in LCA13. 1 PublicationCorresponds to variant dbSNP:rs104894472EnsemblClinVar.1
    Natural variantiVAR_064172193R → C in retinal dystrophy; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs148629905Ensembl.1
    Natural variantiVAR_064173206A → D in retinal dystrophy; exhibits a profound loss of catalytic activity. 1 Publication1
    Natural variantiVAR_064174206A → V in retinal dystrophy; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs1254096311Ensembl.1
    Natural variantiVAR_020864226Y → C in LCA13; diminished activity in interconverting isomers of retinol and retinal. 1 PublicationCorresponds to variant dbSNP:rs28940313EnsemblClinVar.1
    Natural variantiVAR_020865230P → A in LCA13. 1 PublicationCorresponds to variant dbSNP:rs104894476EnsemblClinVar.1
    Natural variantiVAR_064175230P → L in retinal dystrophy; unknown pathological significance. 1 Publication1
    Natural variantiVAR_064176234R → H in retinal dystrophy; unknown pathological significance; exhibits a loss of catalytic activity. 1 PublicationCorresponds to variant dbSNP:rs750636662EnsemblClinVar.1
    Natural variantiVAR_064177239R → W in retinal dystrophy; exhibits a profound loss of catalytic activity. 1 PublicationCorresponds to variant dbSNP:rs751589863Ensembl.1
    Natural variantiVAR_064178274L → P in retinal dystrophy; exhibits a profound loss of catalytic activity. 1 Publication1
    Natural variantiVAR_064179285C → Y in retinal dystrophy; exhibits a profound loss of catalytic activity. 1 PublicationCorresponds to variant dbSNP:rs973306929Ensembl.1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

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    EMBLi

    GenBank nucleotide sequence database

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    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    AK054835 mRNA Translation: BAB70811.1
    AK315462 mRNA Translation: BAG37849.1
    AL049779 Genomic DNA No translation available.
    CH471061 Genomic DNA Translation: EAW80951.1
    BC025724 mRNA Translation: AAH25724.1

    The Consensus CDS (CCDS) project

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    CCDSi
    CCDS9787.1

    NCBI Reference Sequences

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    RefSeqi
    NP_689656.2, NM_152443.2

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

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    Ensembli
    ENST00000267502; ENSP00000267502; ENSG00000139988
    ENST00000551171; ENSP00000449079; ENSG00000139988

    Database of genes from NCBI RefSeq genomes

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    GeneIDi
    145226

    KEGG: Kyoto Encyclopedia of Genes and Genomes

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    KEGGi
    hsa:145226

    UCSC genome browser

    More...
    UCSCi
    uc001xjz.5 human

    Keywords - Coding sequence diversityi

    Polymorphism

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AK054835 mRNA Translation: BAB70811.1
    AK315462 mRNA Translation: BAG37849.1
    AL049779 Genomic DNA No translation available.
    CH471061 Genomic DNA Translation: EAW80951.1
    BC025724 mRNA Translation: AAH25724.1
    CCDSiCCDS9787.1
    RefSeqiNP_689656.2, NM_152443.2

    3D structure databases

    SMRiQ96NR8
    ModBaseiSearch...

    Protein-protein interaction databases

    BioGridi126895, 30 interactors
    IntActiQ96NR8, 19 interactors
    MINTiQ96NR8
    STRINGi9606.ENSP00000449079

    Chemistry databases

    DrugBankiDB00162 Vitamin A
    DrugCentraliQ96NR8
    SwissLipidsiSLP:000001789

    PTM databases

    iPTMnetiQ96NR8
    PhosphoSitePlusiQ96NR8

    Polymorphism and mutation databases

    BioMutaiRDH12
    DMDMi116242750

    Proteomic databases

    jPOSTiQ96NR8
    MassIVEiQ96NR8
    MaxQBiQ96NR8
    PaxDbiQ96NR8
    PeptideAtlasiQ96NR8
    PRIDEiQ96NR8
    ProteomicsDBi77549

    Protocols and materials databases

    Antibodypedia a portal for validated antibodies

    More...
    Antibodypediai
    24894 94 antibodies

    The DNASU plasmid repository

    More...
    DNASUi
    145226

    Genome annotation databases

    EnsembliENST00000267502; ENSP00000267502; ENSG00000139988
    ENST00000551171; ENSP00000449079; ENSG00000139988
    GeneIDi145226
    KEGGihsa:145226
    UCSCiuc001xjz.5 human

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    145226
    DisGeNETi145226

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    RDH12
    GeneReviewsiRDH12
    HGNCiHGNC:19977 RDH12
    HPAiENSG00000139988 Tissue enhanced (skin)
    MalaCardsiRDH12
    MIMi608830 gene
    612712 phenotype
    neXtProtiNX_Q96NR8
    OpenTargetsiENSG00000139988
    Orphaneti65 Leber congenital amaurosis
    791 Retinitis pigmentosa
    PharmGKBiPA134864793

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiKOG1208 Eukaryota
    COG1028 LUCA
    GeneTreeiENSGT00940000161505
    HOGENOMiCLU_010194_44_5_1
    InParanoidiQ96NR8
    KOiK11153
    OMAiDCKRAWV
    OrthoDBi1032903at2759
    PhylomeDBiQ96NR8
    TreeFamiTF105429

    Enzyme and pathway databases

    UniPathwayiUPA00912
    BioCyciMetaCyc:ENSG00000139988-MONOMER
    BRENDAi1.1.1.105 2681
    1.1.1.300 2681
    ReactomeiR-HSA-2453864 Retinoid cycle disease events
    R-HSA-2453902 The canonical retinoid cycle in rods (twilight vision)

    Miscellaneous databases

    The Gene Wiki collection of pages on human genes and proteins

    More...
    GeneWikii
    RDH12

    Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

    More...
    GenomeRNAii
    145226
    PharosiQ96NR8 Tbio

    Protein Ontology

    More...
    PROi
    PR:Q96NR8
    RNActiQ96NR8 protein

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000139988 Expressed in skin of leg and 116 other tissues
    ExpressionAtlasiQ96NR8 baseline and differential
    GenevisibleiQ96NR8 HS

    Family and domain databases

    InterProiView protein in InterPro
    IPR036291 NAD(P)-bd_dom_sf
    IPR002347 SDR_fam
    PfamiView protein in Pfam
    PF00106 adh_short, 1 hit
    PRINTSiPR00081 GDHRDH
    PR00080 SDRFAMILY
    SUPFAMiSSF51735 SSF51735, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRDH12_HUMAN
    <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q96NR8
    Secondary accession number(s): B2RDA2, Q8TAW6
    <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 29, 2003
    Last sequence update: October 17, 2006
    Last modified: April 22, 2020
    This is version 162 of the entry and version 3 of the sequence. See complete history.
    <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

    <p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. Human chromosome 14
      Human chromosome 14: entries, gene names and cross-references to MIM
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