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Entry version 138 (11 Dec 2019)
Sequence version 1 (01 Nov 1996)
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Protein

NADPH-dependent oxidoreductase 2-alkenal reductase

Gene

AER

Organism
Arabidopsis thaliana (Mouse-ear cress)
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

Involved in the detoxification of reactive carbonyls (PubMed:10848984, PubMed:12514241, PubMed:16299173). Acts on lipid peroxide-derived reactive aldehydes (PubMed:12514241). Specific to a double bond activated by an adjacent carbonyl group (PubMed:12514241). Can use both quinones and diamide as substrates, but not menadione, ferricyanide or phylloquinone (PubMed:10848984). Can use 4-hydroxy-(2E)-nonenal (HNE), 4-hydroxy-(2E)-hexenal (HHE), (2E)-nonenal, (2E)-hexenal, (2E)-pentenal, propenal (acrolein), 3-buten-2-one and 3-penten-2-one, but not (R)---carvone, n-nonanal, n-hexanal, (3Z)-hexanal, cyclohex-2-en-1-one or 12-oxo phytodienoic acid (OPDA) as electron acceptors (PubMed:12514241). Catalyzes the reduction of the alpha,beta-unsaturated bond of 2-alkenals, of lipid peroxide-derived oxenes 9-oxo-10(E),12(Z)-octadecadienoic acid (9-KODE) and 13-oxo-9(Z),11(E)-octadecadienoic acid (13-KODE), as well as 4-oxo-(2E)-nonenal and 4-hydroxynonenal (PubMed:16299173). Can use 12-oxo-10(E) dodecanoate (traumatin), trans-1,3 diphenyl-2-propenone, trans-1,4-diphenyl-2-butene-1,4-dione, 9-oxo-12,13-epoxy-(10E)-octadecenoic acid (trans-EKODE-1b) and 9,13-dihydroxy-10-oxo-11-octadecenoic acid as substrates (PubMed:26678323). Catalyzes the reduction of the 7-8 double bond of phenylpropanal substrates, such as p-coumaryl aldehyde and coniferyl aldehyde (in vitro) (PubMed:17028190). Has activity towards toxic substrates, such as 4-hydroxy-(2E)-nonenal (in vitro) (PubMed:17028190). May play a distinct role in plant antioxidant defense and is possibly involved in NAD(P)/NAD(P)H homeostasis (PubMed:17028190).5 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by N-ethylmaleimide and p-chloromercuribenzoic acid.1 Publication

<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 3.8 sec(-1) for trans-1,3 diphenyl-2-propenone. kcat is 4.9 sec(-1) for trans-1,4-diphenyl-2-butene-1,4-dione. kcat is 10 sec(-1) for traumatin (PubMed:26678323). kcat is 98 sec(-1) for 9,10-phenanthrenequinone. kcat is 1.9 sec(-1) for 5-Hydroxy-1,4-naphtoquinone. kcat is 12 sec(-1) for 1,4-Benzoquinone. kcat is 0.10 sec(-1) for decyl-plastoquinone. kcat is 0.03 sec(-1) for ferricytochrome c. kcat is 95 sec(-1) for azodicarboxylic acid bis[dimethylamide]. kcat is 42 sec(-1) for 1,10-(azocarbonyl)-dipeperidine. kcat is 31 sec(-1) for azocarbonamide (PubMed:10848984). kcat is 88 sec(-1) for 4-hydroxy-(2E)-nonenal. kcat is 42 sec(-1) for 4-hydroxy-(2E)-hexenal. kcat is 51 sec(-1) for (2E)-nonenal. kcat is 63 sec(-1) for (2E)-hexenal. kcat is 35 sec(-1) for (2E)-pentenal. kcat is 40 sec(-1) for propenal. kcat is 83 sec(-1) for 3-buten-2-one. kcat is 103 sec(-1) for 3-penten-2-one (PubMed:12514241). kcat is 33.9 sec(-1) for (2E),(6Z)-nonadienal. kcat is 20.1 sec(-1) for 4-oxo-(2E)-nonenal. kcat is 0.94 sec(-1) for 9-oxo-10(E),12(Z)-octadecadienoic acid. kcat is 1.10 sec(-1) for 13-oxo-9(Z),11(E)-octadecadienoic acid. kcat is 18.9 sec(-1) for 3-nonen-2-one (PubMed:16299173).4 Publications
  1. KM=0.53 mM for p-coumaryl aldehyde1 Publication
  2. KM=0.41 mM for coniferyl aldehyde1 Publication
  3. KM=0.28 mM for 4-hydroxy-(2E)-nonenal1 Publication
  4. KM=10 µM for trans-1,3 diphenyl-2-propenone1 Publication
  5. KM=3.7 µM for trans-1,4-diphenyl-2-butene-1,4-dione1 Publication
  6. KM=6.6 µM for traumatin1 Publication
  7. KM=0.65 µM for 9,10-phenanthrenequinone1 Publication
  8. KM=11 µM for 5-Hydroxy-1,4-naphtoquinone1 Publication
  9. KM=152 µM for 1,4-Benzoquinone1 Publication
  10. KM=25 µM for decyl-plastoquinone1 Publication
  11. KM=20 µM for ferricytochrome c1 Publication
  12. KM=128 µM for azodicarboxylic acid bis[dimethylamide]1 Publication
  13. KM=120 µM for 1,10-(azocarbonyl)-dipeperidine1 Publication
  14. KM=3.4 µM for azocarbonamide1 Publication
  15. KM=2.5 µM for NADPH for 9,10-phenanthrenequinone-reduction1 Publication
  16. KM=8.2 µM for NADPH for azodicarboxylic acid bis[dimethylamide]-reduction1 Publication
  17. KM=13.4 µM for 4-hydroxy-(2E)-nonenal1 Publication
  18. KM=145 µM for 4-hydroxy-(2E)-hexenal1 Publication
  19. KM=5.9 µM for (2E)-nonenal1 Publication
  20. KM=232 µM for (2E)-hexenal1 Publication
  21. KM=1420 µM for (2E)-pentenal1 Publication
  22. KM=4650 µM for propenal1 Publication
  23. KM=55 µM for 3-buten-2-one1 Publication
  24. KM=5.2 µM for 3-penten-2-one1 Publication
  25. KM=11.3 µM for (2E),(6Z)-nonadienal1 Publication
  26. KM=1.24 µM for 4-oxo-(2E)-nonenal1 Publication
  27. KM=10.0 µM for 9-oxo-10(E),12(Z)-octadecadienoic acid1 Publication
  28. KM=3.92 µM for 13-oxo-9(Z),11(E)-octadecadienoic acid1 Publication
  29. KM=0.673 µM for 3-nonen-2-one1 Publication

    pH dependencei

    Optimum pH is 8.0 for 9,10-phenanthrenequinone-reduction. Optimum pH is 6.5-7.0 for azodicarboxylic acid bis[dimethylamide]-reduction (PubMed:10848984). Optimum pH is 6.0 with (2E)-hexenal or 4-hydroxy-(2E)-nonenal as substrate (PubMed:12514241).2 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei53SubstrateCombined sources1
    Binding sitei188NADP; via amide nitrogenCombined sources1
    Binding sitei192NADPCombined sources1
    Binding sitei208NADPCombined sources1
    Binding sitei232NADP; via carbonyl oxygenCombined sources1
    Binding sitei254NADPCombined sources1
    Binding sitei260NADPCombined sources1
    Binding sitei260SubstrateCombined sources1
    Binding sitei330NADP; via carbonyl oxygenCombined sources1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi52 – 53NADPCombined sources2
    Nucleotide bindingi163 – 169NADPCombined sources7
    Nucleotide bindingi284 – 286NADPCombined sources3
    Nucleotide bindingi334 – 336NADPCombined sources3

    <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
    LigandNADP

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    ARA:AT5G16970-MONOMER
    MetaCyc:AT5G16970-MONOMER

    <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_and_taxonomy_section">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:
    NADPH-dependent oxidoreductase 2-alkenal reductase1 Publication (EC:1.3.1.-1 Publication, EC:1.3.1.744 Publications)
    Short name:
    AtAER1 Publication
    Alternative name(s):
    NADP-dependent alkenal double bond reductase P11 Publication
    Short name:
    DBR11 Publication
    NADPH-azodicarbonyl/quinone reductase1 Publication
    NADPH:2-alkenal/one alpha,beta-hydrogenase1 Publication
    Short name:
    ALH1 Publication
    P1-zeta-crystallin protein1 Publication
    Short name:
    P1-ZCr1 Publication
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:AER1 Publication
    Synonyms:P11 Publication
    Ordered Locus Names:At5g16970Imported
    ORF Names:F2K13_120Imported
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiArabidopsis thaliana (Mouse-ear cress)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri3702 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
    • UP000006548 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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 5

    Organism-specific databases

    Arabidopsis Information Portal

    More...
    Araporti
    AT5G16970

    The Arabidopsis Information Resource

    More...
    TAIRi
    locus:2148131 AT5G16970

    <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 Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    <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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002180731 – 345NADPH-dependent oxidoreductase 2-alkenal reductaseAdd BLAST345

    Proteomic databases

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

    More...
    PaxDbi
    Q39172

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q39172

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    Q39172

    <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

    Expressed in leaves.1 Publication

    <p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Up-regulated upon treatment with paraquat, t-butylhydroperoxide, diamide, and menadione.1 Publication

    Gene expression databases

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    Q39172 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    Q39172 AT

    <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_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homodimer.

    2 Publications

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    16836, 2 interactors

    Protein interaction database and analysis system

    More...
    IntActi
    Q39172, 1 interactor

    STRING: functional protein association networks

    More...
    STRINGi
    3702.AT5G16970.1

    <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

    Secondary structure

    1345
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

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

    More...
    SMRi
    Q39172

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    Q39172

    <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
    KOG1196 Eukaryota
    COG2130 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000294663

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q39172

    KEGG Orthology (KO)

    More...
    KOi
    K08070

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    IVAWEEY

    Database of Orthologous Groups

    More...
    OrthoDBi
    884151at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    Q39172

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR013149 ADH_C
    IPR041694 ADH_N_2
    IPR011032 GroES-like_sf
    IPR036291 NAD(P)-bd_dom_sf
    IPR020843 PKS_ER

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF16884 ADH_N_2, 1 hit
    PF00107 ADH_zinc_N, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00829 PKS_ER, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF50129 SSF50129, 2 hits
    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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

    Q39172-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MTATNKQVIL KDYVSGFPTE SDFDFTTTTV ELRVPEGTNS VLVKNLYLSC
    60 70 80 90 100
    DPYMRIRMGK PDPSTAALAQ AYTPGQPIQG YGVSRIIESG HPDYKKGDLL
    110 120 130 140 150
    WGIVAWEEYS VITPMTHAHF KIQHTDVPLS YYTGLLGMPG MTAYAGFYEV
    160 170 180 190 200
    CSPKEGETVY VSAASGAVGQ LVGQLAKMMG CYVVGSAGSK EKVDLLKTKF
    210 220 230 240 250
    GFDDAFNYKE ESDLTAALKR CFPNGIDIYF ENVGGKMLDA VLVNMNMHGR
    260 270 280 290 300
    IAVCGMISQY NLENQEGVHN LSNIIYKRIR IQGFVVSDFY DKYSKFLEFV
    310 320 330 340
    LPHIREGKIT YVEDVADGLE KAPEALVGLF HGKNVGKQVV VVARE
    Length:345
    Mass (Da):38,134
    Last modified:November 1, 1996 - v1
    <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:i5AFCEBB2948B2680
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti223P → T in AAM53276 (PubMed:14593172).Curated1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    Z49768 mRNA Translation: CAA89838.1
    AL391141 Genomic DNA Translation: CAC01710.1
    CP002688 Genomic DNA Translation: AED92364.1
    AY120718 mRNA Translation: AAM53276.1
    BT022058 mRNA Translation: AAY25470.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S57611

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_197199.1, NM_121703.4

    Genome annotation databases

    Ensembl plant genome annotation project

    More...
    EnsemblPlantsi
    AT5G16970.1; AT5G16970.1; AT5G16970

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    831560

    Gramene; a comparative resource for plants

    More...
    Gramenei
    AT5G16970.1; AT5G16970.1; AT5G16970

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ath:AT5G16970

    <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
    Z49768 mRNA Translation: CAA89838.1
    AL391141 Genomic DNA Translation: CAC01710.1
    CP002688 Genomic DNA Translation: AED92364.1
    AY120718 mRNA Translation: AAM53276.1
    BT022058 mRNA Translation: AAY25470.1
    PIRiS57611
    RefSeqiNP_197199.1, NM_121703.4

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2J3HX-ray2.50A/B1-345[»]
    2J3IX-ray2.80A/B1-345[»]
    2J3JX-ray2.80A/B1-345[»]
    2J3KX-ray2.80A/B1-345[»]
    SMRiQ39172
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGridi16836, 2 interactors
    IntActiQ39172, 1 interactor
    STRINGi3702.AT5G16970.1

    PTM databases

    iPTMnetiQ39172

    Proteomic databases

    PaxDbiQ39172
    PRIDEiQ39172

    Protocols and materials databases

    The DNASU plasmid repository

    More...
    DNASUi
    831560

    Genome annotation databases

    EnsemblPlantsiAT5G16970.1; AT5G16970.1; AT5G16970
    GeneIDi831560
    GrameneiAT5G16970.1; AT5G16970.1; AT5G16970
    KEGGiath:AT5G16970

    Organism-specific databases

    AraportiAT5G16970
    TAIRilocus:2148131 AT5G16970

    Phylogenomic databases

    eggNOGiKOG1196 Eukaryota
    COG2130 LUCA
    HOGENOMiHOG000294663
    InParanoidiQ39172
    KOiK08070
    OMAiIVAWEEY
    OrthoDBi884151at2759
    PhylomeDBiQ39172

    Enzyme and pathway databases

    BioCyciARA:AT5G16970-MONOMER
    MetaCyc:AT5G16970-MONOMER

    Miscellaneous databases

    EvolutionaryTraceiQ39172

    Protein Ontology

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    PROi
    PR:Q39172

    Gene expression databases

    ExpressionAtlasiQ39172 baseline and differential
    GenevisibleiQ39172 AT

    Family and domain databases

    InterProiView protein in InterPro
    IPR013149 ADH_C
    IPR041694 ADH_N_2
    IPR011032 GroES-like_sf
    IPR036291 NAD(P)-bd_dom_sf
    IPR020843 PKS_ER
    PfamiView protein in Pfam
    PF16884 ADH_N_2, 1 hit
    PF00107 ADH_zinc_N, 1 hit
    SMARTiView protein in SMART
    SM00829 PKS_ER, 1 hit
    SUPFAMiSSF50129 SSF50129, 2 hits
    SSF51735 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 nameiAER_ARATH
    <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: Q39172
    Secondary accession number(s): Q501A9, Q8L865
    <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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: December 11, 2019
    This is version 138 of the entry and version 1 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 programPlant Protein Annotation Program

    <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

    3D-structure, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
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