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Entry version 174 (16 Oct 2019)
Sequence version 2 (29 May 2007)
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Protein

Alcohol dehydrogenase class-P

Gene

ADH1

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

Alcohol dehydrogenase mostly active on ethanol (EtOH), but exhibits broad substrates selectivity for primary and secondary alcohols (e.g. butanol, propyl alcohol, pentanol, isopentanol, ethylene glycol, isopropanol, methanol and tertiary butyl alcohol) (PubMed:23707506). Converts allyl alcohol to highly toxic acryl-aldehyde (PubMed:20508152). Required for survival and acclimation in hypoxic conditions, especially in roots (PubMed:12857811, PubMed:9880346).4 Publications

Miscellaneous

Unlike most plants, Arabidopsis contains only one gene for ADH.1 Publication

<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 ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Zn2+1 PublicationNote: Binds 2 Zn2+ ions per subunit.1 Publication

<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

Alcohol dehydrogenase activity show inverse correlation with the decreasing availability of oxygen.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 328 min(-1) with NAD+ as substrate (at pH 10.5 and 25 degrees Celsius).1 Publication
  1. KM=1.65 mM for NAD+ (at pH 10.5 and 25 degrees Celsius)1 Publication
  2. KM=5.1 mM for ethanol (at pH 10.5 and 25 degrees Celsius)1 Publication
  1. Vmax=7.9 µmol/min/mg enzyme with NAD+ as substrate (at pH 10.5 and 25 degrees Celsius)1 Publication
  2. Vmax=70.1 µmol/min/mg enzyme with ethanol as substrate (at pH 10.5 and 25 degrees Celsius)1 Publication

pH dependencei

Optimum pH is 10.5 (at 25 degrees Celsius).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi47Zinc 1; catalyticCombined sources1 Publication1
Metal bindingi49Zinc 1Combined sources1 Publication1
<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 sitei49NADCombined sources1 Publication1
Binding sitei49SubstrateCombined sources1 Publication1
Metal bindingi69Zinc 1; catalyticCombined sources1 Publication1
Binding sitei69SubstrateBy similarity1
Metal bindingi99Zinc 2Combined sources1 Publication1
Metal bindingi102Zinc 2Combined sources1 Publication1
Metal bindingi105Zinc 2Combined sources1 Publication1
Metal bindingi113Zinc 2Combined sources1 Publication1
Metal bindingi177Zinc 1; catalyticCombined sources1 Publication1
Binding sitei226NADCombined sources1 Publication1
Binding sitei231NADCombined sources1 Publication1
Binding sitei272NAD; via carbonyl oxygenCombined sources1 Publication1
Binding sitei295NAD; via carbonyl oxygenCombined sources1 Publication1
Binding sitei322NAD; via amide nitrogenCombined sources1 Publication1
Binding sitei372NADCombined sources1 Publication1

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 bindingi202 – 207NADCombined sources1 Publication6
Nucleotide bindingi295 – 297NADBy similarity3

<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
LigandMetal-binding, NAD, Nucleotide-binding, Zinc

<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:
Alcohol dehydrogenase class-PCurated (EC:1.1.1.12 Publications)
Short name:
AtADH1 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:ADH11 Publication
Synonyms:ADH1 Publication
Ordered Locus Names:At1g77120Imported
ORF Names:F22K20.19Imported
<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 1

Organism-specific databases

Arabidopsis Information Portal

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Araporti
AT1G77120

The Arabidopsis Information Resource

More...
TAIRi
locus:2025237 AT1G77120

<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

<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 describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Loss of alcohol dehydrogenase activity (PubMed:3377754, PubMed:12509334). Increased resistance to allyl alcohol (PubMed:20508152). Decreased survival, associated with impaired lateral roots development, upon oxygen deprivation leading to hypoxic conditions (PubMed:12509334, PubMed:12857811). Impaired root acclimation to hypoxic stress (PubMed:9880346).5 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi105C → Y in R006; inactive enzyme. 2 Publications1

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<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_00001606972 – 379Alcohol dehydrogenase class-PAdd BLAST378

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylserineCombined sources1
Modified residuei229PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Glutathionylated.1 Publication

Keywords - PTMi

Acetylation, Glutathionylation, Phosphoprotein

Proteomic databases

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

More...
PaxDbi
P06525

PRoteomics IDEntifications database

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PRIDEi
P06525

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P06525

<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

Root specific (PubMed:9611167). Also detected in etiolated seedlings and leaves in cold conditons (PubMed:12231733).2 Publications

<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

Transactivated by MYB2 in response to various stresses (PubMed:9611167). By 2,4-dichlorophenoxyacetic acid (synthetic auxin) in Arabidopsis as well as in maize (PubMed:2937058). Induced mostly in roots and shoot apex by hypoxia during water submergence or oxygen deprivation, in a MYB2-dependent manner, and partly via an ethylene-mediated pathway (PubMed:9522467, PubMed:9611167, PubMed:11402202, PubMed:12509334, PubMed:26566261, PubMed:11987307, PubMed:8787023). Accumulates in response to hydrogen peroxide H2O2 during the early stages of hypoxia signaling (PubMed:24395201, PubMed:18441225). Decreased levels upon combined hypoxia and diphenylene iodonium chloride (DPI, an NADPH oxidase inhibitor) treatments (PubMed:24395201). Induced by abscisic acid (ABA), dehydration, estradiol, salt (NaCl), cold and sucrose treatments (PubMed:12231733, PubMed:18441225, PubMed:11987307, PubMed:9611167, PubMed:8787023). The induction by dehydration is ABA-dependent (PubMed:8787023). Observed in etiolated seedlings and leaves upon exposure to low temperature, probably via anaerobic metabolism and increase of ABA levels (PubMed:12231733). Strongly induced by caffeine (PubMed:12509334). May accumulate in roots during spaceflight, probably due to local hypoxia conditions (PubMed:11402191).1 Publication11 Publications

Gene expression databases

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P06525 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P06525 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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
29266, 2 interactors

STRING: functional protein association networks

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STRINGi
3702.AT1G77120.1

<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

1379
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

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SMRi
P06525

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
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

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eggNOGi
KOG0022 Eukaryota
COG1062 LUCA

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P06525

KEGG Orthology (KO)

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KOi
K18857

Identification of Orthologs from Complete Genome Data

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OMAi
VMHEISV

Database of Orthologous Groups

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OrthoDBi
664798at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P06525

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR013149 ADH_C
IPR013154 ADH_N
IPR002328 ADH_Zn_CS
IPR011032 GroES-like_sf
IPR036291 NAD(P)-bd_dom_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF08240 ADH_N, 1 hit
PF00107 ADH_zinc_N, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF50129 SSF50129, 2 hits
SSF51735 SSF51735, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00059 ADH_ZINC, 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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P06525-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSTTGQIIRC KAAVAWEAGK PLVIEEVEVA PPQKHEVRIK ILFTSLCHTD
60 70 80 90 100
VYFWEAKGQT PLFPRIFGHE AGGIVESVGE GVTDLQPGDH VLPIFTGECG
110 120 130 140 150
ECRHCHSEES NMCDLLRINT ERGGMIHDGE SRFSINGKPI YHFLGTSTFS
160 170 180 190 200
EYTVVHSGQV AKINPDAPLD KVCIVSCGLS TGLGATLNVA KPKKGQSVAI
210 220 230 240 250
FGLGAVGLGA AEGARIAGAS RIIGVDFNSK RFDQAKEFGV TECVNPKDHD
260 270 280 290 300
KPIQQVIAEM TDGGVDRSVE CTGSVQAMIQ AFECVHDGWG VAVLVGVPSK
310 320 330 340 350
DDAFKTHPMN FLNERTLKGT FFGNYKPKTD IPGVVEKYMN KELELEKFIT
360 370
HTVPFSEINK AFDYMLKGES IRCIITMGA
Length:379
Mass (Da):41,178
Last modified:May 29, 2007 - v2
<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:i32550529538B9669
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 conflicti154V → L in AAM65556 (Ref. 11) Curated1

Natural variant

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 varianti43F → Y in strain: cv. Hiroshima. 1 Publication1
Natural varianti51V → L in strain: cv. Bla-10, cv. Ci-0, cv. Cvi-0, cv. Hiroshima, cv. Kas-1 and cv. Ita-0. 3 Publications1
Natural varianti101E → D in strain: cv. Aa-0, cv. Al-0, cv. Bl-1, cv. Bs-0, cv. Gr-1, cv. Mt-0, cv. Shokei and cv. Yo-0. 3 Publications1
Natural varianti106H → K in strain: cv. Bl-1 and cv. Gr-1. 2 Publications1
Natural varianti106H → Q in strain: cv. Aa-0, cv. Al-0, cv. Bs-0, cv. Mt-0, cv. Shokei and cv. Yo-0. 2 Publications1
Natural varianti120T → P in strain: cv. Es-0. 1 Publication1
Natural varianti180S → A in strain: cv. Bla-10. 1 Publication1
Natural varianti197S → T in strain: cv. Cvi-0. 1 Publication1
Natural varianti217A → V in strain: cv. Kas-1. 1 Publication1

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
M12196 Genomic DNA Translation: AAA32728.1
X77943 Genomic DNA Translation: CAA54911.1
D84240 Genomic DNA Translation: BAA19615.1
D84241 Genomic DNA Translation: BAA19616.1
D84242 Genomic DNA Translation: BAA19617.1
D84243 Genomic DNA Translation: BAA19618.1
D84244 Genomic DNA Translation: BAA19619.1
D84245 Genomic DNA Translation: BAA19620.1
D84246 Genomic DNA Translation: BAA19621.1
D84247 Genomic DNA Translation: BAA19622.1
D84248 Genomic DNA Translation: BAA19623.1
D84249 Genomic DNA Translation: BAA19624.1
D63460 Genomic DNA Translation: BAA22983.1
D63461 Genomic DNA Translation: BAA22979.1
D63462 Genomic DNA Translation: BAA22980.1
D63463 Genomic DNA Translation: BAA22981.1
D63464 Genomic DNA Translation: BAA22982.1
AF110456 Genomic DNA Translation: AAF23554.1
AB048394 Genomic DNA Translation: BAB32568.1
AB048395 Genomic DNA Translation: BAB32569.1
AY536888 Genomic DNA Translation: AAS45601.2
AC002291 Genomic DNA Translation: AAC00625.1
CP002684 Genomic DNA Translation: AEE35937.1
AY045612 mRNA Translation: AAK73970.1
AY090330 mRNA Translation: AAL90991.1
AY088010 mRNA Translation: AAM65556.1
AF056557 Genomic DNA Translation: AAD41572.1

Protein sequence database of the Protein Information Resource

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PIRi
A23815 DEMUAM

NCBI Reference Sequences

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RefSeqi
NP_177837.1, NM_106362.3

Genome annotation databases

Ensembl plant genome annotation project

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EnsemblPlantsi
AT1G77120.1; AT1G77120.1; AT1G77120

Database of genes from NCBI RefSeq genomes

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GeneIDi
844047

Gramene; a comparative resource for plants

More...
Gramenei
AT1G77120.1; AT1G77120.1; AT1G77120

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ath:AT1G77120

<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
M12196 Genomic DNA Translation: AAA32728.1
X77943 Genomic DNA Translation: CAA54911.1
D84240 Genomic DNA Translation: BAA19615.1
D84241 Genomic DNA Translation: BAA19616.1
D84242 Genomic DNA Translation: BAA19617.1
D84243 Genomic DNA Translation: BAA19618.1
D84244 Genomic DNA Translation: BAA19619.1
D84245 Genomic DNA Translation: BAA19620.1
D84246 Genomic DNA Translation: BAA19621.1
D84247 Genomic DNA Translation: BAA19622.1
D84248 Genomic DNA Translation: BAA19623.1
D84249 Genomic DNA Translation: BAA19624.1
D63460 Genomic DNA Translation: BAA22983.1
D63461 Genomic DNA Translation: BAA22979.1
D63462 Genomic DNA Translation: BAA22980.1
D63463 Genomic DNA Translation: BAA22981.1
D63464 Genomic DNA Translation: BAA22982.1
AF110456 Genomic DNA Translation: AAF23554.1
AB048394 Genomic DNA Translation: BAB32568.1
AB048395 Genomic DNA Translation: BAB32569.1
AY536888 Genomic DNA Translation: AAS45601.2
AC002291 Genomic DNA Translation: AAC00625.1
CP002684 Genomic DNA Translation: AEE35937.1
AY045612 mRNA Translation: AAK73970.1
AY090330 mRNA Translation: AAL90991.1
AY088010 mRNA Translation: AAM65556.1
AF056557 Genomic DNA Translation: AAD41572.1
PIRiA23815 DEMUAM
RefSeqiNP_177837.1, NM_106362.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4RQTX-ray2.30A6-379[»]
4RQUX-ray2.50A/B6-379[»]
SMRiP06525
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi29266, 2 interactors
STRINGi3702.AT1G77120.1

PTM databases

iPTMnetiP06525

Proteomic databases

PaxDbiP06525
PRIDEiP06525

Genome annotation databases

EnsemblPlantsiAT1G77120.1; AT1G77120.1; AT1G77120
GeneIDi844047
GrameneiAT1G77120.1; AT1G77120.1; AT1G77120
KEGGiath:AT1G77120

Organism-specific databases

AraportiAT1G77120
TAIRilocus:2025237 AT1G77120

Phylogenomic databases

eggNOGiKOG0022 Eukaryota
COG1062 LUCA
InParanoidiP06525
KOiK18857
OMAiVMHEISV
OrthoDBi664798at2759
PhylomeDBiP06525

Miscellaneous databases

Protein Ontology

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PROi
PR:P06525

Gene expression databases

ExpressionAtlasiP06525 baseline and differential
GenevisibleiP06525 AT

Family and domain databases

InterProiView protein in InterPro
IPR013149 ADH_C
IPR013154 ADH_N
IPR002328 ADH_Zn_CS
IPR011032 GroES-like_sf
IPR036291 NAD(P)-bd_dom_sf
PfamiView protein in Pfam
PF08240 ADH_N, 1 hit
PF00107 ADH_zinc_N, 1 hit
SUPFAMiSSF50129 SSF50129, 2 hits
SSF51735 SSF51735, 1 hit
PROSITEiView protein in PROSITE
PS00059 ADH_ZINC, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiADH1_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: P06525
Secondary accession number(s): O04080
, O04713, O04717, O04868, O23821, Q8LA61, Q94AY6, Q9CAZ2, Q9CAZ3, Q9SX08
<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: January 1, 1988
Last sequence update: May 29, 2007
Last modified: October 16, 2019
This is version 174 of the entry and version 2 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, Complete proteome, 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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