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Entry version 144 (02 Jun 2021)
Sequence version 1 (01 Jan 1998)
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Protein

Translocase of chloroplast 33, chloroplastic

Gene

TOC33

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

GTPase involved in protein precursor import into chloroplasts. Seems to recognize chloroplast-destined precursor proteins and regulate their presentation to the translocation channel through GTP hydrolysis. Binds GTP, GDP, XTP, but not ATP. Probably specialized in the import of nuclear encoded photosynthetic preproteins from the cytoplasm to the chloroplast, especially during early development stages.

10 Publications

<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

Mg2+3 PublicationsNote: Binds 1 Mg2+ ion by subunit.3 Publications

<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

  1. KM=290 nM for GDP (at pH 7.4)2 Publications
  2. KM=5.7 µM for GTP (at pH 7.6 and 25 degrees Celsius)2 Publications
  1. Vmax=1040 nmol/min/µg enzyme with GTP as substrate (at pH 7.4)2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi50Magnesium3 Publications1
Metal bindingi68Magnesium3 Publications1
<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 sitei160GTP; via amide nitrogenCombined sources1 Publication1

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 – 51GTPCombined sources1 Publication6
Nucleotide bindingi65 – 70GTP1 Publication6
Nucleotide bindingi208 – 209GTPCombined sources1 Publication2

<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 functionHydrolase, Receptor
Biological processProtein transport, Transport
LigandGTP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
ARA:AT1G02280-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.6.5.2, 399

<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:
Translocase of chloroplast 33, chloroplastic (EC:3.6.5.-)
Short name:
AtToc33
Alternative name(s):
33 kDa chloroplast outer envelope protein
Plastid protein import 1
<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:TOC33
Synonyms:PPI1
Ordered Locus Names:At1g02280
ORF Names:T7I23.11
<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>OrganismiArabidopsis thaliana (Mouse-ear cress)
<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 identifieri3702 [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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
<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
  • UP000006548 <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 1

Organism-specific databases

Arabidopsis Information Portal

More...
Araporti
AT1G02280

The Arabidopsis Information Resource

More...
TAIRi
locus:2204923, AT1G02280

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei37 – 53HelicalSequence analysisAdd BLAST17

Keywords - Cellular componenti

Chloroplast, Membrane, Plastid, Plastid outer 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 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

Plants exhibits a pale yellowish phenotype.3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi45 – 50GGVGKS → RGVGNR: Reduced GTPase activity and impaired interaction with TOC159. 1 Publication6
Mutagenesisi130R → A: Loss of homidimerization and heterodimerization with TOC159, reduction of GTPase activity. 3 Publications1
Mutagenesisi170S → A: Normal phosphorylation. 1 Publication1
Mutagenesisi175S → A: Normal phosphorylation. 1 Publication1
Mutagenesisi181S → A: Loss of phosphorylation, normal activity. 2 Publications1
Mutagenesisi181S → D or E: According to PubMed:16412428, supposed to mimic the effects of phosphoserine, but normal activity. 2 Publications1
Mutagenesisi181S → T: Phosphothreonine instead of phosphoserine. 2 Publications1
Mutagenesisi190S → A: Normal phosphorylation. 1 Publication1
Mutagenesisi200S → A: Normal phosphorylation. 1 Publication1
Mutagenesisi208E → Q: Normal GTPase activity, but weaker nucleotide binding. 1 Publication1
Mutagenesisi217D → N: Normal GTPase activity. 1 Publication1
Mutagenesisi219D → N: Normal GTPase activity. 1 Publication1
Mutagenesisi220E → Q: Normal GTPase activity. 1 Publication1

<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_00003526551 – 297Translocase of chloroplast 33, chloroplasticAdd BLAST297

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 residuei181Phosphoserine3 Publications1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

Phosphorylated by a kinase present in the outer envelope of chloroplast. When Ser-181 is phosphorylated, the binding to preprotein, GTP and GDP is inhibited, and thus, GTPase activity is repressed.3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

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

More...
PaxDbi
O23680

PRoteomics IDEntifications database

More...
PRIDEi
O23680

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
234323

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
O23680

<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

Mostly expressed in seedlings and flowers, and, to a lower extent, in roots, stems, and leaves.2 Publications

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Mostly expressed in photosynthetic tissues undergoing rapid growth. Observed in cotyledons and vascular tissues of hypocotyls of young seedling. In roots, restricted to apical and lateral meristems, and vascular bundles. In stems, mostly detected in the upper part. Expressed in young and middle-aged leaves. In flowers, confined to sepals.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

Up-regulated by CIA2 in leaves. Induced in light but repressed in darkness.2 Publications

Gene expression databases

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
O23680, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
O23680, 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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer, heterodimer with TOC34 and TOC159, and monomer. The homodimerization and the dimerization with TOC159 require the binding of GTP on Arg-130, and a hypothetical coGAP factor. The dimeric form has a higher GTPase activity than the monomeric form. Part of the TOC core complex that includes 1 protein for the specific recognition of transit peptides surrounded by a ring composed of four proteins forming translocation channels, and four to five GTP-binding proteins providing energy. This core complex can interact with components of the TIC complex to form a larger import complex. Chloroplastic protein precursor such as prSS (precursor of the RuBisCO small subunit) interacts with these complexes. The TOC complex contains a specific subset of polar lipids such as digalactosyldiacylglyceride (DGDG), phosphatidylcholine (PC) and phosphatidylglycerol (PG).

Interacts at least with TOC75-3. Forms large complexes including TOC33, pPORA and OEP161 during pPORA import into plastids at the plastid envelope membrane (PubMed:10998188, PubMed:12473690, PubMed:12951325, PubMed:15773849, PubMed:17337454, PubMed:18400179, PubMed:18541539).

Interacts with SP1 (PubMed:23118188).

8 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
24483, 8 interactors

Protein interaction database and analysis system

More...
IntActi
O23680, 8 interactors

STRING: functional protein association networks

More...
STRINGi
3702.AT1G02280.1

<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

1297
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
O23680

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
O23680

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini34 – 258AIG1-type GPROSITE-ProRule annotationAdd BLAST225

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni65 – 68Homodimerization1 Publication4
Regioni125 – 130Homodimerization1 Publication6

<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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG502QSV2, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_051932_0_0_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O23680

Identification of Orthologs from Complete Genome Data

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OMAi
VENNSRC

Database of Orthologous Groups

More...
OrthoDBi
1108753at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
O23680

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR006703, G_AIG1
IPR027417, P-loop_NTPase
IPR005688, Toc34

Pfam protein domain database

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Pfami
View protein in Pfam
PF04548, AIG1, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF038134, Toc34, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF52540, SSF52540, 1 hit

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR00991, 3a0901s02IAP34, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51720, G_AIG1, 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.

O23680-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGSLVREWVG FQQFPAATQE KLIEFFGKLK QKDMNSMTVL VLGKGGVGKS
60 70 80 90 100
STVNSLIGEQ VVRVSPFQAE GLRPVMVSRT MGGFTINIID TPGLVEAGYV
110 120 130 140 150
NHQALELIKG FLVNRTIDVL LYVDRLDVYR VDELDKQVVI AITQTFGKEI
160 170 180 190 200
WCKTLLVLTH AQFSPPDELS YETFSSKRSD SLLKTIRAGS KMRKQEFEDS
210 220 230 240 250
AIAVVYAENS GRCSKNDKDE KALPNGEAWI PNLVKAITDV ATNQRKAIHV
260 270 280 290
DKKMVDGSYS DDKGKKLIPL IIGAQYLIVK MIQGAIRNDI KTSGKPL
Length:297
Mass (Da):32,925
Last modified:January 1, 1998 - 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:iE48892E123BA412D
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 conflicti147G → A in AAK68809 (PubMed:14593172).Curated1

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
AJ010724 mRNA Translation: CAC17698.1
U89959 Genomic DNA Translation: AAC24375.1
CP002684 Genomic DNA Translation: AEE27409.1
CP002684 Genomic DNA Translation: AEE27410.1
AY042869 mRNA Translation: AAK68809.1
AY056448 mRNA Translation: AAL08304.1
BT025654 mRNA Translation: ABF74715.1

NCBI Reference Sequences

More...
RefSeqi
NP_001117215.1, NM_001123743.2
NP_171730.1, NM_100108.5

Genome annotation databases

Ensembl plant genome annotation project

More...
EnsemblPlantsi
AT1G02280.1; AT1G02280.1; AT1G02280
AT1G02280.2; AT1G02280.2; AT1G02280

Database of genes from NCBI RefSeq genomes

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GeneIDi
839248

Gramene; a comparative resource for plants

More...
Gramenei
AT1G02280.1; AT1G02280.1; AT1G02280
AT1G02280.2; AT1G02280.2; AT1G02280

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ath:AT1G02280

<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
AJ010724 mRNA Translation: CAC17698.1
U89959 Genomic DNA Translation: AAC24375.1
CP002684 Genomic DNA Translation: AEE27409.1
CP002684 Genomic DNA Translation: AEE27410.1
AY042869 mRNA Translation: AAK68809.1
AY056448 mRNA Translation: AAL08304.1
BT025654 mRNA Translation: ABF74715.1
RefSeqiNP_001117215.1, NM_001123743.2
NP_171730.1, NM_100108.5

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2J3EX-ray3.20A2-250[»]
3BB3X-ray2.94A1-251[»]
3BB4X-ray2.85A1-251[»]
3DEFX-ray1.96A1-251[»]
SMRiO23680
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi24483, 8 interactors
IntActiO23680, 8 interactors
STRINGi3702.AT1G02280.1

PTM databases

iPTMnetiO23680

Proteomic databases

PaxDbiO23680
PRIDEiO23680
ProteomicsDBi234323

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
839248

Genome annotation databases

EnsemblPlantsiAT1G02280.1; AT1G02280.1; AT1G02280
AT1G02280.2; AT1G02280.2; AT1G02280
GeneIDi839248
GrameneiAT1G02280.1; AT1G02280.1; AT1G02280
AT1G02280.2; AT1G02280.2; AT1G02280
KEGGiath:AT1G02280

Organism-specific databases

AraportiAT1G02280
TAIRilocus:2204923, AT1G02280

Phylogenomic databases

eggNOGiENOG502QSV2, Eukaryota
HOGENOMiCLU_051932_0_0_1
InParanoidiO23680
OMAiVENNSRC
OrthoDBi1108753at2759
PhylomeDBiO23680

Enzyme and pathway databases

BioCyciARA:AT1G02280-MONOMER
BRENDAi3.6.5.2, 399

Miscellaneous databases

EvolutionaryTraceiO23680

Protein Ontology

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PROi
PR:O23680

Gene expression databases

ExpressionAtlasiO23680, baseline and differential
GenevisibleiO23680, AT

Family and domain databases

InterProiView protein in InterPro
IPR006703, G_AIG1
IPR027417, P-loop_NTPase
IPR005688, Toc34
PfamiView protein in Pfam
PF04548, AIG1, 1 hit
PIRSFiPIRSF038134, Toc34, 1 hit
SUPFAMiSSF52540, SSF52540, 1 hit
TIGRFAMsiTIGR00991, 3a0901s02IAP34, 1 hit
PROSITEiView protein in PROSITE
PS51720, G_AIG1, 1 hit

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 nameiTOC33_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: O23680
Secondary accession number(s): Q94B42, Q9GDD3
<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: October 14, 2008
Last sequence update: January 1, 1998
Last modified: June 2, 2021
This is version 144 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. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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