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Entry version 114 (07 Oct 2020)
Sequence version 2 (12 Dec 2006)
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Protein

Bifunctional monothiol glutaredoxin-S16, chloroplastic

Gene

GRXS16

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

May only reduce GSH-thiol disulfides, but not protein disulfides (Probable). Participates probably to the maturation of iron-sulfur proteins and to the regulation of the redox state of the BOLA proteins (Probable). The GRXS16-BOLA1 heterodimer binds a labile, oxygen sensitive iron-sulfur cluster (PubMed:24714563). Able to cleave linearized DNA in vitro (PubMed:23690600).Curated2 Publications

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

The formation of an intramolecular disulfide bond negatively regulates both the N-terminal endonuclease and the C-terminal glutaredoxin activities.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei211GlutathioneBy similarity1
<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 bindingi219Iron-sulfur (2Fe-2S); shared with dimeric partnerBy similarity1
Binding sitei251GlutathioneBy similarity1
Binding sitei263Glutathione; via amide nitrogen and carbonyl oxygenBy similarity1

<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

  • cation transport Source: TAIR

<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, Multifunctional enzyme
Ligand2Fe-2S, Iron, Iron-sulfur, Metal-binding

<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:
Bifunctional monothiol glutaredoxin-S16, chloroplastic1 Publication
Short name:
AtGrxS161 Publication
Alternative name(s):
Atypical GIY-YIG endonuclease1 Publication (EC:3.1.-.-)
CAX-interacting protein 21 Publication
CAXIP1-like protein1 Publication
<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:GRXS161 Publication
Synonyms:CXIP21 Publication
Ordered Locus Names:At2g38270Imported
ORF Names:F16M14.20Imported
<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 2

Organism-specific databases

Arabidopsis Information Portal

More...
Araporti
AT2G38270

The Arabidopsis Information Resource

More...
TAIRi
locus:2042887, AT2G38270

<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

Chloroplast, Plastid

<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

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>Mutagenesisi90Y → F: Strongly reduced nuclease activity. 1 Publication1
Mutagenesisi101F → Y: Enhanced nuclease activity. 1 Publication1
Mutagenesisi111S → A: Strongly reduced nuclease activity. 1 Publication1
Mutagenesisi111S → R: Slightly reduced nuclease activity. 1 Publication1
Mutagenesisi115H → F: Strongly reduced nuclease activity. 1 Publication1
Mutagenesisi123C → S: Increased glutaredoxin activity. 1 Publication1
Mutagenesisi143W → A or E: Slightly reduced nuclease activity. 1 Publication1
Mutagenesisi161N → L: Slightly reduced nuclease activity. 1 Publication1
Mutagenesisi219C → S: Decreased interactions with BOLA proteins and loss of interaction with SUFE1. 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 transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 62ChloroplastSequence analysisAdd BLAST62
<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_000026873663 – 293Bifunctional monothiol glutaredoxin-S16, chloroplasticAdd BLAST231

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi123 ↔ 2191 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

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

More...
PaxDbi
Q8H7F6

PRoteomics IDEntifications database

More...
PRIDEi
Q8H7F6

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
222250

<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

Gene expression databases

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q8H7F6, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q8H7F6, 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

[2Fe-2S]-bridged holo-homodimer (PubMed:23690600).

Interacts in vitro with SUFE1, BOLA1, BOLA2 and BOLA4 (PubMed:24203231).

Interacts in vivo only with SUFE1, BOLA1 and BOLA4 (PubMed:24203231, PubMed:24714563, PubMed:23690600).

Interacts with SBP1 (PubMed:30824043).

4 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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
3749, 12 interactors

Protein interaction database and analysis system

More...
IntActi
Q8H7F6, 8 interactors

STRING: functional protein association networks

More...
STRINGi
3702.AT2G38270.1

<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

1293
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

More...
BMRBi
Q8H7F6

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

More...
SMRi
Q8H7F6

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
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

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>Domaini194 – 293GlutaredoxinPROSITE-ProRule annotationAdd BLAST100

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>Regioni276 – 277Glutathione bindingBy similarity2

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The N-terminal domain (NTD) (63-170) has an intrinsic Mg2+-dependent endonuclease activity in vitro (PubMed:23690600). The glutaredoxin (GRX) domain (194-293) alone is able to complement yeast grx5 cells in vitro, but not the full-length GRXS16 protein.1 Publication

<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

Belongs to the glutaredoxin family. CGFS subfamily.Curated

Keywords - Domaini

Redox-active center, Transit peptide

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0911, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_070932_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q8H7F6

Identification of Orthologs from Complete Genome Data

More...
OMAi
SQNTPSF

Database of Orthologous Groups

More...
OrthoDBi
1449534at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q8H7F6

Family and domain databases

Conserved Domains Database

More...
CDDi
cd03028, GRX_PICOT_like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.1440.10, 1 hit
3.40.30.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR035901, GIY-YIG_endonuc_sf
IPR002109, Glutaredoxin
IPR033658, GRX_PICOT-like
IPR004480, Monothiol_GRX-rel
IPR036249, Thioredoxin-like_sf

The PANTHER Classification System

More...
PANTHERi
PTHR10293, PTHR10293, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00462, Glutaredoxin, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52833, SSF52833, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00365, TIGR00365, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51354, GLUTAREDOXIN_2, 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.

<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 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.

Q8H7F6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAAITISSSL HASASPRVVR PHVSRNTPVI TLYSRFTPSF SFPSLSFTLR
60 70 80 90 100
DTAPSRRRSF FIASAVKSLT ETELLPITEA DSIPSASGVY AVYDKSDELQ
110 120 130 140 150
FVGISRNIAA SVSAHLKSVP ELCGSVKVGI VEEPDKAVLT QAWKLWIEEH
160 170 180 190 200
IKVTGKVPPG NKSGNNTFVK QTPRKKSDIR LTPGRHVELT VPLEELIDRL
210 220 230 240 250
VKESKVVAFI KGSRSAPQCG FSQRVVGILE SQGVDYETVD VLDDEYNHGL
260 270 280 290
RETLKNYSNW PTFPQIFVKG ELVGGCDILT SMYENGELAN ILN
Length:293
Mass (Da):32,206
Last modified:December 12, 2006 - 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:i6B2E6337F8C5F050
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 conflicti194E → G in AAN60257 (Ref. 2) Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AY157989 mRNA Translation: AAO19648.1
AF083698 mRNA Translation: AAN60257.1
AC003028 Genomic DNA Translation: AAC27175.1
CP002685 Genomic DNA Translation: AEC09515.1
AK117441 mRNA Translation: BAC42106.1
BT004974 mRNA Translation: AAO50507.1
AY086273 mRNA Translation: AAM64346.1

Protein sequence database of the Protein Information Resource

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PIRi
T01258

NCBI Reference Sequences

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RefSeqi
NP_565885.1, NM_129383.3

Genome annotation databases

Ensembl plant genome annotation project

More...
EnsemblPlantsi
AT2G38270.1; AT2G38270.1; AT2G38270

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
818407

Gramene; a comparative resource for plants

More...
Gramenei
AT2G38270.1; AT2G38270.1; AT2G38270

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ath:AT2G38270

<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
AY157989 mRNA Translation: AAO19648.1
AF083698 mRNA Translation: AAN60257.1
AC003028 Genomic DNA Translation: AAC27175.1
CP002685 Genomic DNA Translation: AEC09515.1
AK117441 mRNA Translation: BAC42106.1
BT004974 mRNA Translation: AAO50507.1
AY086273 mRNA Translation: AAM64346.1
PIRiT01258
RefSeqiNP_565885.1, NM_129383.3

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
2LWFNMR-A63-170[»]
BMRBiQ8H7F6
SMRiQ8H7F6
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi3749, 12 interactors
IntActiQ8H7F6, 8 interactors
STRINGi3702.AT2G38270.1

Proteomic databases

PaxDbiQ8H7F6
PRIDEiQ8H7F6
ProteomicsDBi222250

Genome annotation databases

EnsemblPlantsiAT2G38270.1; AT2G38270.1; AT2G38270
GeneIDi818407
GrameneiAT2G38270.1; AT2G38270.1; AT2G38270
KEGGiath:AT2G38270

Organism-specific databases

AraportiAT2G38270
TAIRilocus:2042887, AT2G38270

Phylogenomic databases

eggNOGiKOG0911, Eukaryota
HOGENOMiCLU_070932_0_0_1
InParanoidiQ8H7F6
OMAiSQNTPSF
OrthoDBi1449534at2759
PhylomeDBiQ8H7F6

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q8H7F6

Gene expression databases

ExpressionAtlasiQ8H7F6, baseline and differential
GenevisibleiQ8H7F6, AT

Family and domain databases

CDDicd03028, GRX_PICOT_like, 1 hit
Gene3Di3.40.1440.10, 1 hit
3.40.30.10, 1 hit
InterProiView protein in InterPro
IPR035901, GIY-YIG_endonuc_sf
IPR002109, Glutaredoxin
IPR033658, GRX_PICOT-like
IPR004480, Monothiol_GRX-rel
IPR036249, Thioredoxin-like_sf
PANTHERiPTHR10293, PTHR10293, 1 hit
PfamiView protein in Pfam
PF00462, Glutaredoxin, 1 hit
SUPFAMiSSF52833, SSF52833, 1 hit
TIGRFAMsiTIGR00365, TIGR00365, 1 hit
PROSITEiView protein in PROSITE
PS51354, GLUTAREDOXIN_2, 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 nameiGRS16_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: Q8H7F6
Secondary accession number(s): O80451, Q8LD13
<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: December 12, 2006
Last sequence update: December 12, 2006
Last modified: October 7, 2020
This is version 114 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, 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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