Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 143 (07 Apr 2021)
Sequence version 1 (01 Nov 1995)
Previous versions | rss
Add a publicationFeedback
Protein

Tryptophan 2,3-dioxygenase

Gene

tdo-2

Organism
Caenorhabditis elegans
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

Heme-dependent dioxygenase that catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L-tryptophan to N-formyl-L-kynurenine (PubMed:27995966). Catalyzes the oxidative cleavage of the indole moiety (PubMed:27995966). Involved in regulation of protein homeostasis, longevity and reproducive life span (PubMed:22927396, PubMed:27995966). Specifically regulates proteotoxicity due to age-related aggregation of proteins like alpha-synuclein, via its effects on tryptophan metabolism (PubMed:22927396).UniRule annotation2 Publications

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

<p>This subsection of the 'Function' section 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

hemeUniRule annotationNote: Binds 1 heme group per subunit.UniRule annotation

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-tryptophan degradation via kynurenine pathway

This protein is involved in step 1 of the subpathway that synthesizes L-kynurenine from L-tryptophan.UniRule annotation1 Publication1 Publication
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Tryptophan 2,3-dioxygenase (tdo-2)
  2. no protein annotated in this organism
This subpathway is part of the pathway L-tryptophan degradation via kynurenine pathway, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-kynurenine from L-tryptophan, the pathway L-tryptophan degradation via kynurenine pathway and in Amino-acid degradation.

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 sitei140SubstrateUniRule annotation1
<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 bindingi327Iron (heme axial ligand)UniRule annotation1
Binding sitei341SubstrateUniRule annotation1

<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 functionDioxygenase, Oxidoreductase
Biological processTryptophan catabolism
LigandHeme, Iron, Metal-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-CEL-71240, Tryptophan catabolism

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

More...
UniPathwayi
UPA00333;UER00453

<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:
Tryptophan 2,3-dioxygenaseUniRule annotation (EC:1.13.11.11UniRule annotation1 Publication)
Short name:
TDOUniRule annotation
Alternative name(s):
Tryptamin 2,3-dioxygenaseUniRule annotation
Tryptophan oxygenaseUniRule annotation
Short name:
TOUniRule annotation
Short name:
TRPOUniRule annotation
Tryptophan pyrrolaseUniRule annotation
TryptophanaseUniRule annotation
<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:tdo-2Imported
ORF Names:C28H8.11Imported
<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>OrganismiCaenorhabditis elegans
<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 identifieri6239 [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 lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditinaRhabditomorphaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
<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
  • UP000001940 <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 III

Organism-specific databases

WormBase

More...
WormBasei
C28H8.11a ; CE01822 ; WBGene00016201 ; tdo-2
C28H8.11c ; CE39680 ; WBGene00016201 ; tdo-2

<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

RNAi-mediated knockdown of the protein increases longevity and causes a delayed and extended reproductive life span without increasing total progeny. Animals show increased levels of tryptophan, reduced sensitivity to proteotoxic aggregates of alpha-synuclein and reduced age-related decline of motility. A double knockdown of tdo-2 together with an enzyme downstream in the kynurenine pathway, kmo-1, flu-2, afmd-1 or haao-1, causes an increase in motility and tryptophan levels and suppresses the proteotoxicity similarly to knock-down of tdo-2 alone. RNAi-mediated knockdown in a tph-1 deletion background, which is necessary for synthesis of serotonin from trypotophan, shows increased motility, but variable suppression of proteotoxicity. RNAi-mediated knockdown in a mutant background for daf-16, which functions in the IIS pathway, shows suppression of proteotoxicity and only a small increase in median, but not mean life span. RNAi-mediated knockdown in a mutant background for hsf-1, which also functions in the IIS pathway, shows suppression of proteotoxicity and a small increase in life span. RNAi-mediated knockdown in a mutant background for hif-1, which functions in the hypoxia stress response pathway, shows an increase in median, but not mean life span that is lower than for the tdo-2 knockdown alone. RNAi-mediated knockdown in a mutant background for eat-2, which is used as a model for dietary restriction, shows suppression of proteotoxicity and an increase in life span.1 Publication

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>Mutagenesisi133 – 135Missing : Abolishes catalytic activity. Animals have an extended lifespan, an extended reproductive lifespan, have fewer hatched progeny and display increased motility. 1 Publication3

<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_00000723981 – 403Tryptophan 2,3-dioxygenaseAdd BLAST403

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q09474

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

More...
PaxDbi
Q09474

PeptideAtlas

More...
PeptideAtlasi
Q09474

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

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

Expressed in body wall muscle cells, hypodermis, PLM neurons and touch-receptor neurons.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
WBGene00016201, Expressed in multi-cellular organism and 4 other tissues

<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

Homotetramer. Dimer of dimers.

UniRule annotation

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
41057, 7 interactors

Database of interacting proteins

More...
DIPi
DIP-26438N

Protein interaction database and analysis system

More...
IntActi
Q09474, 3 interactors

STRING: functional protein association networks

More...
STRINGi
6239.C28H8.11a.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

3D structure databases

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

More...
SMRi
Q09474

Database of comparative protein structure models

More...
ModBasei
Search...

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

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>Regioni69 – 73Substrate bindingUniRule annotation5

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi133 – 135PLD motif; required for enzymatic activity1 Publication3

<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 tryptophan 2,3-dioxygenase family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3906, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000008593

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_045599_1_1_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q09474

Identification of Orthologs from Complete Genome Data

More...
OMAi
MLVPHRG

Database of Orthologous Groups

More...
OrthoDBi
896211at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q09474

Family and domain databases

HAMAP database of protein families

More...
HAMAPi
MF_01972, T23O, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR037217, Trp/Indoleamine_2_3_dOase-like
IPR004981, Trp_2_3_dOase

The PANTHER Classification System

More...
PANTHERi
PTHR10138, PTHR10138, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03301, Trp_dioxygenase, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF140959, SSF140959, 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>Sequences (2)i

<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.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform aImported (identifier: Q09474-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MACPYLGSGE LTHRVTFMEG GEECQQGVNK VEMGFGQTYS EYLQLDKILT
60 70 80 90 100
AQRLKSEADG QRVDDEHLFI VIHQAHELWF KQIIFDLDNV RKLLNNTIVD
110 120 130 140 150
ETKTLKIVSG LDRMTKILSL LTEQITLLDT MSPLDFVDFR KYLTPASGFQ
160 170 180 190 200
SLQFRVLENK LGVRQERRIK YNAQHYKNVF NDTDLKTLNV TEEEKSLLTL
210 220 230 240 250
IESWLERTPG LKSTSEDEGF WIKYEKSVNK YLADLAKQAA DPSNTEEIAK
260 270 280 290 300
QLTAEYHKTA DAFQSILDPR QHEQHIRNGN RLLSHDATKG AMMIYFYRDM
310 320 330 340 350
PRFSQPYQIL TFLMDIDSLF TKWRYNHVLL VQRMLGAKQG TGGSSGYMYL
360 370 380 390 400
RSTVSDRYKV FLDLFNLSTW LIPREYIPML SPRMVKTLSE HSNLSHSQSS

ESD
Length:403
Mass (Da):46,716
Last modified:November 1, 1995 - 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:i8F1E98075CA86A65
GO
Isoform cImported (identifier: Q09474-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-291: Missing.

Show »
Length:112
Mass (Da):13,263
Checksum:i6413E43D275F44B6
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0573111 – 291Missing in isoform c. CuratedAdd BLAST291

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
BX284603 Genomic DNA Translation: CCD65972.1
BX284603 Genomic DNA Translation: CCD65974.1

Protein sequence database of the Protein Information Resource

More...
PIRi
B88470

NCBI Reference Sequences

More...
RefSeqi
NP_001040847.1, NM_001047382.4 [Q09474-3]
NP_498284.1, NM_065883.4 [Q09474-1]

Genome annotation databases

Ensembl metazoan genome annotation project

More...
EnsemblMetazoai
C28H8.11a.1; C28H8.11a.1; WBGene00016201 [Q09474-1]
C28H8.11a.2; C28H8.11a.2; WBGene00016201 [Q09474-1]
C28H8.11c.1; C28H8.11c.1; WBGene00016201 [Q09474-3]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
175836

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
cel:CELE_C28H8.11

UCSC genome browser

More...
UCSCi
C28H8.11c.3, c. elegans

Keywords - Coding sequence diversityi

Alternative splicing

<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
BX284603 Genomic DNA Translation: CCD65972.1
BX284603 Genomic DNA Translation: CCD65974.1
PIRiB88470
RefSeqiNP_001040847.1, NM_001047382.4 [Q09474-3]
NP_498284.1, NM_065883.4 [Q09474-1]

3D structure databases

SMRiQ09474
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi41057, 7 interactors
DIPiDIP-26438N
IntActiQ09474, 3 interactors
STRINGi6239.C28H8.11a.1

Proteomic databases

EPDiQ09474
PaxDbiQ09474
PeptideAtlasiQ09474

Genome annotation databases

EnsemblMetazoaiC28H8.11a.1; C28H8.11a.1; WBGene00016201 [Q09474-1]
C28H8.11a.2; C28H8.11a.2; WBGene00016201 [Q09474-1]
C28H8.11c.1; C28H8.11c.1; WBGene00016201 [Q09474-3]
GeneIDi175836
KEGGicel:CELE_C28H8.11
UCSCiC28H8.11c.3, c. elegans

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
175836
WormBaseiC28H8.11a ; CE01822 ; WBGene00016201 ; tdo-2
C28H8.11c ; CE39680 ; WBGene00016201 ; tdo-2

Phylogenomic databases

eggNOGiKOG3906, Eukaryota
GeneTreeiENSGT00390000008593
HOGENOMiCLU_045599_1_1_1
InParanoidiQ09474
OMAiMLVPHRG
OrthoDBi896211at2759
PhylomeDBiQ09474

Enzyme and pathway databases

UniPathwayiUPA00333;UER00453
ReactomeiR-CEL-71240, Tryptophan catabolism

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q09474

Gene expression databases

BgeeiWBGene00016201, Expressed in multi-cellular organism and 4 other tissues

Family and domain databases

HAMAPiMF_01972, T23O, 1 hit
InterProiView protein in InterPro
IPR037217, Trp/Indoleamine_2_3_dOase-like
IPR004981, Trp_2_3_dOase
PANTHERiPTHR10138, PTHR10138, 1 hit
PfamiView protein in Pfam
PF03301, Trp_dioxygenase, 1 hit
SUPFAMiSSF140959, SSF140959, 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 nameiT23O_CAEEL
<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: Q09474
Secondary accession number(s): Q27GU8, Q8I7L6
<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: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 7, 2021
This is version 143 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 programCaenorhabditis annotation project

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

Keywords - Technical termi

Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again