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Entry version 161 (02 Jun 2021)
Sequence version 2 (01 Oct 2001)
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Protein

Dual oxidase 1

Gene

bli-3

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

Plays a role in cuticle biogenesis (PubMed:11514595, PubMed:19406744, PubMed:23028364, PubMed:25480962, PubMed:18460651).

In complex with doxa-1 and tsp-15, produces reactive oxygen species (ROS), which are probably used by mlt-7 for tyrosine cross-linking, thus stabilizing cuticular extracellular matrix (PubMed:11514595, PubMed:19406744, PubMed:23028364).

May regulate the production of ROS by playing a role in modulating proline catabolism (PubMed:27974198).

Required in combination with mlt-7 for correct formation of cross-links in cuticle collagens (PubMed:19406744).

Association with the GTPase rho-1 promotes ROS production and this interaction may be modulated by memo-1, in order to control the oxidative stress response and longevity (PubMed:28085666).

7 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 <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

Peroxidase activity is inhibited by aminobenzohydrazide.1 Publication

<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, Peroxidase
Biological processHydrogen peroxide
LigandCalcium, FAD, Flavoprotein, NADP

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.6.3.1, 1045

Protein family/group databases

PeroxiBase, a peroxidase database

More...
PeroxiBasei
3349, CelDuOx01

<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:
Dual oxidase 1 (EC:1.11.1.-, EC:1.6.3.1)
Short name:
DUOX1
Alternative name(s):
Blistered cuticle protein 3
NADPH thyroid oxidase 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:bli-3Imported
ORF Names:F56C11.1Imported
<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 I

Organism-specific databases

WormBase

More...
WormBasei
F56C11.1 ; CE28463 ; WBGene00000253 ; bli-3

<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 subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini22 – 587ExtracellularSequence analysisAdd BLAST566
<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>Transmembranei588 – 608HelicalSequence analysisAdd BLAST21
Topological domaini609 – 986CytoplasmicSequence analysisAdd BLAST378
Transmembranei987 – 1007HelicalSequence analysisAdd BLAST21
Topological domaini1008 – 1024ExtracellularSequence analysisAdd BLAST17
Transmembranei1025 – 1045HelicalSequence analysisAdd BLAST21
Topological domaini1046 – 1068CytoplasmicSequence analysisAdd BLAST23
Transmembranei1069 – 1089HelicalSequence analysisAdd BLAST21
Topological domaini1090 – 1134ExtracellularSequence analysisAdd BLAST45
Transmembranei1135 – 1155HelicalSequence analysisAdd BLAST21
Topological domaini1156 – 1163CytoplasmicSequence analysis8
Transmembranei1164 – 1184HelicalSequence analysisAdd BLAST21
Topological domaini1185 – 1189ExtracellularSequence analysis5
Transmembranei1190 – 1210HelicalSequence analysisAdd BLAST21
Topological domaini1211 – 1497CytoplasmicSequence analysisAdd BLAST287

Keywords - Cellular componenti

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

RNAi-mediated knockdown results in a blistered cuticle phenotype (PubMed:23028364, PubMed:25480962). Resistant to iodide toxicity (PubMed:25480962). RNAi-mediated knockdown in combination with proline supplementation suppresses the effects of exogenous proline alone and increases reactive oxygen species production and reduces the expression of skn-1 transcriptional targets including gst-4 following infection by P.aeruginosa (PubMed:27974198). RNAi-mediated knockdown rescues the enhanced longevity and increased reactive oxygen species production defects in memo-1 mutants (PubMed:28085666). RNAi-mediated knockdown suppresses the nuclear localization of transcription factor skn-1 in memo-1 RNAi mutants (PubMed:28085666).4 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>Mutagenesisi246G → D in e767; growth arrest, severe blistering of the cuticle, incomplete molting and mild shorter and stouter body shape. Resistant to iodide toxicity. Reduced catalase activity. In a pah-1(tm520) mutant background, growth arrest in early larval development, severe cuticle abnormalities with large blisters and increased superoxide dismutase activity. 2 Publications1
Mutagenesisi1263A → T in mac40; blistered cuticle phenotype in some animals with blisters containing cellular material. Resistant to iodide toxicity. 1 Publication1
Mutagenesisi1311P → L in im10; blistered cuticle phenotype with accumulation of cellular material in blisters. 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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 21Sequence analysisAdd BLAST21
<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_000022334822 – 1497Dual oxidase 1Add BLAST1476

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi66N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi305N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi567N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi586N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
O61213

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

More...
PaxDbi
O61213

PeptideAtlas

More...
PeptideAtlasi
O61213

PRoteomics IDEntifications database

More...
PRIDEi
O61213

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
O61213

<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 hypodermal cells.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
WBGene00000253, 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

Interacts with doxa-1 and tsp-15 (PubMed:23028364).

Interacts with rho-1 (PubMed:28085666).

2 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
37112, 6 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1020, BLI-3/DOXA-1/TSP-15 dual oxidase complex

STRING: functional protein association networks

More...
STRINGi
6239.F56C11.1

<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
O61213

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

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>Domaini817 – 852EF-hand 1PROSITE-ProRule annotationAdd BLAST36
Domaini853 – 888EF-hand 2PROSITE-ProRule annotationAdd BLAST36
Domaini1030 – 1210Ferric oxidoreductaseAdd BLAST181
Domaini1211 – 1318FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST108

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>Regioni26 – 590Peroxidase-like; mediates peroxidase activityAdd BLAST565

<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

In the N-terminal section; belongs to the peroxidase family.Curated

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0039, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000163963

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_004482_1_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
O61213

Identification of Orthologs from Complete Genome Data

More...
OMAi
DVFMWRT

Database of Orthologous Groups

More...
OrthoDBi
27424at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
O61213

Family and domain databases

Conserved Domains Database

More...
CDDi
cd09820, dual_peroxidase_like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.640.10, 1 hit
3.40.50.80, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR029595, DUOX1/Duox
IPR034821, DUOX_peroxidase
IPR011992, EF-hand-dom_pair
IPR002048, EF_hand_dom
IPR013112, FAD-bd_8
IPR017927, FAD-bd_FR_type
IPR013130, Fe3_Rdtase_TM_dom
IPR013121, Fe_red_NAD-bd_6
IPR039261, FNR_nucleotide-bd
IPR019791, Haem_peroxidase_animal
IPR010255, Haem_peroxidase_sf
IPR037120, Haem_peroxidase_sf_animal
IPR017938, Riboflavin_synthase-like_b-brl

The PANTHER Classification System

More...
PANTHERi
PTHR11972:SF175, PTHR11972:SF175, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF03098, An_peroxidase, 1 hit
PF08022, FAD_binding_8, 1 hit
PF01794, Ferric_reduct, 1 hit
PF08030, NAD_binding_6, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00457, ANPEROXIDASE

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47473, SSF47473, 1 hit
SSF48113, SSF48113, 1 hit
SSF52343, SSF52343, 1 hit
SSF63380, SSF63380, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50222, EF_HAND_2, 2 hits
PS51384, FAD_FR, 1 hit
PS50292, PEROXIDASE_3, 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.

O61213-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRSKHVLYIA ILFSSIFGGK GIQQNEEFQR YDGWYNNLAN SEWGSAGSRL
60 70 80 90 100
HRDARSYYSD GVYSVNNSLP SARELSDILF KGESGIPNTR GCTTLLAFFS
110 120 130 140 150
QVVAYEIMQS NGVSCPLETL KIQVPLCDNV FDKECEGKTE IPFTRAKYDK
160 170 180 190 200
ATGNGLNSPR EQINERTSWI DGSFIYGTTQ PWVSSLRSFK QGRLAEGVPG
210 220 230 240 250
YPPLNNPHIP LNNPAPPQVH RLMSPDRLFM LGDSRVNENP GLLSFGLILF
260 270 280 290 300
RWHNYNANQI HREHPDWTDE QIFQAARRLV IASMQKIIAY DFVPGLLGED
310 320 330 340 350
VRLSNYTKYM PHVPPGISHA FGAAAFRFPH SIVPPAMLLR KRGNKCEFRT
360 370 380 390 400
EVGGYPALRL CQNWWNAQDI VKEYSVDEII LGMASQIAER DDNIVVEDLR
410 420 430 440 450
DYIFGPMHFS RLDVVASSIM RGRDNGVPPY NELRRTFGLA PKTWETMNED
460 470 480 490 500
FYKKHTAKVE KLKELYGGNI LYLDAYVGGM LEGGENGPGE LFKEIIKDQF
510 520 530 540 550
TRIRDGDRFW FENKLNGLFT DEEVQMIHSI TLRDIIKATT DIDETMLQKD
560 570 580 590 600
VFFFKEGDPC PQPFQVNTTG LEPCVPFMQS TYWTDNDTTY VFTLIGLACV
610 620 630 640 650
PLICYGIGRY LVNRRIAIGH NSACDSLTTD FANDDCGAKG DIYGVNALEW
660 670 680 690 700
LQEEYIRQVR IEIENTTLAV KKPRGGILRK IRFETGQKIE LFHSMPNPSA
710 720 730 740 750
MHGPFVLLSQ KNNHHLVIRL SSDRDLSKFL DQIRQAASGI NAEVIIKDEE
760 770 780 790 800
NSILLSQAIT KERRQDRLDL FFREAYAKAF NDSELQDSET SFDSSNDDIL
810 820 830 840 850
NETISREELA SAMGMKANNE FVKRMFAMTA KHNEDSLSFN EFLTVLREFV
860 870 880 890 900
NAPQKQKLQT LFKMCDLEGK NKVLRKDLAE LVKSLNQTAG VHITESVQLR
910 920 930 940 950
LFNEVLHYAG VSNDAKYLTY DDFNALFSDI PDKQPVGLPF NRKNYQPSIG
960 970 980 990 1000
ETSSLNSFAV VDRSINSSAP LTLIHKVSAF LETYRQHVFI VFCFVAINLV
1010 1020 1030 1040 1050
LFFERFWHYR YMAENRDLRR VMGAGIAITR GAAGALSFCM ALILLTVCRN
1060 1070 1080 1090 1100
IITLLRETVI AQYIPFDSAI AFHKIVALFA AFWATLHTVG HCVNFYHVGT
1110 1120 1130 1140 1150
QSQEGLACLF QEAFFGSNFL PSISYWFFST ITGLTGIALV AVMCIIYVFA
1160 1170 1180 1190 1200
LPCFIKRAYH AFRLTHLLNI AFYALTLLHG LPKLLDSPKF GYYVVGPIVL
1210 1220 1230 1240 1250
FVIDRIIGLM QYYKKLEIVN AEILPSDIIY IEYRRPREFK YKSGQWVTVS
1260 1270 1280 1290 1300
SPSISCTFNE SHAFSIASSP QDENMKLYIK AVGPWTWKLR SELIRSLNTG
1310 1320 1330 1340 1350
SPFPLIHMKG PYGDGNQEWM DYEVAIMVGA GIGVTPYAST LVDLVQRTSS
1360 1370 1380 1390 1400
DSFHRVRCRK VYFLWVCSTH KNYEWFVDVL KNVEDQARSG ILETHIFVTQ
1410 1420 1430 1440 1450
TFHKFDLRTT MLYICEKHFR ATNSGISMFT GLHAKNHFGR PNFKAFFQFI
1460 1470 1480 1490
QSEHKEQSKI GVFSCGPVNL NESIAEGCAD ANRQRDAPSF AHRFETF
Length:1,497
Mass (Da):170,416
Last modified:October 1, 2001 - 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:i6C648F193796A730
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 conflicti105Y → H in AAF71303 (PubMed:11514595).Curated1
Sequence conflicti829T → I in AAF71303 (PubMed:11514595).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

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DDBJi
Links Updated
AF229855 mRNA Translation: AAF71303.1
BX284601 Genomic DNA Translation: CCD71714.1

Protein sequence database of the Protein Information Resource

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PIRi
T29025

NCBI Reference Sequences

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RefSeqi
NP_490686.3, NM_058285.4

Genome annotation databases

Ensembl metazoan genome annotation project

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EnsemblMetazoai
F56C11.1.1; F56C11.1.1; WBGene00000253

Database of genes from NCBI RefSeq genomes

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GeneIDi
171608

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
cel:CELE_F56C11.1

UCSC genome browser

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UCSCi
F56C11.1, c. elegans

<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
AF229855 mRNA Translation: AAF71303.1
BX284601 Genomic DNA Translation: CCD71714.1
PIRiT29025
RefSeqiNP_490686.3, NM_058285.4

3D structure databases

SMRiO61213
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi37112, 6 interactors
ComplexPortaliCPX-1020, BLI-3/DOXA-1/TSP-15 dual oxidase complex
STRINGi6239.F56C11.1

Protein family/group databases

PeroxiBasei3349, CelDuOx01

PTM databases

iPTMnetiO61213

Proteomic databases

EPDiO61213
PaxDbiO61213
PeptideAtlasiO61213
PRIDEiO61213

Genome annotation databases

EnsemblMetazoaiF56C11.1.1; F56C11.1.1; WBGene00000253
GeneIDi171608
KEGGicel:CELE_F56C11.1
UCSCiF56C11.1, c. elegans

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
171608
WormBaseiF56C11.1 ; CE28463 ; WBGene00000253 ; bli-3

Phylogenomic databases

eggNOGiKOG0039, Eukaryota
GeneTreeiENSGT00940000163963
HOGENOMiCLU_004482_1_0_1
InParanoidiO61213
OMAiDVFMWRT
OrthoDBi27424at2759
PhylomeDBiO61213

Enzyme and pathway databases

BRENDAi1.6.3.1, 1045

Miscellaneous databases

Protein Ontology

More...
PROi
PR:O61213

Gene expression databases

BgeeiWBGene00000253, Expressed in multi-cellular organism and 4 other tissues

Family and domain databases

CDDicd09820, dual_peroxidase_like, 1 hit
Gene3Di1.10.640.10, 1 hit
3.40.50.80, 1 hit
InterProiView protein in InterPro
IPR029595, DUOX1/Duox
IPR034821, DUOX_peroxidase
IPR011992, EF-hand-dom_pair
IPR002048, EF_hand_dom
IPR013112, FAD-bd_8
IPR017927, FAD-bd_FR_type
IPR013130, Fe3_Rdtase_TM_dom
IPR013121, Fe_red_NAD-bd_6
IPR039261, FNR_nucleotide-bd
IPR019791, Haem_peroxidase_animal
IPR010255, Haem_peroxidase_sf
IPR037120, Haem_peroxidase_sf_animal
IPR017938, Riboflavin_synthase-like_b-brl
PANTHERiPTHR11972:SF175, PTHR11972:SF175, 1 hit
PfamiView protein in Pfam
PF03098, An_peroxidase, 1 hit
PF08022, FAD_binding_8, 1 hit
PF01794, Ferric_reduct, 1 hit
PF08030, NAD_binding_6, 1 hit
PRINTSiPR00457, ANPEROXIDASE
SUPFAMiSSF47473, SSF47473, 1 hit
SSF48113, SSF48113, 1 hit
SSF52343, SSF52343, 1 hit
SSF63380, SSF63380, 1 hit
PROSITEiView protein in PROSITE
PS50222, EF_HAND_2, 2 hits
PS51384, FAD_FR, 1 hit
PS50292, PEROXIDASE_3, 1 hit

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 nameiDUOX1_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: O61213
Secondary accession number(s): Q9NH90
<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: February 21, 2006
Last sequence update: October 1, 2001
Last modified: June 2, 2021
This is version 161 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 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. SIMILARITY comments
    Index of protein domains and families
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