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Protein

Dual oxidase 1

Gene

bli-3

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in cuticle biogenesis (PubMed:11514595, PubMed:19406744, PubMed:23028364, PubMed:25480962). 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). Required in combination with mlt-7 for correct formation of cross-links in cuticle collagens (PubMed:19406744).4 Publications

Catalytic activityi

NAD(P)H + O2 = NAD(P)+ + H2O2.1 Publication

Enzyme regulationi

Peroxidase activity is inhibited by aminobenzohydrazide.1 Publication

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • heme binding Source: WormBase
  • NAD(P)H oxidase activity Source: WormBase
  • peroxidase activity Source: WormBase

GO - Biological processi

  • collagen and cuticulin-based cuticle development Source: WormBase
  • cuticle development involved in collagen and cuticulin-based cuticle molting cycle Source: WormBase
  • defense response to fungus Source: WormBase
  • defense response to Gram-positive bacterium Source: WormBase
  • hydrogen peroxide catabolic process Source: UniProtKB-KW
  • nematode larval development Source: WormBase
  • oxidation-reduction process Source: WormBase
  • peptide cross-linking Source: WormBase
  • post-embryonic body morphogenesis Source: WormBase
  • response to oxidative stress Source: WormBase
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Calcium, FAD, Flavoprotein, NADP

Enzyme and pathway databases

BRENDAi1.6.3.1. 1045.
ReactomeiR-CEL-209968. Thyroxine biosynthesis.

Protein family/group databases

PeroxiBasei3349. CelDuOx01.

Names & Taxonomyi

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
Gene namesi
Name:bli-3Imported
ORF Names:F56C11.1Imported
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome I

Organism-specific databases

WormBaseiF56C11.1; CE28463; WBGene00000253; bli-3.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini22 – 587ExtracellularSequence analysisAdd BLAST566
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

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: WormBase
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Disruption phenotypei

RNAi-mediated knockdown results in a blistered cuticle phenotype (PubMed:23028364, PubMed:25480962). Resistant to iodide toxicity (PubMed:25480962).2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi246G → D in e767; resistant to iodide toxicity. 1 Publication1
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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Sequence analysisAdd BLAST21
ChainiPRO_000022334822 – 1497Dual oxidase 1Add BLAST1476

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi66N-linked (GlcNAc...)1 Publication1
Glycosylationi305N-linked (GlcNAc...)Sequence analysis1
Glycosylationi567N-linked (GlcNAc...)Sequence analysis1
Glycosylationi586N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

EPDiO61213.
PaxDbiO61213.
PeptideAtlasiO61213.
PRIDEiO61213.

Expressioni

Tissue specificityi

Expressed in hypodermal cells.1 Publication

Gene expression databases

BgeeiWBGene00000253.

Interactioni

Subunit structurei

Interacts with doxa-1 and tsp-15.1 Publication

Protein-protein interaction databases

STRINGi6239.F56C11.1.

Structurei

3D structure databases

ProteinModelPortaliO61213.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
Regioni26 – 590Peroxidase-like; mediates peroxidase activityAdd BLAST565

Sequence similaritiesi

In the N-terminal section; belongs to the peroxidase family.Curated
Contains 2 EF-hand domains.PROSITE-ProRule annotation
Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation
Contains 1 ferric oxidoreductase domain.Curated

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0039. Eukaryota.
ENOG410XNZY. LUCA.
GeneTreeiENSGT00550000074350.
HOGENOMiHOG000231774.
InParanoidiO61213.
KOiK13411.
OMAiILECELT.
OrthoDBiEOG091G00PO.
PhylomeDBiO61213.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
1.10.640.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR002048. EF_hand_dom.
IPR013112. FAD-bd_8.
IPR017927. Fd_Rdtase_FAD-bd.
IPR013130. Fe3_Rdtase_TM_dom.
IPR013121. Fe_red_NAD-bd_6.
IPR010255. Haem_peroxidase.
IPR019791. Haem_peroxidase_animal.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF03098. An_peroxidase. 1 hit.
PF08022. FAD_binding_8. 1 hit.
PF01794. Ferric_reduct. 1 hit.
PF08030. NAD_binding_6. 1 hit.
[Graphical view]
PRINTSiPR00457. ANPEROXIDASE.
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF48113. SSF48113. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiPS50222. EF_HAND_2. 2 hits.
PS51384. FAD_FR. 1 hit.
PS50292. PEROXIDASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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
Checksum:i6C648F193796A730
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti105Y → H in AAF71303 (PubMed:11514595).Curated1
Sequence conflicti829T → I in AAF71303 (PubMed:11514595).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF229855 mRNA. Translation: AAF71303.1.
FO081456 Genomic DNA. Translation: CCD71714.1.
PIRiT29025.
RefSeqiNP_490686.3. NM_058285.4.
UniGeneiCel.31857.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF229855 mRNA. Translation: AAF71303.1.
FO081456 Genomic DNA. Translation: CCD71714.1.
PIRiT29025.
RefSeqiNP_490686.3. NM_058285.4.
UniGeneiCel.31857.

3D structure databases

ProteinModelPortaliO61213.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi6239.F56C11.1.

Protein family/group databases

PeroxiBasei3349. CelDuOx01.

Proteomic databases

EPDiO61213.
PaxDbiO61213.
PeptideAtlasiO61213.
PRIDEiO61213.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi171608.
WormBaseiF56C11.1; CE28463; WBGene00000253; bli-3.

Phylogenomic databases

eggNOGiKOG0039. Eukaryota.
ENOG410XNZY. LUCA.
GeneTreeiENSGT00550000074350.
HOGENOMiHOG000231774.
InParanoidiO61213.
KOiK13411.
OMAiILECELT.
OrthoDBiEOG091G00PO.
PhylomeDBiO61213.

Enzyme and pathway databases

BRENDAi1.6.3.1. 1045.
ReactomeiR-CEL-209968. Thyroxine biosynthesis.

Miscellaneous databases

PROiO61213.

Gene expression databases

BgeeiWBGene00000253.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
1.10.640.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR002048. EF_hand_dom.
IPR013112. FAD-bd_8.
IPR017927. Fd_Rdtase_FAD-bd.
IPR013130. Fe3_Rdtase_TM_dom.
IPR013121. Fe_red_NAD-bd_6.
IPR010255. Haem_peroxidase.
IPR019791. Haem_peroxidase_animal.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF03098. An_peroxidase. 1 hit.
PF08022. FAD_binding_8. 1 hit.
PF01794. Ferric_reduct. 1 hit.
PF08030. NAD_binding_6. 1 hit.
[Graphical view]
PRINTSiPR00457. ANPEROXIDASE.
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF48113. SSF48113. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiPS50222. EF_HAND_2. 2 hits.
PS51384. FAD_FR. 1 hit.
PS50292. PEROXIDASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDUOX1_CAEEL
AccessioniPrimary (citable) accession number: O61213
Secondary accession number(s): Q9NH90
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: October 1, 2001
Last modified: November 2, 2016
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.