Dual oxidase 1 precursor - Caenorhabditis elegans

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O61213 (DUOX1_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 101. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Dual oxidase 1
Short name=DUOX1
EC=1.11.1.-
EC=1.6.3.1

Alternative name(s):
Blistered cuticle protein 3
NADPH thyroid oxidase 1

Gene names

Name:	bli-3
ORF Names:	F56C11.1

Organism

Caenorhabditis elegans [Reference proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Ecdysozoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	1497 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays a role in cuticle biogenesis. May stabilize cuticular extracellular matrix by cross-linking proteins through its peroxidase activity. Ref.1
Catalytic activity	NAD(P)H + O₂ = NAD(P)⁺ + H₂O₂. Ref.1
Enzyme regulation	Peroxidase activity is inhibited by aminobenzohydrazide. Ref.1
Subcellular location	Membrane; Multi-pass membrane protein By similarity.
Tissue specificity	Expressed in hypodermal cells. Ref.1
Sequence similarities	In the N-terminal section; belongs to the peroxidase family. Contains 2 EF-hand domains. Contains 1 FAD-binding FR-type domain. Contains 1 ferric oxidoreductase domain.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Cellular component	Membrane
Domain	Repeat Signal Transmembrane Transmembrane helix
Ligand	Calcium FAD NADP
Molecular function	Oxidoreductase Peroxidase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cuticle development involved in collagen and cuticulin-based cuticle molting cycle Inferred from genetic interaction PubMed 19406744. Source: WormBase hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW nematode larval development Inferred from genetic interaction PubMed 19406744. Source: WormBase peptide cross-linking Inferred from direct assay PubMed 19460756. Source: WormBase post-embryonic body morphogenesis Inferred from genetic interaction PubMed 19406744. Source: WormBase response to oxidative stress Inferred from genetic interaction PubMed 18460651. Source: WormBase
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	NAD(P)H oxidase activity Inferred from electronic annotation. Source: EC calcium ion binding Inferred from electronic annotation. Source: InterPro heme binding Inferred from direct assay PubMed 19460756. Source: WormBase peroxidase activity Inferred from direct assay PubMed 19460756. Source: WormBase
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

Potential

Chain

22 – 1497

1476

Dual oxidase 1

PRO_0000223348

Regions

Topological domain

22 – 587

566

Extracellular Potential

Transmembrane

588 – 608

Helical; Potential

Topological domain

609 – 986

378

Cytoplasmic Potential

Transmembrane

987 – 1007

Helical; Potential

Topological domain

1008 – 1024

Extracellular Potential

Transmembrane

1025 – 1045

Helical; Potential

Topological domain

1046 – 1068

Cytoplasmic Potential

Transmembrane

1069 – 1089

Helical; Potential

Topological domain

1090 – 1134

Extracellular Potential

Transmembrane

1135 – 1155

Helical; Potential

Topological domain

1156 – 1163

Cytoplasmic Potential

Transmembrane

1164 – 1184

Helical; Potential

Topological domain

1185 – 1189

Extracellular Potential

Transmembrane

1190 – 1210

Helical; Potential

Topological domain

1211 – 1497

287

Cytoplasmic Potential

Domain

817 – 852

EF-hand 1

Domain

853 – 888

EF-hand 2

Domain

1030 – 1210

181

Ferric oxidoreductase

Domain

1211 – 1318

108

FAD-binding FR-type

Region

26 – 590

565

Peroxidase-like; mediates peroxidase activity

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Ref.3

Glycosylation

305

N-linked (GlcNAc...) Potential

Glycosylation

567

N-linked (GlcNAc...) Potential

Glycosylation

586

N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict

105

Y → H in AAF71303. Ref.1

Sequence conflict

829

T → I in AAF71303. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

O61213 [UniParc].

Last modified October 1, 2001. Version 2.
Checksum: 6C648F193796A730
Show »

FASTA

1,497

170,416

        10         20         30         40         50         60 
MRSKHVLYIA ILFSSIFGGK GIQQNEEFQR YDGWYNNLAN SEWGSAGSRL HRDARSYYSD 

        70         80         90        100        110        120 
GVYSVNNSLP SARELSDILF KGESGIPNTR GCTTLLAFFS QVVAYEIMQS NGVSCPLETL 

       130        140        150        160        170        180 
KIQVPLCDNV FDKECEGKTE IPFTRAKYDK ATGNGLNSPR EQINERTSWI DGSFIYGTTQ 

       190        200        210        220        230        240 
PWVSSLRSFK QGRLAEGVPG YPPLNNPHIP LNNPAPPQVH RLMSPDRLFM LGDSRVNENP 

       250        260        270        280        290        300 
GLLSFGLILF RWHNYNANQI HREHPDWTDE QIFQAARRLV IASMQKIIAY DFVPGLLGED 

       310        320        330        340        350        360 
VRLSNYTKYM PHVPPGISHA FGAAAFRFPH SIVPPAMLLR KRGNKCEFRT EVGGYPALRL 

       370        380        390        400        410        420 
CQNWWNAQDI VKEYSVDEII LGMASQIAER DDNIVVEDLR DYIFGPMHFS RLDVVASSIM 

       430        440        450        460        470        480 
RGRDNGVPPY NELRRTFGLA PKTWETMNED FYKKHTAKVE KLKELYGGNI LYLDAYVGGM 

       490        500        510        520        530        540 
LEGGENGPGE LFKEIIKDQF TRIRDGDRFW FENKLNGLFT DEEVQMIHSI TLRDIIKATT 

       550        560        570        580        590        600 
DIDETMLQKD VFFFKEGDPC PQPFQVNTTG LEPCVPFMQS TYWTDNDTTY VFTLIGLACV 

       610        620        630        640        650        660 
PLICYGIGRY LVNRRIAIGH NSACDSLTTD FANDDCGAKG DIYGVNALEW LQEEYIRQVR 

       670        680        690        700        710        720 
IEIENTTLAV KKPRGGILRK IRFETGQKIE LFHSMPNPSA MHGPFVLLSQ KNNHHLVIRL 

       730        740        750        760        770        780 
SSDRDLSKFL DQIRQAASGI NAEVIIKDEE NSILLSQAIT KERRQDRLDL FFREAYAKAF 

       790        800        810        820        830        840 
NDSELQDSET SFDSSNDDIL NETISREELA SAMGMKANNE FVKRMFAMTA KHNEDSLSFN 

       850        860        870        880        890        900 
EFLTVLREFV NAPQKQKLQT LFKMCDLEGK NKVLRKDLAE LVKSLNQTAG VHITESVQLR 

       910        920        930        940        950        960 
LFNEVLHYAG VSNDAKYLTY DDFNALFSDI PDKQPVGLPF NRKNYQPSIG ETSSLNSFAV 

       970        980        990       1000       1010       1020 
VDRSINSSAP LTLIHKVSAF LETYRQHVFI VFCFVAINLV LFFERFWHYR YMAENRDLRR 

      1030       1040       1050       1060       1070       1080 
VMGAGIAITR GAAGALSFCM ALILLTVCRN IITLLRETVI AQYIPFDSAI AFHKIVALFA 

      1090       1100       1110       1120       1130       1140 
AFWATLHTVG HCVNFYHVGT QSQEGLACLF QEAFFGSNFL PSISYWFFST ITGLTGIALV 

      1150       1160       1170       1180       1190       1200 
AVMCIIYVFA LPCFIKRAYH AFRLTHLLNI AFYALTLLHG LPKLLDSPKF GYYVVGPIVL 

      1210       1220       1230       1240       1250       1260 
FVIDRIIGLM QYYKKLEIVN AEILPSDIIY IEYRRPREFK YKSGQWVTVS SPSISCTFNE 

      1270       1280       1290       1300       1310       1320 
SHAFSIASSP QDENMKLYIK AVGPWTWKLR SELIRSLNTG SPFPLIHMKG PYGDGNQEWM 

      1330       1340       1350       1360       1370       1380 
DYEVAIMVGA GIGVTPYAST LVDLVQRTSS DSFHRVRCRK VYFLWVCSTH KNYEWFVDVL 

      1390       1400       1410       1420       1430       1440 
KNVEDQARSG ILETHIFVTQ TFHKFDLRTT MLYICEKHFR ATNSGISMFT GLHAKNHFGR 

      1450       1460       1470       1480       1490 
PNFKAFFQFI QSEHKEQSKI GVFSCGPVNL NESIAEGCAD ANRQRDAPSF AHRFETF

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Tyrosine cross-linking of extracellular matrix is catalyzed by Duox, a multidomain oxidase/peroxidase with homology to the phagocyte oxidase subunit gp91phox." Edens W.A., Sharling L., Cheng G., Shapira R., Kinkade J.M., Lee T., Edens H.A., Tang X., Sullards C., Flaherty D.B., Benian G.M., Lambeth J.D. J. Cell Biol. 154:879-891(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, TISSUE SPECIFICITY.
[2]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.
[3]	"Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis elegans and suggests an atypical translocation mechanism for integral membrane proteins." Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T., Taoka M., Takahashi N., Isobe T. Mol. Cell. Proteomics 6:2100-2109(2007) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-66, MASS SPECTROMETRY. Strain: Bristol N2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF229855 mRNA. Translation: AAF71303.1. FO081456 Genomic DNA. Translation: CCD71714.1.
PIR	T29025.
RefSeq	NP_490686.3. NM_058285.4.
3D structure databases
ProteinModelPortal	O61213.
SMR	O61213. Positions 24-548, 1306-1476.
ModBase	Search...
Protein-protein interaction databases
STRING	6239.F56C11.1.
Protein family/group databases
PeroxiBase	3349. CelDuOx01.
Proteomic databases
PaxDb	O61213.
PRIDE	O61213.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	F56C11.1; F56C11.1; F56C11.1.
GeneID	171608.
KEGG	cel:CELE_F56C11.1.
UCSC	F56C11.1. c. elegans.
Organism-specific databases
CTD	171608.
WormBase	F56C11.1; CE28463; WBGene00000253; bli-3.
Phylogenomic databases
eggNOG	NOG287712.
GeneTree	ENSGT00550000074350.
HOGENOM	HOG000231774.
InParanoid	O61213.
KO	K13411.
OMA	PNVDPQV.
Family and domain databases
Gene3D	1.10.238.10. 1 hit. 1.10.640.10. 1 hit.
InterPro	IPR011992. EF-hand-like_dom. 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. IPR002007. Haem_peroxidase_animal. IPR019791. Haem_peroxidase_animal_subgr. IPR017938. Riboflavin_synthase-like_b-brl. [Graphical view]
Pfam	PF03098. An_peroxidase. 1 hit. PF08022. FAD_binding_8. 1 hit. PF01794. Ferric_reduct. 1 hit. PF08030. NAD_binding_6. 1 hit. [Graphical view]
PRINTS	PR00457. ANPEROXIDASE.
SMART	SM00054. EFh. 2 hits. [Graphical view]
SUPFAM	SSF48113. Peroxidase_super. 1 hit. SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
PROSITE	PS00018. EF_HAND_1. False negative. PS50222. EF_HAND_2. 2 hits. PS51384. FAD_FR. 1 hit. PS50292. PEROXIDASE_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	871991.

Entry information

Entry name

DUOX1_CAEEL

Accession

Primary (citable) accession number: O61213
Secondary accession number(s): Q9NH90

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2006
Last sequence update:	October 1, 2001
Last modified:	May 1, 2013
This is version 101 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project

Relevant documents

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormBase

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents