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Reviewed, UniProtKB/Swiss-Prot Q8CIY2 (DUOX1_RAT)

Last modified June 16, 2009. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Dual oxidase 1
    EC=1.6.3.1
    EC=1.11.1.-
Gene names
Name: Duox1
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length1551 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Generates hydrogen peroxide which is required for the activity of thyroid peroxidase/TPO and lactoperoxidase/LPO. Plays a role in thyroid hormones synthesis and lactoperoxidase-mediated antimicrobial defense at the surface of mucosa. May have its own peroxidase activity through its N-terminal peroxidase-like domain.

Catalytic activity

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

Enzyme regulation

The NADPH oxidase activity is calcium-dependent. Peroxidase activity is inhibited by aminobenzohydrazide By similarity.

Pathway

Hormone biosynthesis; thyroid hormone biosynthesis.

Subunit structure

Interacts with TXNDC11, TPO and CYBA By similarity.

Subcellular location

Apical cell membrane; Multi-pass membrane protein By similarity. Note: Localizes to the apical membrane of epithelial cells By similarity.

Tissue specificity

Expressed in thyrocytes (at protein level). Ref.2

Post-translational modification

N-glycosylated By similarity.

Sequence similarities

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

Contains 3 EF-hand domains.

Contains 1 FAD-binding FR-type domain.

Contains 1 ferric oxidoreductase domain.

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Ontologies

Keywords
   Biological processHydrogen peroxide
Thyroid hormones biosynthesis
   Cellular componentCell membrane
Membrane
   DomainRepeat
Signal
Transmembrane
   LigandCalcium
FAD
NADP
   Molecular functionOxidoreductase
Peroxidase
   PTMGlycoprotein
Gene Ontology (GO)
   Biological processcuticle development

Inferred from sequence or structural similarity. Source: UniProtKB

cytokine-mediated signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

hormone biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

hydrogen peroxide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

response to cAMP

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular componentapical plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionFAD binding

Inferred from electronic annotation. Source: InterPro

NAD(P)H oxidase activity

Inferred from electronic annotation. Source: EC

calcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

electron carrier activity

Inferred from electronic annotation. Source: InterPro

heme binding

Inferred from electronic annotation. Source: InterPro

peroxidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 15511530Dual oxidase 1
PRO_0000223346

Regions

Topological domain22 – 596575Extracellular Potential
Transmembrane597 – 61721 Potential
Topological domain618 – 1044427Cytoplasmic Potential
Transmembrane1045 – 106521 Potential
Topological domain1066 – 108015Extracellular Potential
Transmembrane1081 – 110121 Potential
Topological domain1102 – 113635Cytoplasmic Potential
Transmembrane1137 – 115721 Potential
Topological domain1158 – 118831Extracellular Potential
Transmembrane1189 – 120921 Potential
Topological domain1210 – 122617Cytoplasmic Potential
Transmembrane1227 – 124721 Potential
Topological domain12481Extracellular Potential
Transmembrane1249 – 126921 Potential
Topological domain1270 – 1551282Cytoplasmic Potential
Domain815 – 85036EF-hand 1
Domain851 – 88636EF-hand 2
Domain895 – 93036EF-hand 3
Domain1087 – 1269183Ferric oxidoreductase
Domain1270 – 1376107FAD-binding FR-type
Calcium binding828 – 839121 Potential
Calcium binding864 – 875122 Potential
Region26 – 593568Peroxidase-like; mediates peroxidase activity By similarity
Region956 – 1248293Interaction with TXNDC11 By similarity

Amino acid modifications

Glycosylation941N-linked (GlcNAc...) Potential
Glycosylation3421N-linked (GlcNAc...) Potential
Glycosylation3541N-linked (GlcNAc...) Potential
Glycosylation4611N-linked (GlcNAc...) Potential
Glycosylation5341N-linked (GlcNAc...) Potential

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Sequences

Sequence LengthMass (Da)Tools
Q8CIY2-1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 52B07F83EF4E1FE2

FASTA1,551177,197
        10         20         30         40         50         60 
MAVYSAVAWI LLFGVLASLG AQNPVSWEVQ RFDGWYNNLM EHRWGSKGSR LQRLVPASYA 

        70         80         90        100        110        120 
DGVYQPLREP YLPNPRHLSN RVMRGPAGQP SLRNRTVLGV FFGYHVLSDL VSVETPGCPA 

       130        140        150        160        170        180 
EFLNIYIPRG DPVFDPDKRG NVVLPFQRSR WDRSTGQSPS NPRDLTNQVT GWLDGSAIYG 

       190        200        210        220        230        240 
SSHSWSDTLR SFSGGQLASG PDPAFPRNSQ NSLLMWMAPD PATGQGGPQG LYAFGAQRGN 

       250        260        270        280        290        300 
REPFLQALGL LWFRYHNLCA KRLAQEHPHW GDEELFQHAR KRVIATYQNI AMYEWLPSFL 

       310        320        330        340        350        360 
KQTPPEYPGY HPFLDPSISP EFVVASEQFL STMVPPGVYM RNASCHFQGI ANRNSSVSGA 

       370        380        390        400        410        420 
LRVCNSYWSR ENPKLQRAED VDALLLGMAS QIAEREDHLV VEDVQDFWPG PLKFSRTDYL 

       430        440        450        460        470        480 
ASCLQRGRDL GLPSYTKARE ALGLPPVSHW QDINPALSRS NGTVLEATAA LYNQDLSRLE 

       490        500        510        520        530        540 
LLAGGLLESH GDPGPLFSAI VLDQFVRLRD GDRYWFENNR NGLFSKEEIA EIRNTSLRDI 

       550        560        570        580        590        600 
LVAVTNVDPS ALQPSVFFWL AGDPCPQPSQ LSTQGLPACA PLFVRDYFKG SGFGFGLTIG 

       610        620        630        640        650        660 
TLCCFPLVSL LSAWIVARLR MRNFKRLQRQ DRQSIMCEKL VGGVEALEWQ GRKEPCRPVL 

       670        680        690        700        710        720 
VHLQPGQIRV VDGRLTVLRT IQLRPPQQVN LILSSNRGRR TLLLKIPKEY DLVLLFNMEE 

       730        740        750        760        770        780 
ERQALVENIR AALKENGLSF QEWELREQEL MRAAVTRQQR GHLLETFFRH LFSQVLDINQ 

       790        800        810        820        830        840 
ADAGTLPLDS STKVREALTC ELSRAEFADS LGLKPQDMFV ESMFSLADKD GNGYLSFREF 

       850        860        870        880        890        900 
LDILVVFMKG SPEEKSRLMF RMYDFDGNGL ISKDEFIRML RSFIEISNNC LSKDQLAEVV 

       910        920        930        940        950        960 
ESMFRESGFQ DKEELTWEDF HFMLRDHDSD LRFTQLCVKG VEVPEVIKNL CRRASYISQE 

       970        980        990       1000       1010       1020 
KICPSPRMSA HCARNNTKTA SSPQRLQCPV DTDPPQEIRR RFGKKVTSFQ PLLFTEAHRE 

      1030       1040       1050       1060       1070       1080 
KFQRSRRHQT VQQFKRFIEN YRRHIGCVAV FYTITGALFL ERAYYYAFAA HHSGITDTTR 

      1090       1100       1110       1120       1130       1140 
VGIILSRGTA ASISFMFSYI LLTMCRNLIT FLRETFLNRY IPFDAAVDFH RFIASTAIIL 

      1150       1160       1170       1180       1190       1200 
TVLHSAGHVV NVYLFSISPL SVLSCLFPDL FHDDGSEFPQ KYYWWFFQTV PGLTGVLLLL 

      1210       1220       1230       1240       1250       1260 
ALAIMYVFAS HHFRRRSFRG FWLTHHLYIF LYILLIIHGS FALIQMPRFH IFFLVPAIIY 

      1270       1280       1290       1300       1310       1320 
VGDKLVSLSR KKVEISVVKA ELLPSGVTHL RFQRPQGFEY KSGQWVRIAC LALGTTEYHP 

      1330       1340       1350       1360       1370       1380 
FTLTSAPHED TLSLHIRAAG PWTTRLREIY SPPTGDTCAR YPKLYLDGPF GEGHQEWHKF 

      1390       1400       1410       1420       1430       1440 
EVSVLVGAGI GVTPFASILK DLVFKSSVSC QVFCKKIYFI WVTRTQRQFE WLADIIREVE 

      1450       1460       1470       1480       1490       1500 
ENDSRDLVSV HIYITQLAEK FDLRTTMLYI CERHFQKVLN RSLFTGLRSV THFGRPPFEP 

      1510       1520       1530       1540       1550 
FFNSLQEVHP QVRKIGVFSC GPPGMTKNVE KACQLINKQD RTHFSHHYEN F

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References

[1]"Identification of a truncated dual oxidase 2 (DUOX2) messenger ribonucleic acid (mRNA) in two rat thyroid cell lines. Insulin and forskolin regulation of DUOX2 mRNA levels in FRTL-5 cells and porcine thyrocytes."
Morand S., Dos Santos O.F., Ohayon R., Kaniewski J., Noel-Hudson M.-S., Virion A., Dupuy C.
Endocrinology 144:567-574(2003) [PubMed: 12538618] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Fischer 344.
[2]"Cloning of two human thyroid cDNAs encoding new members of the NADPH oxidase family."
De Deken X., Wang D., Many M.-C., Costagliola S., Libert F., Vassart G., Dumont J.E., Miot F.
J. Biol. Chem. 275:23227-23233(2000) [PubMed: 10806195] [Abstract]
Cited for: TISSUE SPECIFICITY.

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Cross-references

Sequence databases

AF542180 mRNA. Translation: AAN33120.1.
IPIIPI00194282.
RefSeqNP_714961.1.
UniGeneRn.162682

3D structure databases

HSSPHSSP built from PDB template 1RRO based on UniProtKB P02631.
ModBaseSearch...

Protein family/group databases

PeroxiBase3970. RnoDuOx01.

Genome annotation databases

EnsemblENSRNOG00000033348. Rattus norvegicus. [Contig view]
GeneID266807.
KEGGrno:266807.

Organism-specific databases

RGD628760. Duox1.

Phylogenomic databases

HOVERGENQ8CIY2.

Enzyme and pathway databases

BRENDA1.6.3.1. 248.

Family and domain databases

InterProIPR011992. EF-Hand_type.
IPR018248. EF_hand.
IPR018247. EF_HAND_1.
IPR018249. EF_HAND_2.
IPR002048. EF_hand_Ca_bd.
IPR013112. FAD_bd_8.
IPR017927. Fd_Rdtase_FAD-bd.
IPR013130. Fe3_reduct_TM_N.
IPR013121. Fe_red_NAD_bd_6.
IPR002007. Haem_peroxidase_animal.
IPR019791. Haem_peroxidase_animal_sg.
[Graphical view]
Gene3DG3DSA:1.10.238.10. EF-Hand_type. 1 hit.
G3DSA:1.10.640.10. Haem_peroxidase_animal. 1 hit.
PfamPF03098. An_peroxidase. 1 hit.
PF00036. efhand. 2 hits.
PF08022. FAD_binding_8. 1 hit.
PF01794. Ferric_reduct. 1 hit.
PF08030. NAD_binding_6. 1 hit.
[Graphical view]
PRINTSPR00457. ANPEROXIDASE.
ProDomPD000012. EF-hand. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00054. EFh. 2 hits.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
PS51384. FAD_FR. 1 hit.
PS50292. PEROXIDASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio624725.

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Entry information

Entry nameDUOX1_RAT
AccessionPrimary (citable) accession number: Q8CIY2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: March 1, 2003
Last modified: June 16, 2009
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents