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Q9ES45 (DUOX2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dual oxidase 2
EC=1.11.1.-
EC=1.6.3.1
Alternative name(s):
Large NOX 2
Long NOX 2
NADH/NADPH thyroid oxidase THOX2
Thyroid oxidase 2
Gene names
Name:Duox2
Synonyms:Lnox2, Thox2
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length1517 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

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 colon, duodenum, rectum and thyroid. Ref.1 Ref.3

Induction

By forskolin, thyrotropin and insulin. Down-regulated by the antithyroid drug methimazole. Ref.1 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.

Sequence caution

The sequence AAN39340.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processHydrogen peroxide
Thyroid hormones biosynthesis
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandCalcium
FAD
NADP
   Molecular functionOxidoreductase
Peroxidase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
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

response to cAMP

Inferred from sequence or structural similarity. Source: UniProtKB

thyroid hormone generation

Traceable author statement Ref.2. Source: RGD

   Cellular componentapical plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionNAD(P)H oxidase activity

Inferred from electronic annotation. Source: EC

calcium ion binding

Inferred from electronic annotation. Source: InterPro

electron carrier activity

Inferred from electronic annotation. Source: InterPro

flavin adenine dinucleotide binding

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...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9ES45-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9ES45-2)

Also known as: short;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1061: Missing.
Note: There is no evidence for the expression of the corresponding protein in vitro.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 15171492Dual oxidase 2
PRO_0000223351

Regions

Topological domain26 – 599574Extracellular Potential
Transmembrane600 – 62021Helical; Potential
Topological domain621 – 1010390Cytoplasmic Potential
Transmembrane1011 – 103121Helical; Potential
Topological domain1032 – 104615Extracellular Potential
Transmembrane1047 – 106721Helical; Potential
Topological domain1068 – 110033Cytoplasmic Potential
Transmembrane1101 – 112121Helical; Potential
Topological domain1122 – 115433Extracellular Potential
Transmembrane1155 – 117521Helical; Potential
Topological domain1176 – 118510Cytoplasmic Potential
Transmembrane1186 – 120621Helical; Potential
Topological domain12071Extracellular Potential
Transmembrane1208 – 122821Helical; Potential
Topological domain1229 – 1517289Cytoplasmic Potential
Domain819 – 85436EF-hand 1
Domain855 – 89036EF-hand 2
Domain899 – 93436EF-hand 3
Domain1053 – 1235183Ferric oxidoreductase
Domain1236 – 1342107FAD-binding FR-type
Calcium binding832 – 843121 Potential
Calcium binding868 – 879122 Potential
Region30 – 596567Peroxidase-like; mediates peroxidase activity By similarity
Region960 – 1214255Interaction with TXNDC11 By similarity

Amino acid modifications

Glycosylation1001N-linked (GlcNAc...) Potential
Glycosylation3481N-linked (GlcNAc...) Potential
Glycosylation4551N-linked (GlcNAc...) Potential
Glycosylation5371N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 10611061Missing in isoform 2.
VSP_017264

Experimental info

Sequence conflict12431V → A in AAN39340. Ref.2
Sequence conflict12461V → A in AAN39340. Ref.2
Sequence conflict14091G → D in AAN39340. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 07FBA427DEA299D1

FASTA1,517171,558
        10         20         30         40         50         60 
MLPTSLKTLV LLGALLTGPL GPAGGQDAPS LPREVQRYDG WFNNLKYHQR GAAGSQLRRL 

        70         80         90        100        110        120 
VPANYADGVY QALQEPLLPN ARLLSDAVSK GKAGLPSAHN RTVLGLFFGY HVLSDLVSVE 

       130        140        150        160        170        180 
TPGCPAEFLN IYIPRGDPVF DPDKRGNVVL PFQRSRWDRS TGQSPSNPRD LTNQVTGWLD 

       190        200        210        220        230        240 
GSAIYGSSHS WSDTLRSFSG GQLASGPDPA FPRNSQNSLL MWMAPDPATG QGGPQGLYAF 

       250        260        270        280        290        300 
GAQRGNREPF LQALGLLWFR YHNLCAKRLA QEHPHWGDEE LFQHARKRVI ATYQNIALYQ 

       310        320        330        340        350        360 
WLPSFLQKTP PEYSGYRPFM DPSISPEFVA ASEQFLSTMV PPGVYMRNSS CHFREFPKEG 

       370        380        390        400        410        420 
SSSSPALRVC NNYWIRENPS LKTAQDVDQL LLGMASQISE LEDRIVIEDL RDYWPGPDRY 

       430        440        450        460        470        480 
SRTDYVASSI QSGRDMGLPS YSQALQALGL EPPKNWSALN PKVDPQVLEA TAALYNQDLS 

       490        500        510        520        530        540 
RLELFLGGLL ESHGDPGPLF SNIILDQFVR LRDGDRYWFE NTRNGLFSKE EIAEIRNTTL 

       550        560        570        580        590        600 
RDVLVAVSNV DPSALQPNVF FWQEGAPCPQ PQQLTTEGLP QCVPVTVIDY FEGSGAGYGV 

       610        620        630        640        650        660 
TLLAVCCFPV VSLIIAWVVA RFRNRERKML LKKGKESLKK QTASDGVPAM EWPGPKESSY 

       670        680        690        700        710        720 
PVTVQLLPDR SLKVLDKRLT VLRTIQLQPT QQVNLILSSS HGRRTLLLKI PKEYDLVLMF 

       730        740        750        760        770        780 
NSEEDRDAFV QLLQDLCVCS TPGLRIAEMD EKELLRKAVT KQQRAGILEI FFRQLFAQVL 

       790        800        810        820        830        840 
DINQADAGTL PLDSSQQVRE ALTCELSRAE FADSLGLKPQ DMFVESMFSL ADKDGNGYIS 

       850        860        870        880        890        900 
FREFLDILVV FMKGSPQDKS RLMFTMYDLD GNGFLSKEEF FTMMRSFIEI SNNCLSKDQL 

       910        920        930        940        950        960 
AEVVESMFRE SGFQDKEELT WEDFHFMLRD HDSDLRFTQL CVKGGAGGTG DIFKQSNACR 

       970        980        990       1000       1010       1020 
VSFLTRTPGN RVMAPSPRLY TEALQEKMQR GFLAQKLKQF KRFVENYRRH IVCVTIFSAI 

      1030       1040       1050       1060       1070       1080 
CAGLFADRAY YYGFASPPTD IEETTYVGII LSRGTAASIS FMFSYILLTM CRNLITFLRE 

      1090       1100       1110       1120       1130       1140 
TFLNRYIPFD AAVDFHRWIA MAAVVLAVVH SLGHAVNVYI FSVSPLSLMT CVFPSVFVND 

      1150       1160       1170       1180       1190       1200 
GSKLPPKYYW WFFETVPGMT GVLLLLVLAI MYVFASHHFR RHSFRGFWLT HHLYVVLYAL 

      1210       1220       1230       1240       1250       1260 
IIIHGSYALI QLPSFHIYFL VPAIIYVGDK LVSLSRKKVE ISVVKVELLP SGVTYLQFQR 

      1270       1280       1290       1300       1310       1320 
PKTFEYKSGQ WVRIACLSLG TNEYHPFTLT SAPHEDTLSL HIRAVGPWTT RLREIYSPPV 

      1330       1340       1350       1360       1370       1380 
GGTSARYPKL YLDGPFGEGH QEWHKFEVSV LVGGGIGVTP FASILKDLVF KSSMGTQMLC 

      1390       1400       1410       1420       1430       1440 
KKIYFIWVTR TQRQFEWLAD IIREVEENGS RDLVSVHIYI TQLAEKFDLR TTMLYICERH 

      1450       1460       1470       1480       1490       1500 
FQKVLNRSLF TGLRSVTHFG RPPFELFLDS LQEVHPQVHK IGVFSCGPPG MTKNVEKACQ 

      1510 
LINRQDRAHF VHHYENF

« Hide

Isoform 2 (short) [UniParc].

Checksum: B39E79E45F2DF3FE
Show »

FASTA45652,576

References

[1]"Thyroid oxidase (THOX2) gene expression in the rat thyroid cell line FRTL-5."
Dupuy C., Pomerance M., Ohayon R., Noel-Hudson M.-S., Deme D., Chaaraoui M., Francon J., Virion A.
Biochem. Biophys. Res. Commun. 277:287-292(2000) [PubMed: 11032719] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INDUCTION.
Tissue: Thyroid.
[2]"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] (ISOFORM 2), INDUCTION.
Strain: Fischer.
[3]"Dual oxidases represent novel hydrogen peroxide sources supporting mucosal surface host defense."
Geiszt M., Witta J., Baffi J., Lekstrom K., Leto T.L.
FASEB J. 17:1502-1504(2003) [PubMed: 12824283] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF237962 mRNA. Translation: AAG21895.1.
AF547268 mRNA. Translation: AAN39340.1. Different initiation.
IPIIPI00191453.
IPI00734574.
RefSeqNP_077055.1. NM_024141.1.
UniGeneRn.55542.

3D structure databases

ProteinModelPortalQ9ES45.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9ES45.

Protein family/group databases

PeroxiBase3971. RnoDuOx02-b.
3972. RnoDuOx02-a.

PTM databases

PhosphoSiteQ9ES45.

Proteomic databases

PRIDEQ9ES45.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID79107.
KEGGrno:79107.
UCSCNM_024141. rat.

Organism-specific databases

CTD50506.
RGD628761. Duox2.

Phylogenomic databases

eggNOGroNOG12698.
GeneTreeENSGT00550000074350.
HOVERGENHBG080428.
InParanoidQ9ES45.
PhylomeDBQ9ES45.

Gene expression databases

ArrayExpressQ9ES45.
GenevestigatorQ9ES45.
GermOnlineENSRNOG00000017395. Rattus norvegicus.

Family and domain databases

InterProIPR018248. EF-hand.
IPR011992. EF-hand-like_dom.
IPR018247. EF_Hand_1_Ca_BS.
IPR018249. EF_HAND_2.
IPR002048. EF_hand_Ca-bd.
IPR013112. FAD-bd_8.
IPR017927. Fd_Rdtase_FAD-bd.
IPR013121. Fe_red_NAD-bd_6.
IPR013130. Flavoprotein_TM.
IPR010255. Haem_peroxidase.
IPR002007. Haem_peroxidase_animal.
IPR019791. Haem_peroxidase_animal_subgr.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
Gene3DG3DSA:1.10.238.10. EF-Hand_type. 1 hit.
G3DSA:1.10.640.10. Haem_peroxidase_animal. 2 hits.
KOK13411.
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.
SMARTSM00054. EFh. 2 hits.
[Graphical view]
SUPFAMSSF48113. Peroxidase_super. 1 hit.
SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
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

NextBio614498.

Entry information

Entry nameDUOX2_RAT
AccessionPrimary (citable) accession number: Q9ES45
Secondary accession number(s): Q811Y4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: March 1, 2001
Last modified: November 16, 2011
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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