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Q8HZK2 (DUOX2_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·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):
NADH/NADPH thyroid oxidase p138-tox
Gene names
Name:DUOX2
OrganismSus scrofa (Pig) [Complete proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length1545 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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. Ref.5

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. Note: Localizes to the apical membrane of epithelial cells. Ref.4

Tissue specificity

Expressed in thyroid, and the digestive tract especially in stomach, cecum and sigmoidal colon (at protein level). Expressed in thyroid. Ref.2 Ref.4

Induction

By forskolin and down-regulated by iodide (at protein level). By insulin. Ref.1 Ref.2 Ref.3

Post-translational modification

N-glycosylated. Ref.1

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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 15451520Dual oxidase 2
PRO_0000223350

Regions

Topological domain26 – 601576Extracellular Potential
Transmembrane602 – 62221Helical; Potential
Topological domain623 – 1037415Cytoplasmic Potential
Transmembrane1038 – 105821Helical; Potential
Topological domain1059 – 107416Extracellular Potential
Transmembrane1075 – 109723Helical; Potential
Topological domain1098 – 114548Cytoplasmic Potential
Transmembrane1146 – 116621Helical; Potential
Topological domain1167 – 118216Extracellular Potential
Transmembrane1183 – 120321Helical; Potential
Topological domain1204 – 122017Cytoplasmic Potential
Transmembrane1221 – 124121Helical; Potential
Topological domain12421Extracellular Potential
Transmembrane1243 – 126321Helical; Potential
Topological domain1264 – 1545282Cytoplasmic Potential
Domain819 – 85436EF-hand 1
Domain855 – 89036EF-hand 2
Domain899 – 93436EF-hand 3
Domain1081 – 1263183Ferric oxidoreductase
Domain1264 – 1370107FAD-binding FR-type
Calcium binding832 – 843121 Potential
Calcium binding868 – 879122 Potential
Region30 – 596567Peroxidase-like; mediates peroxidase activity By similarity
Region960 – 1242283Interaction with TXNDC11 By similarity

Amino acid modifications

Glycosylation1001N-linked (GlcNAc...) Potential
Glycosylation3121N-linked (GlcNAc...) Potential
Glycosylation3481N-linked (GlcNAc...) Potential
Glycosylation3581N-linked (GlcNAc...) Potential
Glycosylation4551N-linked (GlcNAc...) Potential
Glycosylation5491N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict15311N → S in AAF20056. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8HZK2 [UniParc].

Last modified October 11, 2004. Version 2.
Checksum: 29A6B1A0C69552DD

FASTA1,545175,284
        10         20         30         40         50         60 
MLCIRPEALV LLGALLTVPL DPVGGQDALS LTWEVQRYDG WFNNLRQHEH GAAGSPLRRL 

        70         80         90        100        110        120 
VPANYADGVY QALGEPLLPN PRQLSHTTMR GPAGLRSIRN RTVLGVFFGY HVLSDLVSIE 

       130        140        150        160        170        180 
KPGCPAEFLN IHIPPGDPVF DPHKSGDVVL PFQRSRWDPN TGQSPSNPRD LTNEVTGWLD 

       190        200        210        220        230        240 
GSAIYGSSHS WSDELRSFSG GQLASGPDPA FPRQAQDPLF MWTPPDPATG QRGPQGLYAF 

       250        260        270        280        290        300 
GAEQGNREPF LQALGLLWFR YHNLCAQKLA REHPLWGDEE LFQHARKRVI ATYQSITMYE 

       310        320        330        340        350        360 
WLPSFLQQTP PNYTEYRPFL DPSISPEFLA ASEQFFSTMV PPGVYMRNAS CHFQMVLNES 

       370        380        390        400        410        420 
YGSFPALRVC NSYWIRENPN LNSAEAVNQL LLGMASQISE LEDWIVVEDL RDYWPGPGKF 

       430        440        450        460        470        480 
SRTDYVASSI QRGRDMGLPS YTQALQALGL NTPKNWSDFN PNVDPQVLEA TAALYNQDLS 

       490        500        510        520        530        540 
RLELFSGGLL ESYGDPGPLF STIVLDQFVR LRDGDRYWFE NTKNGLFSKE EIAEIRSTTL 

       550        560        570        580        590        600 
RDVLVAVTNV SSSALQPNVF IWNEDSPCPQ PQQLTTEDLP HCVPLTVIQY FEGSGPGFGI 

       610        620        630        640        650        660 
TIVALCCLPL MSLLISGVVA YFRSRERKKL QKRGKESVKK EADKDGVSAM EWPGPKERSY 

       670        680        690        700        710        720 
PVSIQLLPDR HLQVLDRHLS VLRTIQLRPR HRVNLILSNN LGRRTLLLKI PKEYDLVLLF 

       730        740        750        760        770        780 
NSEDERGAFV QHLQGFCASC ALGLDIDEMG ESELFRKAVT KQQRGRILEI FFRHLFAQVL 

       790        800        810        820        830        840 
DIDQADAGAL PLDSSQKVRE ALTCELSRAE FAESLGLKPQ DMFVESMFSL ADKDGNGYLS 

       850        860        870        880        890        900 
FREFLDVLVV FMKGSPEDKS RLMFTMYDLD GNGFLSKDEF FTMIRSFIEI SNNCLSKAQL 

       910        920        930        940        950        960 
TEVVESMFRE AGFQDKQELT WEDFHFMLRD HDSELRHTQL CVKGGGGGVG VIFKPDISSR 

       970        980        990       1000       1010       1020 
VSFIIRTPEE RSSPQGVRLP ASEASELGGP VLKKRFGKKA VVPPPRLYTE ALQEKKQRGF 

      1030       1040       1050       1060       1070       1080 
LAQKLQQYKR FVENYRRHIV CVAIFSAICA GLFVERAYYY AFVSPPSGIA ETTFVGIILS 

      1090       1100       1110       1120       1130       1140 
RGTAASVSFM FSYILLTMCR NLITFLRETF LNHYVPFDAA VDFHRWIAMA ALVLAILHSV 

      1150       1160       1170       1180       1190       1200 
GHVVNVYIFS VSPLSLLACV FPSVFVNDGS KLPQKFYWWF FQTIPGMTGV LLLVVLAIMY 

      1210       1220       1230       1240       1250       1260 
VFASPYFRRR SFRGFWLTHH FYILLYVLLI IHGSFALIQL PRFHIFFLVP ALIYVGDKLV 

      1270       1280       1290       1300       1310       1320 
SLSRKKVEIS VVKAELLPSG VTHLQFQRPQ GFEYKSGQWV RIACLGLGTN EYHPFTLTSA 

      1330       1340       1350       1360       1370       1380 
PHEDTLSLHI RAVGPWTTRL REIYSHPMGD GYARYPKLYL DGPFGEGHQE WHKFEVSVLV 

      1390       1400       1410       1420       1430       1440 
GGGIGVTPFA SILKDLVFKS SLGSQMLCKK IYFIWVTRTQ RQFEWLADII REVEENDHRD 

      1450       1460       1470       1480       1490       1500 
LVSVHIYITQ LAEKFDLRTT MLYICERHFQ KVLNRSLFTG LRSITHFGRP PFEPFFNSLQ 

      1510       1520       1530       1540 
EVHPQVRKIG VFSCGPPGMT KNVEKTCQLI NRQDQTHFVH HYENF

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References

[1]"Effect of iodide on nicotinamide adenine dinucleotide phosphate oxidase activity and Duox2 protein expression in isolated porcine thyroid follicles."
Morand S., Chaaraoui M., Kaniewski J., Deme D., Ohayon R., Noel-Hudson M.-S., Virion A., Dupuy C.
Endocrinology 144:1241-1248(2003) [PubMed: 12639906] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], GLYCOSYLATION, INDUCTION.
Tissue: Thyroid.
[2]"Purification of a novel flavoprotein involved in the thyroid NADPH oxidase. Cloning of the porcine and human cDNAs."
Dupuy C., Ohayon R., Valent A., Noel-Hudson M.-S., Deme D., Virion A.
J. Biol. Chem. 274:37265-37269(1999) [PubMed: 10601291] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 339-1545, INDUCTION, TISSUE SPECIFICITY.
Tissue: Thyroid.
[3]"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: INDUCTION.
[4]"Dual oxidase2 is expressed all along the digestive tract."
Ameziane-El-Hassani R., Benfares N., Caillou B., Talbot M., Sabourin J.-C., Belotte V., Morand S., Gnidehou S., Agnandji D., Ohayon R., Kaniewski J., Noel-Hudson M.-S., Bidart J.-M., Schlumberger M., Virion A., Dupuy C.
Am. J. Physiol. 288:G933-G942(2005) [PubMed: 15591162] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[5]"Dual oxidase-2 has an intrinsic Ca2+-dependent H2O2-generating activity."
Ameziane-El-Hassani R., Morand S., Boucher J.L., Frapart Y.-M., Apostolou D., Agnandji D., Gnidehou S., Ohayon R., Noel-Hudson M.-S., Francon J., Lalaoui K., Virion A., Dupuy C.
J. Biol. Chem. 280:30046-30054(2005) [PubMed: 15972824] [Abstract]
Cited for: CATALYTIC ACTIVITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF547267 mRNA. Translation: AAN39339.2.
AF181973 mRNA. Translation: AAF20056.1.
RefSeqNP_999164.2. NM_213999.2.
UniGeneSsc.33.

3D structure databases

ProteinModelPortalQ8HZK2.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8HZK2.

Protein family/group databases

PeroxiBase3340. SscDuOx02.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID397060.
KEGGssc:397060.

Organism-specific databases

CTD50506.

Phylogenomic databases

GeneTreeENSGT00550000074350.
HOVERGENHBG080428.

Family and domain databases

InterProIPR011992. 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.
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...

Entry information

Entry nameDUOX2_PIG
AccessionPrimary (citable) accession number: Q8HZK2
Secondary accession number(s): Q9TT98
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: October 11, 2004
Last modified: November 16, 2011
This is version 65 of the entry and version 2 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents