Dual oxidase 1 precursor - Sus scrofa (Pig)

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Q8HZK3 (DUOX1_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 74. 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
EC=1.11.1.-
EC=1.6.3.1

Gene names

Name:

DUOX1

Organism

Sus scrofa (Pig) [Reference proteome]

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	1553 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Specifically expressed in thyroid. 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.

Ontologies

Keywords
Biological process	Hydrogen peroxide Thyroid hormones biosynthesis
Cellular component	Cell membrane Membrane
Domain	Repeat Signal Transmembrane Transmembrane helix
Ligand	Calcium FAD Metal-binding NADP
Molecular function	Oxidoreductase Peroxidase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cuticle 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 Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	apical plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell 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 electronic annotation. Source: InterPro peroxidase activity Inferred from electronic annotation. Source: UniProtKB-KW
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 – 1553

1532

Dual oxidase 1

PRO_0000223345

Regions

Topological domain

22 – 596

575

Extracellular Potential

Transmembrane

597 – 617

Helical; Potential

Topological domain

618 – 1046

429

Cytoplasmic Potential

Transmembrane

1047 – 1067

Helical; Potential

Topological domain

1068 – 1082

Extracellular Potential

Transmembrane

1083 – 1103

Helical; Potential

Topological domain

1104 – 1138

Cytoplasmic Potential

Transmembrane

1139 – 1159

Helical; Potential

Topological domain

1160 – 1190

Extracellular Potential

Transmembrane

1191 – 1211

Helical; Potential

Topological domain

1212 – 1228

Cytoplasmic Potential

Transmembrane

1229 – 1249

Helical; Potential

Topological domain

1250

Extracellular Potential

Transmembrane

1251 – 1271

Helical; Potential

Topological domain

1272 – 1553

282

Cytoplasmic Potential

Domain

815 – 850

EF-hand 1

Domain

851 – 886

EF-hand 2

Domain

895 – 930

EF-hand 3

Domain

1089 – 1271

183

Ferric oxidoreductase

Domain

1272 – 1378

107

FAD-binding FR-type

Calcium binding

828 – 839

1 Potential

Calcium binding

864 – 875

2 Potential

Region

26 – 593

568

Peroxidase-like; mediates peroxidase activity By similarity

Region

956 – 1250

295

Interaction with TXNDC11 By similarity

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

342

N-linked (GlcNAc...) Potential

Glycosylation

354

N-linked (GlcNAc...) Potential

Glycosylation

534

N-linked (GlcNAc...) Potential

Sequences

Sequence

Length

Mass (Da)

Tools

Q8HZK3 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 9F9364322977B710
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FASTA

1,553

177,861

        10         20         30         40         50         60 
MGFRLALAWT LLVGPWMPMG ARNSISWEVQ RFDGWYNNLM EHKWGSKGSR LQRLVPASYA 

        70         80         90        100        110        120 
DGVYQPLGEP HLPNPRDLSN TAMRGPAGQA SLRNRTVLGV FFGYHVLSDL VSIEKPGCPA 

       130        140        150        160        170        180 
EFLNIHIPPG DPVFDPHKSG DVVLPFQRSR WDPNTGQSPS NPRDLTNEVT GWLDGSAIYG 

       190        200        210        220        230        240 
SSHSWSDELR SFSGGQLASG PDPAFPRQAQ DPLFMWTPPD PATGQRGPQG LYAFGAEQGN 

       250        260        270        280        290        300 
REPFLQALGL LWFRYHNLCA QKLAREHPLW GDEELFQHAR KRVIATYQSI TMYEWLPSFL 

       310        320        330        340        350        360 
RKMPQEYTGY RPFLDPSISP EFLAASEQFF STMVPPGVYM RNASCHFQGV INRNSSVSRA 

       370        380        390        400        410        420 
LRVCNSYWSR EHPNLQRAED VDALLLGMAS QIAEREDHMV VEDVQDFWPG PLKFSRTDHL 

       430        440        450        460        470        480 
ASCLQRGRDL GLPSYTKARA RLGLPPVTRW QDINPALSRS DGIVLEATAA LYNQDLSRLE 

       490        500        510        520        530        540 
LLPGGLLESY GDPGPLFSTI VLDQFVRLRD GDRYWFENTK NGLFSEKEIA EIRNTSLRDV 

       550        560        570        580        590        600 
LVAVTNMTPG ALQPNVFFWH AGDPCPQPRQ LSTKDLPACA PLIMRDYFKG SGFGFGVTIG 

       610        620        630        640        650        660 
TLCCFPLVSL LSAWIVAQLR RRNFKRLQVQ NRQSIMCEKL VGGMKALEWQ GRKEPCRPVL 

       670        680        690        700        710        720 
VHLQSGQIHV MDGRLSVLRT IQLRPPQQVN LILSSNHGRR TLLLKIPKEY DLVLMFDLEE 

       730        740        750        760        770        780 
ERQVMVENLQ SALKESGLSF QEWELREQEL MRAAVTREQR SHLLETFFRH LFSQVLDIDQ 

       790        800        810        820        830        840 
ADAGALPLDS SQKVREALTC ELSRAEFAES LGLKPQDMFV ESMFSLADKD GNGYLSFREF 

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

       910        920        930        940        950        960 
ESMFREAGFQ DKQELTWEDF HFMLRDHDSE LRFTQLCVKG VEVPEVIKDL CRRASYISQE 

       970        980        990       1000       1010       1020 
KLCPSPRVSA HCPRSNVDVE VELTPWKLQC PTDTDPPQEI RRRFGKKVTS FQPLLFTEAH 

      1030       1040       1050       1060       1070       1080 
REKFQRSRRH QTVQQFKRFV ENYRRHIGCL AVFYTIAGGL FLERAYYYAF AAHHMGITDT 

      1090       1100       1110       1120       1130       1140 
TRVGIILSRG TAASISFMFS YILLTMCRNL ITFLRETFLN RYVPFDAAVD FHRLIASTAI 

      1150       1160       1170       1180       1190       1200 
ILTVLHSAGH VVNVYLFSIS PLSVLSCLFP GLFHDNGSEF PQKYYWWFFQ TVPGLTGVML 

      1210       1220       1230       1240       1250       1260 
LLILAIMYVF ASHHFRRCSF RGFWLTHHLY ILLYMLLIIH GSFALIQLPR FHIFFLVPAL 

      1270       1280       1290       1300       1310       1320 
IYVGDKLVSL SRKKVEISVV KAELLPSGVT HLQFQRPQGF EYKSGQWVRI ACLALGTTEY 

      1330       1340       1350       1360       1370       1380 
HPFTLTSAPH EDTLSLHIRA AGPWTTRLRE IYSPPTDDNC AKYPKLYLDG PFGEGHQEWH 

      1390       1400       1410       1420       1430       1440 
KFEVSVLVGG GIGVTPFASI LKDLVFKSSV SCQVFCKKIY FIWVTRTQRQ FEWLADIIRE 

      1450       1460       1470       1480       1490       1500 
VEENDHRDLV SVHIYITQLA EKFDLRTTML YICERHFQKV LNRSLFTGLR SITHFGRPPF 

      1510       1520       1530       1540       1550 
EPFFNSLQEV HPQVRKIGVF SCGPPGMTKN VEKACQLINR QDRTHFSHHY ENF

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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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Thyroid.
[2]	"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] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF547266 mRNA. Translation: AAN39338.1.
RefSeq	NP_999261.1. NM_214096.2.
UniGene	Ssc.35919.
3D structure databases
ProteinModelPortal	Q8HZK3.
ModBase	Search...
Protein-protein interaction databases
STRING	9823.ENSSSCP00000005035.
Protein family/group databases
PeroxiBase	3348. SscDuOx01.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	397177.
KEGG	ssc:397177.
Organism-specific databases
CTD	53905.
Phylogenomic databases
eggNOG	COG5126.
HOGENOM	HOG000231774.
HOVERGEN	HBG080428.
KO	K13411.
OrthoDB	EOG4VQ9ND.
Enzyme and pathway databases
UniPathway	UPA00194.
Family and domain databases
Gene3D	1.10.238.10. 1 hit. 1.10.640.10. 1 hit.
InterPro	IPR011992. EF-hand-like_dom. IPR018247. EF_Hand_1_Ca_BS. 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. PF13499. EF_hand_5. 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. 2 hits. PS50222. EF_HAND_2. 3 hits. PS51384. FAD_FR. 1 hit. PS50292. PEROXIDASE_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DUOX1_PIG

Accession

Primary (citable) accession number: Q8HZK3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2006
Last sequence update:	March 1, 2003
Last modified:	May 1, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

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

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents