Reviewed, UniProtKB/Swiss-Prot Q8HZK3 (DUOX1_PIG)

Names and origin

Protein names

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

Gene names

Name:

DUOX1

Organism

Sus scrofa (Pig)

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
Ligand	Calcium FAD NADP
Molecular function	Oxidoreductase Peroxidase
PTM	Glycoprotein
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 oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to cAMP Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	FAD 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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 21	21	Potential
	Chain	22 – 1553	1532	Dual oxidase 1		PRO_0000223345
Regions
	Topological domain	22 – 596	575	Extracellular Potential
	Transmembrane	597 – 617	21	Potential
	Topological domain	618 – 1046	429	Cytoplasmic Potential
	Transmembrane	1047 – 1067	21	Potential
	Topological domain	1068 – 1082	15	Extracellular Potential
	Transmembrane	1083 – 1103	21	Potential
	Topological domain	1104 – 1138	35	Cytoplasmic Potential
	Transmembrane	1139 – 1159	21	Potential
	Topological domain	1160 – 1190	31	Extracellular Potential
	Transmembrane	1191 – 1211	21	Potential
	Topological domain	1212 – 1228	17	Cytoplasmic Potential
	Transmembrane	1229 – 1249	21	Potential
	Topological domain	1250	1	Extracellular Potential
	Transmembrane	1251 – 1271	21	Potential
	Topological domain	1272 – 1553	282	Cytoplasmic Potential
	Domain	815 – 850	36	EF-hand 1
	Domain	851 – 886	36	EF-hand 2
	Domain	895 – 930	36	EF-hand 3
	Domain	1089 – 1271	183	Ferric oxidoreductase
	Domain	1272 – 1378	107	FAD-binding FR-type
	Calcium binding	828 – 839	12	1 Potential
	Calcium binding	864 – 875	12	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	94	1	N-linked (GlcNAc...) Potential
	Glycosylation	342	1	N-linked (GlcNAc...) Potential
	Glycosylation	354	1	N-linked (GlcNAc...) Potential
	Glycosylation	534	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q8HZK3-1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 9F9364322977B710	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

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]. 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: 15591162] [Abstract] Cited for: TISSUE SPECIFICITY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF547266 mRNA. Translation: AAN39338.1.
RefSeq	NP_999261.1.
UniGene	Ssc.54800
3D structure databases
ModBase	Search...
Protein family/group databases
PeroxiBase	3348. SscDuOx01.
Genome annotation databases
Ensembl	ENSSSCT00000005161; ENSSSCP00000005035; ENSSSCG00000004675; Sus scrofa. [Genome view]
GeneID	397177.
KEGG	ssc:397177.
Organism-specific databases
CTD	397177.
Phylogenomic databases
HOVERGEN	Q8HZK3.
Enzyme and pathway databases
BRENDA	1.6.3.1. 249.
Family and domain databases
InterPro	IPR011992. EF-Hand_type. IPR018247. EF_Hand_1_Ca_BS. IPR018249. EF_HAND_2. IPR002048. EF_hand_Ca_bd. IPR018248. EF_Hand_dom. IPR013112. FAD_bd_8. IPR017927. Fd_Rdtase_FAD-bd. IPR013130. Fe3_reduct_TM_N. IPR013121. Fe_red_NAD_bd_6. IPR010255. Haem_peroxidase. IPR002007. Haem_peroxidase_animal. IPR019791. Haem_peroxidase_animal_sg. IPR017938. Riboflavin_synthase-like_b-brl. [Graphical view]
Gene3D	G3DSA:1.10.238.10. EF-Hand_type. 1 hit. G3DSA:1.10.640.10. Haem_peroxidase_animal. 1 hit.
Pfam	PF03098. 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]
PRINTS	PR00457. ANPEROXIDASE.
SMART	SM00054. EFh. 2 hits. [Graphical view]
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:	November 24, 2009
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)