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Protein

Dual oxidase 2

Gene

DUOX2

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

NAD(P)H + O2 = NAD(P)+ + H2O2.1 Publication

Enzyme regulationi

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

Pathwayi: thyroid hormone biosynthesis

This protein is involved in the pathway thyroid hormone biosynthesis, which is part of Hormone biosynthesis.
View all proteins of this organism that are known to be involved in the pathway thyroid hormone biosynthesis and in Hormone biosynthesis.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi832 – 8431PROSITE-ProRule annotationAdd BLAST12
Calcium bindingi868 – 8792PROSITE-ProRule annotationAdd BLAST12

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase, Peroxidase
Biological processHydrogen peroxide, Thyroid hormones biosynthesis
LigandCalcium, FAD, Flavoprotein, Metal-binding, NADP

Enzyme and pathway databases

BRENDAi1.6.3.1. 6170.
UniPathwayiUPA00194.

Protein family/group databases

PeroxiBasei3340. SscDuOx02.

Names & Taxonomyi

Protein namesi
Recommended name:
Dual oxidase 2 (EC:1.11.1.-, EC:1.6.3.1)
Alternative name(s):
NADH/NADPH thyroid oxidase p138-tox
Gene namesi
Name:DUOX2
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini26 – 601ExtracellularSequence analysisAdd BLAST576
Transmembranei602 – 622HelicalSequence analysisAdd BLAST21
Topological domaini623 – 1037CytoplasmicSequence analysisAdd BLAST415
Transmembranei1038 – 1058HelicalSequence analysisAdd BLAST21
Topological domaini1059 – 1074ExtracellularSequence analysisAdd BLAST16
Transmembranei1075 – 1097HelicalSequence analysisAdd BLAST23
Topological domaini1098 – 1145CytoplasmicSequence analysisAdd BLAST48
Transmembranei1146 – 1166HelicalSequence analysisAdd BLAST21
Topological domaini1167 – 1182ExtracellularSequence analysisAdd BLAST16
Transmembranei1183 – 1203HelicalSequence analysisAdd BLAST21
Topological domaini1204 – 1220CytoplasmicSequence analysisAdd BLAST17
Transmembranei1221 – 1241HelicalSequence analysisAdd BLAST21
Topological domaini1242ExtracellularSequence analysis1
Transmembranei1243 – 1263HelicalSequence analysisAdd BLAST21
Topological domaini1264 – 1545CytoplasmicSequence analysisAdd BLAST282

GO - Cellular componenti

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25Sequence analysisAdd BLAST25
ChainiPRO_000022335026 – 1545Dual oxidase 2Add BLAST1520

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi100N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi312N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi348N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi358N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi455N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi549N-linked (GlcNAc...) asparagineSequence analysis1

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ8HZK2.
PRIDEiQ8HZK2.

Expressioni

Tissue specificityi

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

Inductioni

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

Interactioni

Subunit structurei

Interacts with TXNDC11, TPO and CYBA.By similarity

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000005038.

Structurei

3D structure databases

ProteinModelPortaliQ8HZK2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini819 – 854EF-hand 1PROSITE-ProRule annotationAdd BLAST36
Domaini855 – 890EF-hand 2PROSITE-ProRule annotationAdd BLAST36
Domaini899 – 934EF-hand 3PROSITE-ProRule annotationAdd BLAST36
Domaini1081 – 1263Ferric oxidoreductaseAdd BLAST183
Domaini1264 – 1370FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST107

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni30 – 596Peroxidase-like; mediates peroxidase activityBy similarityAdd BLAST567
Regioni960 – 1242Interaction with TXNDC11By similarityAdd BLAST283

Sequence similaritiesi

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

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0039. Eukaryota.
ENOG410XNZY. LUCA.
HOGENOMiHOG000231774.
HOVERGENiHBG080428.
InParanoidiQ8HZK2.
KOiK13411.

Family and domain databases

CDDicd09820. dual_peroxidase_like. 1 hit.
cd00051. EFh. 2 hits.
Gene3Di1.10.640.10. 1 hit.
InterProiView protein in InterPro
IPR034818. DUOX2.
IPR034821. DUOX_peroxidase.
IPR011992. EF-hand-dom_pair.
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.
IPR019791. Haem_peroxidase_animal.
IPR017938. Riboflavin_synthase-like_b-brl.
PANTHERiPTHR11972:SF121. PTHR11972:SF121. 1 hit.
PfamiView protein in Pfam
PF03098. An_peroxidase. 1 hit.
PF00036. EF-hand_1. 1 hit.
PF13202. EF-hand_5. 1 hit.
PF08022. FAD_binding_8. 1 hit.
PF01794. Ferric_reduct. 1 hit.
PF08030. NAD_binding_6. 1 hit.
PRINTSiPR00457. ANPEROXIDASE.
SMARTiView protein in SMART
SM00054. EFh. 2 hits.
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF48113. SSF48113. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiView protein in PROSITE
PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
PS51384. FAD_FR. 1 hit.
PS50292. PEROXIDASE_3. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8HZK2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLCIRPEALV LLGALLTVPL DPVGGQDALS LTWEVQRYDG WFNNLRQHEH
60 70 80 90 100
GAAGSPLRRL VPANYADGVY QALGEPLLPN PRQLSHTTMR GPAGLRSIRN
110 120 130 140 150
RTVLGVFFGY HVLSDLVSIE KPGCPAEFLN IHIPPGDPVF DPHKSGDVVL
160 170 180 190 200
PFQRSRWDPN TGQSPSNPRD LTNEVTGWLD GSAIYGSSHS WSDELRSFSG
210 220 230 240 250
GQLASGPDPA FPRQAQDPLF MWTPPDPATG QRGPQGLYAF GAEQGNREPF
260 270 280 290 300
LQALGLLWFR YHNLCAQKLA REHPLWGDEE LFQHARKRVI ATYQSITMYE
310 320 330 340 350
WLPSFLQQTP PNYTEYRPFL DPSISPEFLA ASEQFFSTMV PPGVYMRNAS
360 370 380 390 400
CHFQMVLNES YGSFPALRVC NSYWIRENPN LNSAEAVNQL LLGMASQISE
410 420 430 440 450
LEDWIVVEDL RDYWPGPGKF SRTDYVASSI QRGRDMGLPS YTQALQALGL
460 470 480 490 500
NTPKNWSDFN PNVDPQVLEA TAALYNQDLS RLELFSGGLL ESYGDPGPLF
510 520 530 540 550
STIVLDQFVR LRDGDRYWFE NTKNGLFSKE EIAEIRSTTL RDVLVAVTNV
560 570 580 590 600
SSSALQPNVF IWNEDSPCPQ PQQLTTEDLP HCVPLTVIQY FEGSGPGFGI
610 620 630 640 650
TIVALCCLPL MSLLISGVVA YFRSRERKKL QKRGKESVKK EADKDGVSAM
660 670 680 690 700
EWPGPKERSY PVSIQLLPDR HLQVLDRHLS VLRTIQLRPR HRVNLILSNN
710 720 730 740 750
LGRRTLLLKI PKEYDLVLLF NSEDERGAFV QHLQGFCASC ALGLDIDEMG
760 770 780 790 800
ESELFRKAVT KQQRGRILEI FFRHLFAQVL DIDQADAGAL PLDSSQKVRE
810 820 830 840 850
ALTCELSRAE FAESLGLKPQ DMFVESMFSL ADKDGNGYLS FREFLDVLVV
860 870 880 890 900
FMKGSPEDKS RLMFTMYDLD GNGFLSKDEF FTMIRSFIEI SNNCLSKAQL
910 920 930 940 950
TEVVESMFRE AGFQDKQELT WEDFHFMLRD HDSELRHTQL CVKGGGGGVG
960 970 980 990 1000
VIFKPDISSR VSFIIRTPEE RSSPQGVRLP ASEASELGGP VLKKRFGKKA
1010 1020 1030 1040 1050
VVPPPRLYTE ALQEKKQRGF LAQKLQQYKR FVENYRRHIV CVAIFSAICA
1060 1070 1080 1090 1100
GLFVERAYYY AFVSPPSGIA ETTFVGIILS RGTAASVSFM FSYILLTMCR
1110 1120 1130 1140 1150
NLITFLRETF LNHYVPFDAA VDFHRWIAMA ALVLAILHSV GHVVNVYIFS
1160 1170 1180 1190 1200
VSPLSLLACV FPSVFVNDGS KLPQKFYWWF FQTIPGMTGV LLLVVLAIMY
1210 1220 1230 1240 1250
VFASPYFRRR SFRGFWLTHH FYILLYVLLI IHGSFALIQL PRFHIFFLVP
1260 1270 1280 1290 1300
ALIYVGDKLV SLSRKKVEIS VVKAELLPSG VTHLQFQRPQ GFEYKSGQWV
1310 1320 1330 1340 1350
RIACLGLGTN EYHPFTLTSA PHEDTLSLHI RAVGPWTTRL REIYSHPMGD
1360 1370 1380 1390 1400
GYARYPKLYL DGPFGEGHQE WHKFEVSVLV GGGIGVTPFA SILKDLVFKS
1410 1420 1430 1440 1450
SLGSQMLCKK IYFIWVTRTQ RQFEWLADII REVEENDHRD LVSVHIYITQ
1460 1470 1480 1490 1500
LAEKFDLRTT MLYICERHFQ KVLNRSLFTG LRSITHFGRP PFEPFFNSLQ
1510 1520 1530 1540
EVHPQVRKIG VFSCGPPGMT KNVEKTCQLI NRQDQTHFVH HYENF
Length:1,545
Mass (Da):175,284
Last modified:October 11, 2004 - v2
Checksum:i29A6B1A0C69552DD
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1531N → S in AAF20056 (PubMed:10601291).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF547267 mRNA. Translation: AAN39339.2.
AF181973 mRNA. Translation: AAF20056.1.
RefSeqiNP_999164.2. NM_213999.2.
UniGeneiSsc.33.

Genome annotation databases

GeneIDi397060.
KEGGissc:397060.

Similar proteinsi

Entry informationi

Entry nameiDUOX2_PIG
AccessioniPrimary (citable) accession number: Q8HZK2
Secondary accession number(s): Q9TT98
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: October 11, 2004
Last modified: July 5, 2017
This is version 100 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families