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UniProtKB/Swiss-Prot entry Q8HZK3

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DUOX1_PIG
Primary accession number Q8HZK3
Secondary accession numbers None
Integrated into Swiss-Prot on February 21, 2006
Sequence was last modified on March 1, 2003 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 37)
Name and origin of the protein
Protein name Dual oxidase 1 [Precursor]
Synonyms EC 1.6.3.1
EC 1.11.1.-
Gene name
Name: DUOX1
From
Sus scrofa (Pig) [TaxID: 9823] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; Sus.
Protein existence 2: Evidence at transcript level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Thyroid;
DOI=10.1210/en.2002-220981; PubMed=12639906 [NCBI, ExPASy, EBI, Israel, Japan]
Morand S., Chaaraoui M., Kaniewski J., Deme D., Ohayon R., Noel-Hudson M.-S., Virion A., Dupuy C.;
"Effect of iodide on nicotinamide adenine dinucleotide phosphate oxidase activity and Duox2 protein expression in isolated porcine thyroid follicles.";
Endocrinology 144:1241-1248(2003).
[2]
 TISSUE SPECIFICITY.
DOI=10.1152/ajpgi.00198.2004; PubMed=15591162 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Dual oxidase2 is expressed all along the digestive tract.";
Am. J. Physiol. 288:G933-G942(2005).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF547266; AAN39338.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_999261.1; -.
UniGene Ssc.54800
3D structure databases
HSSP P62157; 1A29. [HSSP ENTRY / PDB]
ModBase Q8HZK3.
Protein family/group databases
PeroxiBase 3348; SscDuOx01.
Ontologies
GO
GO:0016324; Cellular component: apical plasma membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from InterPro).
GO:0005509; Molecular function: calcium ion binding (inferred from electronic annotation from InterPro).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660; Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0020037; Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0016174; Molecular function: NAD(P)H oxidase activity (inferred from electronic annotation from EC).
GO:0004601; Molecular function: peroxidase activity (inferred from electronic annotation from InterPro).
GO:0042335; Biological process: cuticle development (inferred from sequence or structural similarity from UniProtKB).
GO:0019221; Biological process: cytokine-mediated signaling pathway (inferred from sequence or structural similarity from UniProtKB).
GO:0042446; Biological process: hormone biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0042744; Biological process: hydrogen peroxide catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0051591; Biological process: response to cAMP (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR011992; EF-Hand_type.
IPR002048; EF_hand_Ca_bd.
IPR013112; FAD_bd_8.
IPR013130; Fe3_reduct_TM_N.
IPR013121; Fe_red_NAD_bd_6.
IPR002007; Haem_peroxidase_animal.
Graphical view of domain structure.
Gene3D G3DSA:1.10.238.10; EF-Hand_type; 1.
G3DSA:1.10.640.10; Haem_peroxidase_animal; 1.
Pfam PF03098; An_peroxidase; 1.
PF00036; efhand; 2.
PF08022; FAD_binding_8; 1.
PF01794; Ferric_reduct; 1.
PF08030; NAD_binding_6; 1.
Pfam graphical view of domain structure.
PRINTS PR00457; ANPEROXIDASE.
ProDom PD000012; EF-hand; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00054; EFh; 2.
SMART graphical view of domain structure.
PROSITE PS00018; EF_HAND_1; 2.
PS50222; EF_HAND_2; 3.
PS51384; FAD_FR; 1.
PS50292; PEROXIDASE_3; 1.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
GeneID 397177; -.
KEGG ssc:397177; -.
Phylogenomic databases
HOVERGEN Q8HZK3; -.
Other
ProtoNet Q8HZK3.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Calcium; Cell membrane; FAD; Glycoprotein; Hydrogen peroxide; Membrane; NADP; Oxidoreductase; Peroxidase; Repeat; Signal; Thyroid hormones biosynthesis; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
SIGNAL   1     21  21     Potential. 
CHAIN   22   1553  1532     Dual oxidase 1. PRO_0000223345
TOPO_DOM   22    596  575     Extracellular (Potential). 
TRANSMEM   597    617  21     Potential. 
TOPO_DOM   618   1046  429     Cytoplasmic (Potential). 
TRANSMEM   1047   1067  21     Potential. 
TOPO_DOM   1068   1082  15     Extracellular (Potential). 
TRANSMEM   1083   1103  21     Potential. 
TOPO_DOM   1104   1138  35     Cytoplasmic (Potential). 
TRANSMEM   1139   1159  21     Potential. 
TOPO_DOM   1160   1190  31     Extracellular (Potential). 
TRANSMEM   1191   1211  21     Potential. 
TOPO_DOM   1212   1228  17     Cytoplasmic (Potential). 
TRANSMEM   1229   1249  21     Potential. 
TOPO_DOM   1250   1250  1     Extracellular (Potential). 
TRANSMEM   1251   1271  21     Potential. 
TOPO_DOM   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. 
CA_BIND   828    839  12     1 (Potential). 
CA_BIND   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). 
CARBOHYD   94     94        N-linked (GlcNAc...) (Potential). 
CARBOHYD   342    342        N-linked (GlcNAc...) (Potential). 
CARBOHYD   354    354        N-linked (GlcNAc...) (Potential). 
CARBOHYD   534    534        N-linked (GlcNAc...) (Potential). 
Sequence information
Length: 1553 AA [This is the length of the unprocessed precursor] Molecular weight: 177861 Da [This is the MW of the unprocessed precursor] CRC64: 9F9364322977B710 [This is a checksum on the sequence] 
        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
Q8HZK3 in FASTA format

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