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UniProtKB/Swiss-Prot entry Q9ES45

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

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Entry information
Entry name DUOX2_RAT
Primary accession number Q9ES45
Secondary accession number Q811Y4
Integrated into Swiss-Prot on February 21, 2006
Sequence was last modified on March 1, 2001 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 45)
Name and origin of the protein
Protein name Dual oxidase 2 [Precursor]
Synonyms EC 1.6.3.1
EC 1.11.1.-
NADH/NADPH thyroid oxidase THOX2
Large NOX 2
Long NOX 2
Thyroid oxidase 2
Gene name
Name: Duox2
Synonyms: Lnox2, Thox2
From
Rattus norvegicus (Rat) [TaxID: 10116] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Rattus.
Protein existence 2: Evidence at transcript level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND INDUCTION.
TISSUE=Thyroid;
DOI=10.1006/bbrc.2000.3671; PubMed=11032719 [NCBI, ExPASy, EBI, Israel, Japan]
Dupuy C., Pomerance M., Ohayon R., Noel-Hudson M.-S., Deme D., Chaaraoui M., Francon J., Virion A.;
"Thyroid oxidase (THOX2) gene expression in the rat thyroid cell line FRTL-5.";
Biochem. Biophys. Res. Commun. 277:287-292(2000).
[2]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND INDUCTION.
STRAIN=Fischer;
DOI=10.1210/en.2002-220824; PubMed=12538618 [NCBI, ExPASy, EBI, Israel, Japan]
Morand S., Dos Santos O.F., Ohayon R., Kaniewski J., Noel-Hudson M.-S., Virion A., Dupuy C.;
"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.";
Endocrinology 144:567-574(2003).
[3]
 TISSUE SPECIFICITY.
DOI=10.1096/fj.02-1104fje; PubMed=12824283 [NCBI, ExPASy, EBI, Israel, Japan]
Geiszt M., Witta J., Baffi J., Lekstrom K., Leto T.L.;
"Dual oxidases represent novel hydrogen peroxide sources supporting mucosal surface host defense.";
FASEB J. 17:1502-1504(2003).
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
AF237962; AAG21895.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF547268; AAN39340.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_077055.1; -.
UniGene Rn.55542
3D structure databases
ModBase Q9ES45.
Protein family/group databases
PeroxiBase 3971; RnoDuOx02-b.
3972; RnoDuOx02-a.
Organism-specific databases
RGD 628761; Duox2.
Gene expression databases
ArrayExpress Q9ES45; -.
GermOnline ENSRNOG00000017395; Rattus norvegicus.
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).
ProtoNet Q9ES45.
Genome annotation databases
Ensembl ENSRNOG00000017395; Rattus norvegicus. [Contig view]
GeneID 79107; -.
KEGG rno:79107; -.
Phylogenomic databases
HOVERGEN Q9ES45; -.
Other
NextBio 614498; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; 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     25  25     Potential. 
CHAIN   26   1517  1492     Dual oxidase 2. PRO_0000223351
TOPO_DOM   26    599  574     Extracellular (Potential). 
TRANSMEM   600    620  21     Potential. 
TOPO_DOM   621   1010  390     Cytoplasmic (Potential). 
TRANSMEM   1011   1031  21     Potential. 
TOPO_DOM   1032   1046  15     Extracellular (Potential). 
TRANSMEM   1047   1067  21     Potential. 
TOPO_DOM   1068   1100  33     Cytoplasmic (Potential). 
TRANSMEM   1101   1121  21     Potential. 
TOPO_DOM   1122   1154  33     Extracellular (Potential). 
TRANSMEM   1155   1175  21     Potential. 
TOPO_DOM   1176   1185  10     Cytoplasmic (Potential). 
TRANSMEM   1186   1206  21     Potential. 
TOPO_DOM   1207   1207  1     Extracellular (Potential). 
TRANSMEM   1208   1228  21     Potential. 
TOPO_DOM   1229   1517  289     Cytoplasmic (Potential). 
DOMAIN   819    854  36     EF-hand 1. 
DOMAIN   855    890  36     EF-hand 2. 
DOMAIN   899    934  36     EF-hand 3. 
DOMAIN   1053   1235  183     Ferric oxidoreductase. 
DOMAIN   1236   1342  107     FAD-binding FR-type. 
CA_BIND   832    843  12     1 (Potential). 
CA_BIND   868    879  12     2 (Potential). 
REGION   30    596  567     Peroxidase-like; mediates peroxidase activity (By similarity). 
REGION   960   1214  255     Interaction with TXNDC11 (By similarity). 
CARBOHYD   100    100        N-linked (GlcNAc...) (Potential). 
CARBOHYD   348    348        N-linked (GlcNAc...) (Potential). 
CARBOHYD   455    455        N-linked (GlcNAc...) (Potential). 
CARBOHYD   537    537        N-linked (GlcNAc...) (Potential). 
VAR_SEQ   1   1061        Missing (in isoform 2). VSP_017264
CONFLICT   1243   1243        V -> A (in Ref. 2; AAN39340). 
CONFLICT   1246   1246        V -> A (in Ref. 2; AAN39340). 
CONFLICT   1409   1409        G -> D (in Ref. 2; AAN39340). 
Sequence information
Length: 1517 AA [This is the length of the unprocessed precursor] Molecular weight: 171558 Da [This is the MW of the unprocessed precursor] CRC64: 07FBA427DEA299D1 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MLPTSLKTLV LLGALLTGPL GPAGGQDAPS LPREVQRYDG WFNNLKYHQR GAAGSQLRRL 

        70         80         90        100        110        120 
VPANYADGVY QALQEPLLPN ARLLSDAVSK GKAGLPSAHN RTVLGLFFGY HVLSDLVSVE 

       130        140        150        160        170        180 
TPGCPAEFLN IYIPRGDPVF DPDKRGNVVL PFQRSRWDRS TGQSPSNPRD LTNQVTGWLD 

       190        200        210        220        230        240 
GSAIYGSSHS WSDTLRSFSG GQLASGPDPA FPRNSQNSLL MWMAPDPATG QGGPQGLYAF 

       250        260        270        280        290        300 
GAQRGNREPF LQALGLLWFR YHNLCAKRLA QEHPHWGDEE LFQHARKRVI ATYQNIALYQ 

       310        320        330        340        350        360 
WLPSFLQKTP PEYSGYRPFM DPSISPEFVA ASEQFLSTMV PPGVYMRNSS CHFREFPKEG 

       370        380        390        400        410        420 
SSSSPALRVC NNYWIRENPS LKTAQDVDQL LLGMASQISE LEDRIVIEDL RDYWPGPDRY 

       430        440        450        460        470        480 
SRTDYVASSI QSGRDMGLPS YSQALQALGL EPPKNWSALN PKVDPQVLEA TAALYNQDLS 

       490        500        510        520        530        540 
RLELFLGGLL ESHGDPGPLF SNIILDQFVR LRDGDRYWFE NTRNGLFSKE EIAEIRNTTL 

       550        560        570        580        590        600 
RDVLVAVSNV DPSALQPNVF FWQEGAPCPQ PQQLTTEGLP QCVPVTVIDY FEGSGAGYGV 

       610        620        630        640        650        660 
TLLAVCCFPV VSLIIAWVVA RFRNRERKML LKKGKESLKK QTASDGVPAM EWPGPKESSY 

       670        680        690        700        710        720 
PVTVQLLPDR SLKVLDKRLT VLRTIQLQPT QQVNLILSSS HGRRTLLLKI PKEYDLVLMF 

       730        740        750        760        770        780 
NSEEDRDAFV QLLQDLCVCS TPGLRIAEMD EKELLRKAVT KQQRAGILEI FFRQLFAQVL 

       790        800        810        820        830        840 
DINQADAGTL PLDSSQQVRE ALTCELSRAE FADSLGLKPQ DMFVESMFSL ADKDGNGYIS 

       850        860        870        880        890        900 
FREFLDILVV FMKGSPQDKS RLMFTMYDLD GNGFLSKEEF FTMMRSFIEI SNNCLSKDQL 

       910        920        930        940        950        960 
AEVVESMFRE SGFQDKEELT WEDFHFMLRD HDSDLRFTQL CVKGGAGGTG DIFKQSNACR 

       970        980        990       1000       1010       1020 
VSFLTRTPGN RVMAPSPRLY TEALQEKMQR GFLAQKLKQF KRFVENYRRH IVCVTIFSAI 

      1030       1040       1050       1060       1070       1080 
CAGLFADRAY YYGFASPPTD IEETTYVGII LSRGTAASIS FMFSYILLTM CRNLITFLRE 

      1090       1100       1110       1120       1130       1140 
TFLNRYIPFD AAVDFHRWIA MAAVVLAVVH SLGHAVNVYI FSVSPLSLMT CVFPSVFVND 

      1150       1160       1170       1180       1190       1200 
GSKLPPKYYW WFFETVPGMT GVLLLLVLAI MYVFASHHFR RHSFRGFWLT HHLYVVLYAL 

      1210       1220       1230       1240       1250       1260 
IIIHGSYALI QLPSFHIYFL VPAIIYVGDK LVSLSRKKVE ISVVKVELLP SGVTYLQFQR 

      1270       1280       1290       1300       1310       1320 
PKTFEYKSGQ WVRIACLSLG TNEYHPFTLT SAPHEDTLSL HIRAVGPWTT RLREIYSPPV 

      1330       1340       1350       1360       1370       1380 
GGTSARYPKL YLDGPFGEGH QEWHKFEVSV LVGGGIGVTP FASILKDLVF KSSMGTQMLC 

      1390       1400       1410       1420       1430       1440 
KKIYFIWVTR TQRQFEWLAD IIREVEENGS RDLVSVHIYI TQLAEKFDLR TTMLYICERH 

      1450       1460       1470       1480       1490       1500 
FQKVLNRSLF TGLRSVTHFG RPPFELFLDS LQEVHPQVHK IGVFSCGPPG MTKNVEKACQ 

      1510 
LINRQDRAHF VHHYENF
Q9ES45 in FASTA format

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