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UniProtKB/Swiss-Prot entry Q8CIY2

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

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Entry information
Entry name DUOX1_RAT
Primary accession number Q8CIY2
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 38)
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
Rattus norvegicus (Rat) [TaxID: 10116] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Rattus.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Fischer 344;
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).
[2]
 TISSUE SPECIFICITY.
DOI=10.1074/jbc.M000916200; PubMed=10806195 [NCBI, ExPASy, EBI, Israel, Japan]
De Deken X., Wang D., Many M.-C., Costagliola S., Libert F., Vassart G., Dumont J.E., Miot F.;
"Cloning of two human thyroid cDNAs encoding new members of the NADPH oxidase family.";
J. Biol. Chem. 275:23227-23233(2000).
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
AF542180; AAN33120.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_714961.1; -.
UniGene Rn.162682
3D structure databases
HSSP P02631; 1RRO. [HSSP ENTRY / PDB]
ModBase Q8CIY2.
Protein family/group databases
PeroxiBase 3970; RnoDuOx01.
Organism-specific databases
RGD 628760; Duox1.
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
Ensembl ENSRNOG00000033348; Rattus norvegicus. [Contig view]
GeneID 266807; -.
KEGG rno:266807; -.
Phylogenomic databases
HOVERGEN Q8CIY2; -.
Other
NextBio 624725; -.
ProtoNet Q8CIY2.
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   1551  1530     Dual oxidase 1. PRO_0000223346
TOPO_DOM   22    596  575     Extracellular (Potential). 
TRANSMEM   597    617  21     Potential. 
TOPO_DOM   618   1044  427     Cytoplasmic (Potential). 
TRANSMEM   1045   1065  21     Potential. 
TOPO_DOM   1066   1080  15     Extracellular (Potential). 
TRANSMEM   1081   1101  21     Potential. 
TOPO_DOM   1102   1136  35     Cytoplasmic (Potential). 
TRANSMEM   1137   1157  21     Potential. 
TOPO_DOM   1158   1188  31     Extracellular (Potential). 
TRANSMEM   1189   1209  21     Potential. 
TOPO_DOM   1210   1226  17     Cytoplasmic (Potential). 
TRANSMEM   1227   1247  21     Potential. 
TOPO_DOM   1248   1248  1     Extracellular (Potential). 
TRANSMEM   1249   1269  21     Potential. 
TOPO_DOM   1270   1551  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   1087   1269  183     Ferric oxidoreductase. 
DOMAIN   1270   1376  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   1248  293     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   461    461        N-linked (GlcNAc...) (Potential). 
CARBOHYD   534    534        N-linked (GlcNAc...) (Potential). 
Sequence information
Length: 1551 AA [This is the length of the unprocessed precursor] Molecular weight: 177197 Da [This is the MW of the unprocessed precursor] CRC64: 52B07F83EF4E1FE2 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MAVYSAVAWI LLFGVLASLG AQNPVSWEVQ RFDGWYNNLM EHRWGSKGSR LQRLVPASYA 

        70         80         90        100        110        120 
DGVYQPLREP YLPNPRHLSN RVMRGPAGQP SLRNRTVLGV FFGYHVLSDL VSVETPGCPA 

       130        140        150        160        170        180 
EFLNIYIPRG DPVFDPDKRG NVVLPFQRSR WDRSTGQSPS NPRDLTNQVT GWLDGSAIYG 

       190        200        210        220        230        240 
SSHSWSDTLR SFSGGQLASG PDPAFPRNSQ NSLLMWMAPD PATGQGGPQG LYAFGAQRGN 

       250        260        270        280        290        300 
REPFLQALGL LWFRYHNLCA KRLAQEHPHW GDEELFQHAR KRVIATYQNI AMYEWLPSFL 

       310        320        330        340        350        360 
KQTPPEYPGY HPFLDPSISP EFVVASEQFL STMVPPGVYM RNASCHFQGI ANRNSSVSGA 

       370        380        390        400        410        420 
LRVCNSYWSR ENPKLQRAED VDALLLGMAS QIAEREDHLV VEDVQDFWPG PLKFSRTDYL 

       430        440        450        460        470        480 
ASCLQRGRDL GLPSYTKARE ALGLPPVSHW QDINPALSRS NGTVLEATAA LYNQDLSRLE 

       490        500        510        520        530        540 
LLAGGLLESH GDPGPLFSAI VLDQFVRLRD GDRYWFENNR NGLFSKEEIA EIRNTSLRDI 

       550        560        570        580        590        600 
LVAVTNVDPS ALQPSVFFWL AGDPCPQPSQ LSTQGLPACA PLFVRDYFKG SGFGFGLTIG 

       610        620        630        640        650        660 
TLCCFPLVSL LSAWIVARLR MRNFKRLQRQ DRQSIMCEKL VGGVEALEWQ GRKEPCRPVL 

       670        680        690        700        710        720 
VHLQPGQIRV VDGRLTVLRT IQLRPPQQVN LILSSNRGRR TLLLKIPKEY DLVLLFNMEE 

       730        740        750        760        770        780 
ERQALVENIR AALKENGLSF QEWELREQEL MRAAVTRQQR GHLLETFFRH LFSQVLDINQ 

       790        800        810        820        830        840 
ADAGTLPLDS STKVREALTC ELSRAEFADS LGLKPQDMFV ESMFSLADKD GNGYLSFREF 

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

       910        920        930        940        950        960 
ESMFRESGFQ DKEELTWEDF HFMLRDHDSD LRFTQLCVKG VEVPEVIKNL CRRASYISQE 

       970        980        990       1000       1010       1020 
KICPSPRMSA HCARNNTKTA SSPQRLQCPV DTDPPQEIRR RFGKKVTSFQ PLLFTEAHRE 

      1030       1040       1050       1060       1070       1080 
KFQRSRRHQT VQQFKRFIEN YRRHIGCVAV FYTITGALFL ERAYYYAFAA HHSGITDTTR 

      1090       1100       1110       1120       1130       1140 
VGIILSRGTA ASISFMFSYI LLTMCRNLIT FLRETFLNRY IPFDAAVDFH RFIASTAIIL 

      1150       1160       1170       1180       1190       1200 
TVLHSAGHVV NVYLFSISPL SVLSCLFPDL FHDDGSEFPQ KYYWWFFQTV PGLTGVLLLL 

      1210       1220       1230       1240       1250       1260 
ALAIMYVFAS HHFRRRSFRG FWLTHHLYIF LYILLIIHGS FALIQMPRFH IFFLVPAIIY 

      1270       1280       1290       1300       1310       1320 
VGDKLVSLSR KKVEISVVKA ELLPSGVTHL RFQRPQGFEY KSGQWVRIAC LALGTTEYHP 

      1330       1340       1350       1360       1370       1380 
FTLTSAPHED TLSLHIRAAG PWTTRLREIY SPPTGDTCAR YPKLYLDGPF GEGHQEWHKF 

      1390       1400       1410       1420       1430       1440 
EVSVLVGAGI GVTPFASILK DLVFKSSVSC QVFCKKIYFI WVTRTQRQFE WLADIIREVE 

      1450       1460       1470       1480       1490       1500 
ENDSRDLVSV HIYITQLAEK FDLRTTMLYI CERHFQKVLN RSLFTGLRSV THFGRPPFEP 

      1510       1520       1530       1540       1550 
FFNSLQEVHP QVRKIGVFSC GPPGMTKNVE KACQLINKQD RTHFSHHYEN F
Q8CIY2 in FASTA format

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