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Database: UniProt
Entry: U3BY65_CALJA
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ID   U3BY65_CALJA            Unreviewed;      1551 AA.
AC   U3BY65;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   RecName: Full=NAD(P)H oxidase (H2O2-forming) {ECO:0000256|ARBA:ARBA00012698};
DE            EC=1.6.3.1 {ECO:0000256|ARBA:ARBA00012698};
GN   Name=DUOX1 {ECO:0000313|EMBL:JAB10839.1};
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483 {ECO:0000313|EMBL:JAB10839.1};
RN   [1] {ECO:0000313|EMBL:JAB10839.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Bladder {ECO:0000313|EMBL:JAB10839.1};
RX   PubMed=25243066; DOI=10.1186/2047-217X-3-14;
RA   Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C.,
RA   Moriyama E.N., French J.A., Norgren R.B.Jr.;
RT   "De novo assembly of the common marmoset transcriptome from NextGen mRNA
RT   sequences.";
RL   Gigascience 3:14-14(2014).
CC   -!- FUNCTION: Generates hydrogen peroxide which is required for the
CC       activity of thyroid peroxidase/TPO and lactoperoxidase/LPO. Plays a
CC       role in thyroid hormones synthesis and lactoperoxidase-mediated
CC       antimicrobial defense at the surface of mucosa. May have its own
CC       peroxidase activity through its N-terminal peroxidase-like domain.
CC       {ECO:0000256|ARBA:ARBA00003796}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + NADH + O2 = H2O2 + NAD(+); Xref=Rhea:RHEA:11264,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.6.3.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000518};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + NADPH + O2 = H2O2 + NADP(+); Xref=Rhea:RHEA:11260,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.6.3.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000547};
CC   -!- PATHWAY: Hormone biosynthesis; thyroid hormone biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005197}.
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000256|ARBA:ARBA00004424}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004424}. Cell membrane
CC       {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the peroxidase
CC       family. {ECO:0000256|ARBA:ARBA00005644}.
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DR   EMBL; GAMT01001022; JAB10839.1; -; mRNA.
DR   UniPathway; UPA00194; -.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0016174; F:NAD(P)H oxidase H2O2-forming activity; IEA:UniProtKB-EC.
DR   GO; GO:0004601; F:peroxidase activity; IEA:InterPro.
DR   GO; GO:0042446; P:hormone biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   GO; GO:0006590; P:thyroid hormone generation; IEA:UniProtKB-UniPathway.
DR   CDD; cd09820; dual_peroxidase_like; 1.
DR   CDD; cd00051; EFh; 2.
DR   CDD; cd06186; NOX_Duox_like_FAD_NADP; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR034821; DUOX_peroxidase.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR013112; FAD-bd_8.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR   InterPro; IPR013121; Fe_red_NAD-bd_6.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR019791; Haem_peroxidase_animal.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR11972:SF75; DUAL OXIDASE 1; 1.
DR   PANTHER; PTHR11972; NADPH OXIDASE; 1.
DR   Pfam; PF03098; An_peroxidase; 1.
DR   Pfam; PF00036; EF-hand_1; 1.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   Pfam; PF08022; FAD_binding_8; 1.
DR   Pfam; PF01794; Ferric_reduct; 1.
DR   Pfam; PF08030; NAD_binding_6; 1.
DR   PRINTS; PR00457; ANPEROXIDASE.
DR   SFLD; SFLDS00052; Ferric_Reductase_Domain; 1.
DR   SFLD; SFLDG01168; Ferric_reductase_subgroup_(FRE; 1.
DR   SFLD; SFLDG01169; NADPH_oxidase_subgroup_(NOX); 1.
DR   SMART; SM00054; EFh; 2.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS50292; PEROXIDASE_3; 1.
PE   2: Evidence at transcript level;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00023324};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW   Thyroid hormones biosynthesis {ECO:0000256|ARBA:ARBA00022534};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..1551
FT                   /note="NAD(P)H oxidase (H2O2-forming)"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004639138"
FT   TRANSMEM        593..617
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1045..1068
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1088..1109
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1152..1171
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1183..1209
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1221..1243
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          815..850
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          851..886
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          1270..1376
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          147..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1551 AA;  176949 MW;  ABE5F3C29362439F CRC64;
     MGFCLALAWT LLVGPWTPVG AQNPISWEVQ RFDGWYNNLM EHRWGSKGSR LQRLVPASYA
     DGVYQPLGEP HLPNPRDLSN TISRGPAGLA SLRNRTVLGV FFGYHLLSDL LNVETPGCPA
     EFLNIRIPPG DPVFDPDQRG DVVLPFQRSR WDPETGRSPS NPRDLTNQVT GWLDGSAIYG
     SSHSWNDALR SFSGGQLASG PDPAFPRDSQ NPLLMWAAPD PATGQSGPRG LYAFGAERGN
     REPFLQALGL LWFRYHNLCA QRLARQHPDW GDEELFQHAR KRVIATYQNI AVYEWLPSFL
     QKTLPEYTGY RPFLDPSISS EFVAASEQFL STMVPPGVYM RNASCHFQGV INRNSSVSRA
     LRVCNSYWSR EHPSLQSAED VDALLLGMTS QIAEREDHVV VEDVRDFWPG PLKFSRTDHL
     ASCLQRGRDL GLPSYNKARA ALGLPPITRW QDINTALSWS DDTVLEATAS LYNQDLSWLE
     LLPGGLLESH GDPGPLFSTI VLDQFVRLRD GDRYWFENTR NGLFSKKEIE EIRNTTLRDV
     LAAVINVDPS ALQPNVFVWH KGDPCPQPRQ LSTEGLPACA PSIVRDYFEG SGFGFGVTIG
     TLCCFPLVSL LSAWIVARLR MRNFKRLQGQ DCQSIVSEKL VGGTEALEWQ GRKEPCRPVL
     VHLQPGQIRV VDGRLTVLRT IQLQPPQQIN LVLSSNRGRR TLLLKIPKEY DLVLLFNLEE
     ERQALVENLR AALKESGLSF QEWELREQEL MRAAVTREQR SHLLETFFRH LFSQVLDINQ
     ADAGTLPLDS SQKVREALTC ELSRAEFAES LGLKPQDMFV ESMFSLADKD GNGYLSFREF
     LDILVVFMKG SPEEKSRLMF RMYDFDGNGL ISKDEFIRML RSFIEISNNC LSKAQLAEVV
     ESMFQESGFQ DKEELTWEDF HFMLRDHDSE LRFTQLCVKG VDVPEVIKDL CRRASYISQE
     KICPSPRVSA RCSRSGVETE LTPQRLQCPM DTDPPQEIRR RFGKKVTSFQ PLLFTEAHRE
     KFQRSRLHQT VQQFKRFIEN YRRHIGCVAV FYTIAGGLFL ERAYYYAFAA HHMGITDTTR
     VGIILSRGTA ASISFMFSYI LLTMCRNLIT FLRETFLNRY VPFDAAVDFH RLIASTAIVL
     TVLHSVGHVV NVYLFSISPL SILSCLFPGL FHDDGSEFPQ KYYWWFFQTV PGLTGVVLLL
     VLAIMYVFAS HHFRRRSFRG FWLTHHLYIL LYVLLIIHGS FALIQLPRFH IFFLVPAIIY
     GGDKLVSLSR KKVEISVVKA ELLPSGVTYL RFQRPQGFEY KSGQWVRIAC LSLGTTEYHP
     FTLTSAPHED TLSLHIRAAG PWTTRLREIY SAPTGDRCAR YPKLYLDGPF GEGHQEWHKF
     EVSVLVGGGI GVTPFASILK DLVFKSSVSC QVFCKKIYFI WVTRTQRQFE WLADIIREVE
     ENDHQDLVSV HIYITQLAEK FDLRTTMLYI CERHFQKVLN RSLFTGLRSV THFGRPPFEP
     FFNSLQEVHP QVRKVGVFSC GPPGMTKNVE KACQLVNRQD RAHFIHHYEN F
//
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