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Database: UniProt
Entry: G3TTY1_LOXAF
LinkDB: G3TTY1_LOXAF
Original site: G3TTY1_LOXAF 
ID   G3TTY1_LOXAF            Unreviewed;      1548 AA.
AC   G3TTY1;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 72.
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|Ensembl:ENSLAFP00000019039.1};
OS   Loxodonta africana (African elephant).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX   NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000019039.1, ECO:0000313|Proteomes:UP000007646};
RN   [1] {ECO:0000313|Ensembl:ENSLAFP00000019039.1, ECO:0000313|Proteomes:UP000007646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000019039.1,
RC   ECO:0000313|Proteomes:UP000007646};
RA   Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Loxodonta africana (African elephant).";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLAFP00000019039.1}
RP   IDENTIFICATION.
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000019039.1};
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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   Ensembl; ENSLAFT00000033568.1; ENSLAFP00000019039.1; ENSLAFG00000017095.3.
DR   GeneTree; ENSGT00940000161792; -.
DR   UniPathway; UPA00194; -.
DR   Proteomes; UP000007646; Unassembled WGS sequence.
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; 1.
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; 2.
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; SFLDG01169; NADPH_oxidase_subgroup_(NOX); 2.
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   3: Inferred from homology;
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   Reference proteome {ECO:0000313|Proteomes:UP000007646};
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..1548
FT                   /note="NAD(P)H oxidase (H2O2-forming)"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003455496"
FT   TRANSMEM        593..617
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1045..1065
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1148..1169
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1181..1207
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          1267..1373
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          147..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          968..994
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        153..167
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1548 AA;  175167 MW;  9136CBE412732F93 CRC64;
     MSCQLALAWA LLVGPWASVV SQNSISWEVQ RFDGWYNNLV EHRWGSKGSR LQRLVPASYA
     DGVYQPLGEP HLPNPRAISN TAMRGPAGQA SLQNRTVLGV FFGYHVLSDL VSVERPGCPA
     EFLNIRIPRG DPVFDPDQRG DVVLPFQRSR WDPETGRSPS NPRDLTNQVT GWLDGSAIYG
     SSHSRSDALR SFSGGQLASG PDPAFPRDAQ DSRLMWVAPD PATGQRGPRG LYDFGAERGN
     REPFLQALGL LWFRYHNLWA QRLAREHPRW GDEELFQHAR KRVIATYQNI ALYEWLPSFL
     QNTPPEYAGY RPFLDPSISP EFLVASEQFF STMVPPGVYM RNASCHFQGV INRNSSVSRA
     LRVCNSYWSR EHPNLQSAED VAALLLGMAS QIAEREDHVV VEDLRDFWPG PLKSSRTDYL
     ASCLQRGRDL GLPSYTKARA ALGLPSITRW QDINPALSQS DNVVLEATAA LYSQDLSRLE
     LLPGGLLESH GDPGPLFSTI VLDQFVRLRD GDRYWFENTR NGLFSEEEIE EIRNTSLRDV
     LVAITDVNPS SLQPNVFVWH AGDPCPQPRQ LSTEGLPTCV PPVVRDYFEG SGFGFGVVIG
     TLCCFPLVSL LSAWIVAQLR RRSFKRLQGQ DRQSIMSEKL IGGVEVLEWQ GHKEPCRPVL
     LQLQPGQIRV VDGGLSVLRT VQLQPSQQVN LILSSNHGRR TLLLKIPKEY DLVLQFNLEE
     ERQALVESLR AALKEGGLSV QEWELREQEL MKAAVTREQR SHLLETFFRH LFSQVLDINQ
     ADAGTLPLDS SQKVREALTC ELSRAEFAES LGLKPQDMFV ESMFSLADKD GNGYLSFREF
     LDILVVFMKG SPEDKSRLMF TMYDLDGNGF LSKDEFFTMM RSFIEISNNC LSKAQLAEVV
     ESMFQESGFQ DKEELTWEDF HFMLRDHDSE LRLTQLCVKG VEVPEVIKDL CRRASYISQE
     QICPSPRVSA RCSRSDPEAG PTPQRLPCPV ETGPPQEIRR RFGKKVTSFQ PLLFTEAHRE
     KFQRSRRHQT VQQFKRFVEN YRRHIGCVAV FYAIAVGLFL ERAYLRKDSP GAWPEISDSH
     RGGAYSEKGV PWGILSPNSE GSSSSPQLCL AVVLHFGLNG LSPHTGLPQA DPRPAWSSLV
     LHSVGHVVNV YLFSISPLSV LACLFPGLFR DDGSEFPQKY YWWFFQTVPG LTGVLLLLVL
     AVMYVFASHH FRRRSFRGFW LTHHLYILLY VLVRTPGGWS GEQLERRSPG QAAPLALLTT
     SPCVGMARGV KWLLPSAHHP SSGVTHLRFQ RPQGFEYKSG QWVRIACLAL GTTEYHPFTL
     TSAPHEDTLS LHIRAAGPWT TRLREIYSPP TGNSSARYPK LYLDGPFGEG HQEWHKFEVS
     VLVGGGIGVT PFASILKDLV FKSSVSCQVF CKKIYFIWVT RTQRQFEWLA DIIREVEEND
     HQDLVSVHIY ITQLAEKFDL RTTMLYICER HFQKVLNRSL FTGLRSITHF GRPPFEPFFN
     SLQEVHPQVQ KIGVFSCGPP GMTKNVEKAC QLINKQDRTH FSHHYENF
//
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