ID L8Y416_TUPCH Unreviewed; 1365 AA.
AC L8Y416;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=NAD(P)H oxidase (H2O2-forming) {ECO:0000256|ARBA:ARBA00012698};
DE EC=1.6.3.1 {ECO:0000256|ARBA:ARBA00012698};
GN ORFNames=TREES_T100012673 {ECO:0000313|EMBL:ELV09794.1};
OS Tupaia chinensis (Chinese tree shrew).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Scandentia; Tupaiidae; Tupaia.
OX NCBI_TaxID=246437 {ECO:0000313|EMBL:ELV09794.1, ECO:0000313|Proteomes:UP000011518};
RN [1] {ECO:0000313|Proteomes:UP000011518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zhang G., Fan Y., Yao Y., Huang Z.;
RT "Genome of the Chinese tree shrew, a rising model animal genetically
RT related to primates.";
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000011518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23385571; DOI=10.1038/ncomms2416;
RA Fan Y., Huang Z.Y., Cao C.C., Chen C.S., Chen Y.X., Fan D.D., He J.,
RA Hou H.L., Hu L., Hu X.T., Jiang X.T., Lai R., Lang Y.S., Liang B.,
RA Liao S.G., Mu D., Ma Y.Y., Niu Y.Y., Sun X.Q., Xia J.Q., Xiao J.,
RA Xiong Z.Q., Xu L., Yang L., Zhang Y., Zhao W., Zhao X.D., Zheng Y.T.,
RA Zhou J.M., Zhu Y.B., Zhang G.J., Wang J., Yao Y.G.;
RT "Genome of the Chinese tree shrew.";
RL Nat. Commun. 4:1426-1426(2013).
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}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the peroxidase
CC family. {ECO:0000256|ARBA:ARBA00005644}.
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DR EMBL; KB369669; ELV09794.1; -; Genomic_DNA.
DR STRING; 246437.L8Y416; -.
DR eggNOG; KOG0039; Eukaryota.
DR InParanoid; L8Y416; -.
DR UniPathway; UPA00194; -.
DR Proteomes; UP000011518; 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; 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; 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; 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:SF67; DUAL OXIDASE 2; 1.
DR PANTHER; PTHR11972; NADPH OXIDASE; 1.
DR Pfam; PF03098; An_peroxidase; 2.
DR Pfam; PF00036; EF-hand_1; 1.
DR Pfam; PF13833; EF-hand_8; 1.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
DR PRINTS; PR00450; RECOVERIN.
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 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000011518};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Thyroid hormones biosynthesis {ECO:0000256|ARBA:ARBA00022534};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 448..472
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 883..902
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 946..967
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 974..993
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1005..1031
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1043..1065
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 669..704
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 705..740
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 1092..1198
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 1365 AA; 153662 MW; C24240B126CE3640 CRC64;
MPRAPAVLET VRMWVLGDVS NSFAPEVETA GAPPAAGYHV LSDLVSIETP GCPAEFLNIH
IPPGDPVFDP HQSGDVNIAL YEWLPSFLQV TPPEYAGYRH FLDPSISPEF VVASEQFFST
MVPPGVYMRS PFPPVPAESE QSSLYLQEMH IAKSLLAPRK SRDCPSVLAN SHHVPHPINP
ISPSLSSFTT SLIPHFRNVS CHFQKVLNRA SGSSPAMRVC NSYWIRENPN LNSAEAVNQL
LLGMASQISE LEDRIVVEDL RDYWPGPGKF SRTDYVASSI QRGRDMGLPS YTQALLALGL
EIPKNWSNLN PSVDPQVLQA TAALYNQDLS RLELLPGGLL ESHGDPGPLF STIVLEQFVR
LRDGDRYWFE NTRNGLFSPE EIAEIRNTTL RDVVAAVTNV DPSALQPNVF VWHEGAPCPQ
PRQLTTEGLP PCAPLTVLDY FEGSGPGFGL TIVALCCLPL VSLFISGVVA HFRTRERKKL
QKKDKESVKK KTAKDGVLAM EWPGPSERSY PITVQLLPDR RLQVLDRRLA VLRTVQLRPP
QQVNLLLSSD RGRRTLLLKI PKEYDLVLLF NSEEERAAFV QQLQDFCVHC TLDLHVAETG
EKELFKKAVT KQQRGRILEI FFRHLFAQVL DINQADAGSL PLDSSQKVRE ALTCELSRAE
FAESLGLKPQ DMFVESMFSL ADKDGNGYLS FREFLDILVV FMKGSPEDKS RLMFTMYDLD
ANGFLSKDEF FTMMRSFIEI SNNCLSKDQL AEVVESMFQE SGFQDKEELT WEDFHFMLRD
HDSELRRTQL CVKGGGVGDI FKQNISSRVS FITRTPGTCS YPQKTELPAS EAPELGGHGL
KKRFGKKMVV APSRLYTEAL QEKMQRGFLA QKLQQYKRFV ENYLRHILCV AVFSAICAGL
FAERAYYPQC MHRGAQGLVG LKTLVSYAIL VSPDPDYAFA SPPSGIAQTT FVGIILSRGT
AASVSFLAGH VVNVYIFSVS PLSLLACMFP SVFVNDGSQL PQKFYWWFFQ TVPGMTGVLL
LLVLAIMYVF ASHHFRRRSF RGFWLTHHLY ILLYVLLIIH GSFALIQLPR FHIFFLVPAL
IYVGDKLVSL SRKKVEIGVV KAELLPSGVT HLQFQRPQGF EYKSGQWVRI ACLALGTTEY
HPFTLTSAPH EDTLSLHIRA AGPWTIRLRE IYSSPMGDGC ARYPKLYLDG PFGEGHQEWH
KFEVSVLVGG GIGVTPFASI LKDLVFKSSL GSQMLCKKIY FIWVTRTQRQ FEWLADIIRE
VEENDHQDLV SVHIYITQLA EKFDLRTTML KVLTRSLFTG LRSVTHFGRP PFEPFFNSLQ
EVHPQVRKIG VFSCGPPGMT KNVEKACQLI NRQDQAHFIH HYENF
//
