DUOX1_HUMAN
ID DUOX1_HUMAN Reviewed; 1551 AA.
AC Q9NRD9; A6NH28; Q14C94; Q6ZMB3; Q6ZR09; Q9NZC1;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Dual oxidase 1;
DE EC=1.11.1.-;
DE EC=1.6.3.1;
DE AltName: Full=Large NOX 1;
DE AltName: Full=Long NOX 1;
DE AltName: Full=NADPH thyroid oxidase 1;
DE AltName: Full=Thyroid oxidase 1;
DE Flags: Precursor;
GN Name=DUOX1; Synonyms=DUOX, LNOX1, THOX1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INDUCTION.
RC TISSUE=Thyroid;
RX PubMed=10806195; DOI=10.1074/jbc.m000916200;
RA De Deken X., Wang D., Many M.-C., Costagliola S., Libert F., Vassart G.,
RA Dumont J.E., Miot F.;
RT "Cloning of two human thyroid cDNAs encoding new members of the NADPH
RT oxidase family.";
RL J. Biol. Chem. 275:23227-23233(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT PHE-1178, FUNCTION,
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Lung;
RX PubMed=11514595; DOI=10.1083/jcb.200103132;
RA Edens W.A., Sharling L., Cheng G., Shapira R., Kinkade J.M., Lee T.,
RA Edens H.A., Tang X., Sullards C., Flaherty D.B., Benian G.M., Lambeth J.D.;
RT "Tyrosine cross-linking of extracellular matrix is catalyzed by Duox, a
RT multidomain oxidase/peroxidase with homology to the phagocyte oxidase
RT subunit gp91phox.";
RL J. Cell Biol. 154:879-891(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1030-1551 (ISOFORMS 1/2), AND VARIANT ARG-1026.
RC TISSUE=Lung, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP GLYCOSYLATION.
RX PubMed=11822874; DOI=10.1006/excr.2001.5444;
RA De Deken X., Wang D., Dumont J.E., Miot F.;
RT "Characterization of ThOX proteins as components of the thyroid H(2)O(2)-
RT generating system.";
RL Exp. Cell Res. 273:187-196(2002).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12824283; DOI=10.1096/fj.02-1104fje;
RA Geiszt M., Witta J., Baffi J., Lekstrom K., Leto T.L.;
RT "Dual oxidases represent novel hydrogen peroxide sources supporting mucosal
RT surface host defense.";
RL FASEB J. 17:1502-1504(2003).
RN [8]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15210697; DOI=10.1074/jbc.m404983200;
RA Schwarzer C., Machen T.E., Illek B., Fischer H.;
RT "NADPH oxidase-dependent acid production in airway epithelial cells.";
RL J. Biol. Chem. 279:36454-36461(2004).
RN [9]
RP INDUCTION.
RX PubMed=16111680; DOI=10.1016/j.febslet.2005.08.002;
RA Harper R.W., Xu C., Eiserich J.P., Chen Y., Kao C.-Y., Thai P., Setiadi H.,
RA Wu R.;
RT "Differential regulation of dual NADPH oxidases/peroxidases, Duox1 and
RT Duox2, by Th1 and Th2 cytokines in respiratory tract epithelium.";
RL FEBS Lett. 579:4911-4917(2005).
RN [10]
RP INTERACTION WITH TXNDC11; TPO AND CYBA.
RX PubMed=15561711; DOI=10.1074/jbc.m407709200;
RA Wang D., De Deken X., Milenkovic M., Song Y., Pirson I., Dumont J.E.,
RA Miot F.;
RT "Identification of a novel partner of duox: EFP1, a thioredoxin-related
RT protein.";
RL J. Biol. Chem. 280:3096-3103(2005).
RN [11]
RP CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=15972824; DOI=10.1074/jbc.m500516200;
RA Ameziane-El-Hassani R., Morand S., Boucher J.L., Frapart Y.-M.,
RA Apostolou D., Agnandji D., Gnidehou S., Ohayon R., Noel-Hudson M.-S.,
RA Francon J., Lalaoui K., Virion A., Dupuy C.;
RT "Dual oxidase-2 has an intrinsic Ca2+-dependent H2O2-generating activity.";
RL J. Biol. Chem. 280:30046-30054(2005).
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:0000269|PubMed:11514595, ECO:0000269|PubMed:12824283}.
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:0000269|PubMed:11514595, ECO:0000269|PubMed:15972824};
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:0000269|PubMed:11514595, ECO:0000269|PubMed:15972824};
CC -!- ACTIVITY REGULATION: The NADPH oxidase activity is calcium-dependent.
CC Peroxidase activity is inhibited by aminobenzohydrazide.
CC {ECO:0000269|PubMed:11514595, ECO:0000269|PubMed:15972824}.
CC -!- PATHWAY: Hormone biosynthesis; thyroid hormone biosynthesis.
CC -!- SUBUNIT: Interacts with TXNDC11, TPO and CYBA.
CC {ECO:0000269|PubMed:15561711}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:10806195, ECO:0000269|PubMed:15210697}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:10806195,
CC ECO:0000269|PubMed:15210697}. Note=Localizes to the apical membrane of
CC epithelial cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NRD9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NRD9-2; Sequence=VSP_017262, VSP_017263;
CC -!- TISSUE SPECIFICITY: Expressed in thyrocytes and tracheal surface
CC epithelial cells (at protein level). Expressed in thyroid, trachea,
CC bronchium, and to a lower extent, in placenta, testis, prostate,
CC pancreas and heart. {ECO:0000269|PubMed:10806195,
CC ECO:0000269|PubMed:11514595, ECO:0000269|PubMed:12824283,
CC ECO:0000269|PubMed:15210697}.
CC -!- DEVELOPMENTAL STAGE: Widely expressed in fetal tissues.
CC {ECO:0000269|PubMed:11514595}.
CC -!- INDUCTION: By forskolin (at protein level). By thyrotropin and the Th2-
CC specific cytokines IL-4 and IL-13. {ECO:0000269|PubMed:10806195,
CC ECO:0000269|PubMed:16111680}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:11822874}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the peroxidase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK128591; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD18816.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF230495; AAF73921.1; -; mRNA.
DR EMBL; AF213465; AAF71295.1; -; mRNA.
DR EMBL; AK128591; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK172859; BAD18816.1; ALT_INIT; mRNA.
DR EMBL; AC051619; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC114628; AAI14629.1; -; mRNA.
DR CCDS; CCDS32221.1; -. [Q9NRD9-1]
DR RefSeq; NP_059130.2; NM_017434.4. [Q9NRD9-1]
DR RefSeq; NP_787954.1; NM_175940.2. [Q9NRD9-1]
DR RefSeq; XP_011519984.1; XM_011521682.1. [Q9NRD9-2]
DR PDB; 7D3E; EM; 2.80 A; A/C=1-1551.
DR PDB; 7D3F; EM; 2.30 A; A/C=1-1551.
DR PDBsum; 7D3E; -.
DR PDBsum; 7D3F; -.
DR AlphaFoldDB; Q9NRD9; -.
DR SMR; Q9NRD9; -.
DR BioGRID; 119815; 12.
DR IntAct; Q9NRD9; 3.
DR STRING; 9606.ENSP00000317997; -.
DR PeroxiBase; 3339; HsDuOx01.
DR TCDB; 5.B.1.1.6; the phagocyte (gp91(phox)) nadph oxidase family.
DR GlyGen; Q9NRD9; 5 sites.
DR iPTMnet; Q9NRD9; -.
DR PhosphoSitePlus; Q9NRD9; -.
DR BioMuta; DUOX1; -.
DR DMDM; 74719102; -.
DR EPD; Q9NRD9; -.
DR jPOST; Q9NRD9; -.
DR MassIVE; Q9NRD9; -.
DR MaxQB; Q9NRD9; -.
DR PaxDb; Q9NRD9; -.
DR PeptideAtlas; Q9NRD9; -.
DR PRIDE; Q9NRD9; -.
DR ProteomicsDB; 82341; -. [Q9NRD9-1]
DR ProteomicsDB; 82342; -. [Q9NRD9-2]
DR Antibodypedia; 11716; 126 antibodies from 28 providers.
DR DNASU; 53905; -.
DR Ensembl; ENST00000321429.8; ENSP00000317997.4; ENSG00000137857.18. [Q9NRD9-1]
DR Ensembl; ENST00000389037.7; ENSP00000373689.3; ENSG00000137857.18. [Q9NRD9-1]
DR Ensembl; ENST00000561166.1; ENSP00000454065.1; ENSG00000137857.18. [Q9NRD9-2]
DR GeneID; 53905; -.
DR KEGG; hsa:53905; -.
DR MANE-Select; ENST00000389037.7; ENSP00000373689.3; NM_175940.3; NP_787954.1.
DR UCSC; uc001zus.3; human. [Q9NRD9-1]
DR CTD; 53905; -.
DR DisGeNET; 53905; -.
DR GeneCards; DUOX1; -.
DR HGNC; HGNC:3062; DUOX1.
DR HPA; ENSG00000137857; Tissue enhanced (esophagus, skin).
DR MIM; 606758; gene.
DR neXtProt; NX_Q9NRD9; -.
DR OpenTargets; ENSG00000137857; -.
DR PharmGKB; PA27516; -.
DR VEuPathDB; HostDB:ENSG00000137857; -.
DR eggNOG; KOG0039; Eukaryota.
DR GeneTree; ENSGT00940000161792; -.
DR HOGENOM; CLU_004482_1_0_1; -.
DR InParanoid; Q9NRD9; -.
DR OMA; AREVIYT; -.
DR OrthoDB; 414294at2759; -.
DR PhylomeDB; Q9NRD9; -.
DR TreeFam; TF105424; -.
DR BRENDA; 1.6.3.1; 2681.
DR PathwayCommons; Q9NRD9; -.
DR Reactome; R-HSA-209968; Thyroxine biosynthesis.
DR SABIO-RK; Q9NRD9; -.
DR SignaLink; Q9NRD9; -.
DR SIGNOR; Q9NRD9; -.
DR UniPathway; UPA00194; -.
DR BioGRID-ORCS; 53905; 10 hits in 1063 CRISPR screens.
DR ChiTaRS; DUOX1; human.
DR GeneWiki; Dual_oxidase_1; -.
DR GenomeRNAi; 53905; -.
DR Pharos; Q9NRD9; Tbio.
DR PRO; PR:Q9NRD9; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9NRD9; protein.
DR Bgee; ENSG00000137857; Expressed in tongue squamous epithelium and 136 other tissues.
DR ExpressionAtlas; Q9NRD9; baseline and differential.
DR Genevisible; Q9NRD9; HS.
DR GO; GO:0016324; C:apical plasma membrane; NAS:UniProtKB.
DR GO; GO:0031252; C:cell leading edge; IGI:UniProtKB.
DR GO; GO:0009986; C:cell surface; IGI:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0043020; C:NADPH oxidase complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
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; TAS:Reactome.
DR GO; GO:0106293; F:NADH oxidase H202-forming activity; IEA:RHEA.
DR GO; GO:0050661; F:NADP binding; NAS:UniProtKB.
DR GO; GO:0106294; F:NADPH oxidase H202-forming activity; IEA:RHEA.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0016175; F:superoxide-generating NAD(P)H oxidase activity; IBA:GO_Central.
DR GO; GO:0042335; P:cuticle development; IMP:UniProtKB.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0006952; P:defense response; IBA:GO_Central.
DR GO; GO:0042446; P:hormone biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IGI:UniProtKB.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:2000147; P:positive regulation of cell motility; IGI:UniProtKB.
DR GO; GO:0090303; P:positive regulation of wound healing; IGI:UniProtKB.
DR GO; GO:0051591; P:response to cAMP; IDA:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR GO; GO:0042554; P:superoxide anion generation; IBA:GO_Central.
DR GO; GO:0006590; P:thyroid hormone generation; TAS:Reactome.
DR CDD; cd09820; dual_peroxidase_like; 1.
DR CDD; cd00051; EFh; 2.
DR Gene3D; 1.10.640.10; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR029595; DUOX1/Duox.
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; PTHR11972:SF75; 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 SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF48113; SSF48113; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 3.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cell membrane; FAD;
KW Flavoprotein; Glycoprotein; Hydrogen peroxide; Membrane; Metal-binding;
KW NADP; Oxidoreductase; Peroxidase; Reference proteome; Repeat; Signal;
KW Thyroid hormones biosynthesis; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1551
FT /note="Dual oxidase 1"
FT /id="PRO_0000223344"
FT TOPO_DOM 22..596
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 597..617
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 618..1044
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1045..1065
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1066..1080
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1081..1101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1102..1148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1149..1171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1172..1188
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1189..1209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1210..1226
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1227..1247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1248
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1249..1269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1270..1551
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 815..850
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 851..886
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 895..930
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 1087..1269
FT /note="Ferric oxidoreductase"
FT DOMAIN 1270..1376
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 26..593
FT /note="Peroxidase-like; mediates peroxidase activity"
FT REGION 150..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 956..1248
FT /note="Interaction with TXNDC11"
FT /evidence="ECO:0000250"
FT COMPBIAS 153..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 828
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 830
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 832
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 834
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 839
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 864
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 866
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 868
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 875
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 461
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 534
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..354
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_017262"
FT VAR_SEQ 355..405
FT /note="SSVSRALRVCNSYWSREHPSLQSAEDVDALLLGMASQIAEREDHVLVEDVR
FT -> MWMHCCWAWPPRSQSERTMCWLKMCGVSLRLSLQVVNSWPLGRGSAGLPEP (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_017263"
FT VARIANT 962
FT /note="I -> T (in dbSNP:rs16939743)"
FT /id="VAR_049104"
FT VARIANT 1026
FT /note="C -> R (in dbSNP:rs16939752)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_025321"
FT VARIANT 1178
FT /note="L -> F (in dbSNP:rs2458236)"
FT /evidence="ECO:0000269|PubMed:11514595"
FT /id="VAR_025322"
FT CONFLICT 413
FT /note="K -> E (in Ref. 3; AK128591)"
FT /evidence="ECO:0000305"
FT CONFLICT 1388
FT /note="G -> R (in Ref. 3; BAD18816)"
FT /evidence="ECO:0000305"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:7D3F"
FT TURN 42..45
FT /evidence="ECO:0007829|PDB:7D3F"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:7D3F"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 75..83
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 97..110
FT /evidence="ECO:0007829|PDB:7D3F"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:7D3F"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:7D3F"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 176..179
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 183..189
FT /evidence="ECO:0007829|PDB:7D3F"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:7D3F"
FT TURN 237..240
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 243..266
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 272..293
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 295..300
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 320..331
FT /evidence="ECO:0007829|PDB:7D3F"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:7D3F"
FT STRAND 357..363
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 378..390
FT /evidence="ECO:0007829|PDB:7D3F"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 402..405
FT /evidence="ECO:0007829|PDB:7D3F"
FT STRAND 411..417
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 419..429
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 435..441
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 450..452
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 455..459
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 464..471
FT /evidence="ECO:0007829|PDB:7D3F"
FT TURN 472..474
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 476..478
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 481..488
FT /evidence="ECO:0007829|PDB:7D3F"
FT STRAND 490..492
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 495..510
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 519..521
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 526..534
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 537..545
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 549..551
FT /evidence="ECO:0007829|PDB:7D3F"
FT STRAND 563..565
FT /evidence="ECO:0007829|PDB:7D3E"
FT HELIX 592..618
FT /evidence="ECO:0007829|PDB:7D3F"
FT STRAND 645..648
FT /evidence="ECO:0007829|PDB:7D3F"
FT STRAND 652..654
FT /evidence="ECO:0007829|PDB:7D3F"
FT STRAND 657..663
FT /evidence="ECO:0007829|PDB:7D3F"
FT STRAND 665..672
FT /evidence="ECO:0007829|PDB:7D3F"
FT STRAND 677..682
FT /evidence="ECO:0007829|PDB:7D3F"
FT STRAND 690..693
FT /evidence="ECO:0007829|PDB:7D3F"
FT STRAND 701..705
FT /evidence="ECO:0007829|PDB:7D3F"
FT STRAND 707..709
FT /evidence="ECO:0007829|PDB:7D3F"
FT STRAND 712..715
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 719..734
FT /evidence="ECO:0007829|PDB:7D3F"
FT STRAND 741..744
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 747..752
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 757..775
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 792..798
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 804..811
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 818..827
FT /evidence="ECO:0007829|PDB:7D3F"
FT STRAND 832..835
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 837..849
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 852..863
FT /evidence="ECO:0007829|PDB:7D3F"
FT STRAND 868..871
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 873..883
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 894..901
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 917..923
FT /evidence="ECO:0007829|PDB:7D3F"
FT TURN 1025..1027
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 1028..1068
FT /evidence="ECO:0007829|PDB:7D3F"
FT TURN 1071..1074
FT /evidence="ECO:0007829|PDB:7D3F"
FT TURN 1076..1078
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 1081..1099
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 1100..1104
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 1106..1113
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 1116..1119
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 1123..1125
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 1126..1157
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 1160..1166
FT /evidence="ECO:0007829|PDB:7D3F"
FT TURN 1168..1170
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 1182..1187
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 1190..1208
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 1211..1216
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 1219..1225
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 1228..1238
FT /evidence="ECO:0007829|PDB:7D3F"
FT TURN 1239..1241
FT /evidence="ECO:0007829|PDB:7D3F"
FT STRAND 1243..1245
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 1249..1269
FT /evidence="ECO:0007829|PDB:7D3F"
FT STRAND 1273..1275
FT /evidence="ECO:0007829|PDB:7D3F"
FT STRAND 1277..1283
FT /evidence="ECO:0007829|PDB:7D3F"
FT TURN 1284..1286
FT /evidence="ECO:0007829|PDB:7D3F"
FT STRAND 1287..1293
FT /evidence="ECO:0007829|PDB:7D3F"
FT STRAND 1305..1310
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 1311..1313
FT /evidence="ECO:0007829|PDB:7D3F"
FT STRAND 1319..1323
FT /evidence="ECO:0007829|PDB:7D3F"
FT STRAND 1329..1337
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 1341..1349
FT /evidence="ECO:0007829|PDB:7D3F"
FT STRAND 1364..1367
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 1376..1379
FT /evidence="ECO:0007829|PDB:7D3F"
FT STRAND 1380..1388
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 1389..1392
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 1393..1408
FT /evidence="ECO:0007829|PDB:7D3F"
FT STRAND 1416..1424
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 1430..1442
FT /evidence="ECO:0007829|PDB:7D3F"
FT STRAND 1448..1454
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 1458..1460
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 1463..1473
FT /evidence="ECO:0007829|PDB:7D3F"
FT STRAND 1478..1481
FT /evidence="ECO:0007829|PDB:7D3F"
FT TURN 1483..1485
FT /evidence="ECO:0007829|PDB:7D3F"
FT STRAND 1488..1494
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 1498..1508
FT /evidence="ECO:0007829|PDB:7D3F"
FT STRAND 1509..1511
FT /evidence="ECO:0007829|PDB:7D3F"
FT STRAND 1513..1521
FT /evidence="ECO:0007829|PDB:7D3F"
FT HELIX 1523..1538
FT /evidence="ECO:0007829|PDB:7D3F"
FT STRAND 1539..1548
FT /evidence="ECO:0007829|PDB:7D3F"
SQ SEQUENCE 1551 AA; 177235 MW; 37CF124A579446B0 CRC64;
MGFCLALAWT LLVGAWTPLG AQNPISWEVQ RFDGWYNNLM EHRWGSKGSR LQRLVPASYA
DGVYQPLGEP HLPNPRDLSN TISRGPAGLA SLRNRTVLGV FFGYHVLSDL VSVETPGCPA
EFLNIRIPPG DPMFDPDQRG DVVLPFQRSR WDPETGRSPS NPRDPANQVT GWLDGSAIYG
SSHSWSDALR SFSRGQLASG PDPAFPRDSQ NPLLMWAAPD PATGQNGPRG LYAFGAERGN
REPFLQALGL LWFRYHNLWA QRLARQHPDW EDEELFQHAR KRVIATYQNI AVYEWLPSFL
QKTLPEYTGY RPFLDPSISS EFVAASEQFL STMVPPGVYM RNASCHFQGV INRNSSVSRA
LRVCNSYWSR EHPSLQSAED VDALLLGMAS QIAEREDHVL VEDVRDFWPG PLKFSRTDHL
ASCLQRGRDL GLPSYTKARA ALGLSPITRW QDINPALSRS NDTVLEATAA LYNQDLSWLE
LLPGGLLESH RDPGPLFSTI VLEQFVRLRD GDRYWFENTR NGLFSKKEIE EIRNTTLQDV
LVAVINIDPS ALQPNVFVWH KGDPCPQPRQ LSTEGLPACA PSVVRDYFEG SGFGFGVTIG
TLCCFPLVSL LSAWIVARLR MRNFKRLQGQ DRQSIVSEKL VGGMEALEWQ GHKEPCRPVL
VYLQPGQIRV VDGRLTVLRT IQLQPPQKVN FVLSSNRGRR TLLLKIPKEY DLVLLFNLEE
ERQALVENLR GALKESGLSI QEWELREQEL MRAAVTREQR RHLLETFFRH LFSQVLDINQ
ADAGTLPLDS SQKVREALTC ELSRAEFAES LGLKPQDMFV ESMFSLADKD GNGYLSFREF
LDILVVFMKG SPEEKSRLMF RMYDFDGNGL ISKDEFIRML RSFIEISNNC LSKAQLAEVV
ESMFRESGFQ DKEELTWEDF HFMLRDHNSE LRFTQLCVKG VEVPEVIKDL CRRASYISQD
MICPSPRVSA RCSRSDIETE LTPQRLQCPM DTDPPQEIRR RFGKKVTSFQ PLLFTEAHRE
KFQRSCLHQT VQQFKRFIEN YRRHIGCVAV FYAIAGGLFL ERAYYYAFAA HHTGITDTTR
VGIILSRGTA ASISFMFSYI LLTMCRNLIT FLRETFLNRY VPFDAAVDFH RLIASTAIVL
TVLHSVGHVV NVYLFSISPL SVLSCLFPGL FHDDGSELPQ KYYWWFFQTV PGLTGVVLLL
ILAIMYVFAS HHFRRRSFRG FWLTHHLYIL LYVLLIIHGS FALIQLPRFH IFFLVPAIIY
GGDKLVSLSR KKVEISVVKA ELLPSGVTHL RFQRPQGFEY KSGQWVRIAC LALGTTEYHP
FTLTSAPHED TLSLHIRAAG PWTTRLREIY SAPTGDRCAR YPKLYLDGPF GEGHQEWHKF
EVSVLVGGGI GVTPFASILK DLVFKSSVSC QVFCKKIYFI WVTRTQRQFE WLADIIREVE
ENDHQDLVSV HIYITQLAEK FDLRTTMLYI CERHFQKVLN RSLFTGLRSI THFGRPPFEP
FFNSLQEVHP QVRKIGVFSC GPPGMTKNVE KACQLINRQD RTHFSHHYEN F
