ID A0A091W672_OPIHO Unreviewed; 846 AA.
AC A0A091W672;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Thyroid peroxidase {ECO:0000256|ARBA:ARBA00021693};
DE EC=1.11.1.8 {ECO:0000256|ARBA:ARBA00012311};
DE Flags: Fragment;
GN ORFNames=N306_01904 {ECO:0000313|EMBL:KFR10610.1};
OS Opisthocomus hoazin (Hoatzin) (Phasianus hoazin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Opisthocomiformes; Opisthocomidae;
OC Opisthocomus.
OX NCBI_TaxID=30419 {ECO:0000313|EMBL:KFR10610.1, ECO:0000313|Proteomes:UP000053605};
RN [1] {ECO:0000313|EMBL:KFR10610.1, ECO:0000313|Proteomes:UP000053605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N306 {ECO:0000313|EMBL:KFR10610.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Iodination and coupling of the hormonogenic tyrosines in
CC thyroglobulin to yield the thyroid hormones T(3) and T(4).
CC {ECO:0000256|ARBA:ARBA00003834}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + H2O2 + 2 iodide = diiodine + 2 H2O;
CC Xref=Rhea:RHEA:23336, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:16382, ChEBI:CHEBI:17606; EC=1.11.1.8;
CC Evidence={ECO:0000256|ARBA:ARBA00000959};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 [thyroglobulin]-3,5-diiodo-L-tyrosine + H2O2 =
CC [thyroglobulin]-dehydroalanine + [thyroglobulin]-L-thyroxine + 2 H2O;
CC Xref=Rhea:RHEA:48964, Rhea:RHEA-COMP:12276, Rhea:RHEA-COMP:12277,
CC Rhea:RHEA-COMP:12278, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:90871, ChEBI:CHEBI:90872, ChEBI:CHEBI:90873; EC=1.11.1.8;
CC Evidence={ECO:0000256|ARBA:ARBA00000407};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thyroglobulin]-3,5-diiodo-L-tyrosine + [thyroglobulin]-3-
CC iodo-L-tyrosine + H2O2 = [thyroglobulin]-3,3',5-triiodo-L-thyronine +
CC [thyroglobulin]-dehydroalanine + 2 H2O; Xref=Rhea:RHEA:48968,
CC Rhea:RHEA-COMP:12275, Rhea:RHEA-COMP:12276, Rhea:RHEA-COMP:12278,
CC Rhea:RHEA-COMP:12279, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:90870, ChEBI:CHEBI:90871, ChEBI:CHEBI:90873,
CC ChEBI:CHEBI:90874; EC=1.11.1.8;
CC Evidence={ECO:0000256|ARBA:ARBA00000048};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thyroglobulin]-3-iodo-L-tyrosine + H(+) + H2O2 + iodide =
CC [thyroglobulin]-3,5-diiodo-L-tyrosine + 2 H2O; Xref=Rhea:RHEA:48960,
CC Rhea:RHEA-COMP:12275, Rhea:RHEA-COMP:12276, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:16382,
CC ChEBI:CHEBI:90870, ChEBI:CHEBI:90871; EC=1.11.1.8;
CC Evidence={ECO:0000256|ARBA:ARBA00001533};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thyroglobulin]-L-tyrosine + H(+) + H2O2 + iodide =
CC [thyroglobulin]-3-iodo-L-tyrosine + 2 H2O; Xref=Rhea:RHEA:48956,
CC Rhea:RHEA-COMP:12274, Rhea:RHEA-COMP:12275, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:16382,
CC ChEBI:CHEBI:46858, ChEBI:CHEBI:90870; EC=1.11.1.8;
CC Evidence={ECO:0000256|ARBA:ARBA00000658};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|ARBA:ARBA00001970};
CC -!- PATHWAY: Hormone biosynthesis; thyroid hormone biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005197}.
CC -!- SUBUNIT: Interacts with DUOX1, DUOX2 and CYBA.
CC {ECO:0000256|ARBA:ARBA00011561}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the prostaglandin G/H synthase family.
CC {ECO:0000256|ARBA:ARBA00008928}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; KK734746; KFR10610.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091W672; -.
DR STRING; 30419.A0A091W672; -.
DR PhylomeDB; A0A091W672; -.
DR UniPathway; UPA00194; -.
DR Proteomes; UP000053605; Unassembled WGS sequence.
DR GO; GO:0016020; C: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:0004447; F:iodide peroxidase activity; IEA:UniProtKB-EC.
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; cd00033; CCP; 1.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd09825; thyroid_peroxidase; 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 1.
DR Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR019791; Haem_peroxidase_animal.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR InterPro; IPR029589; TPO.
DR PANTHER; PTHR11475; OXIDASE/PEROXIDASE; 1.
DR PANTHER; PTHR11475:SF60; THYROID PEROXIDASE; 1.
DR Pfam; PF03098; An_peroxidase; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF00084; Sushi; 1.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SMART; SM00032; CCP; 1.
DR SMART; SM00181; EGF; 1.
DR SMART; SM00179; EGF_CA; 1.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
DR PROSITE; PS50923; SUSHI; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR619791-2};
KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR619791-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000313|EMBL:KFR10610.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053605};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Sushi {ECO:0000256|ARBA:ARBA00022659, ECO:0000256|PROSITE-
KW ProRule:PRU00302};
KW Thyroid hormones biosynthesis {ECO:0000256|ARBA:ARBA00022534}.
FT DOMAIN 739..795
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 795..838
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT BINDING 493
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR619791-2"
FT NON_TER 846
FT /evidence="ECO:0000313|EMBL:KFR10610.1"
SQ SEQUENCE 846 AA; 94890 MW; B943086005BBC615 CRC64;
MKVFIILGIS AAIAFTAVFF SFLQIGKDIL FEENEGNCIA EAIQKGSNLV DYAAHNTLKR
NIQGRGIATP ASLLAFAKFP EQESQDISQA AERMEMSVQV LKQRVCRKHK RSLHSTESLS
ADLLTMVANI SGCLPYMLPP KCPNTCFTNK YRLITGACNN RQREIYSAVD IALARWLPPV
YEDGFSQPRG WDPSIRYNGV QLPLVREVTR KIIHASNEAV TEDNLYSDII MVWGQYIDHD
IAFTPQSTSR TSFLNGKECQ ISCEKQNPCF PIQVTNNDTL SAGMDCLPFY RSSPACGTGD
HGILFGNLSA LNPRQQINGL TSFLDASTVY GSTPATENKL RNLTSEEGLL KVNIKYYDNH
REYLPFTDRI PSPCAQDLNA SGDERIECFM AGDSRSSEVT SLAAMHTLWL REHNRLARAL
KHINGHWTAE TVYQEARKIV GALHQIITLR DYIPKIIGPD AFNLYIGLYR GYDPTMNPTV
SNVFSTAAFR FGHATIQPIV RRLNAHYLDD PELPNLHLHE VFFSPWRLIK QGGLDPLLRG
LLAHSAKLQV QDQLLNEELT EKLFVLSNKG SLDLASLNLQ RGRDHGLPGY NDWREFCGLP
KLETQTDLNT VITNHNVSEK IMELYHNPSN IDVWLGGLVE DFLPGARTGP LFACIIGKQM
KALRDGDRFW WENDNVFTEA QKHELKKHSL SRVICDNTGI SEVPADAFQL GKFPQDFKHC
DSVPGMNLEA WQEFYQAGEI CGTPKSVKNG DFVYCSDFEK STVTYSCQYG FQLQGEEQLT
CTSKGWNFEV PICIDINECE NEINPPCSLS AKCINTEGSY KCLCTDPYKL AEDGRTCIGN
ACEPTV
//
