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Database: UniProt
Entry: P09933
LinkDB: P09933
Original site: P09933 
ID   PERT_PIG                Reviewed;         926 AA.
AC   P09933;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   16-JAN-2019, entry version 155.
DE   RecName: Full=Thyroid peroxidase;
DE            Short=TPO;
DE            EC=1.11.1.8 {ECO:0000269|PubMed:12325367, ECO:0000269|PubMed:2996435, ECO:0000269|PubMed:7142155};
DE   Flags: Precursor;
GN   Name=TPO;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC   Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3654642;
RA   Magnusson R.P., Gestautas J., Taurog A., Rapoport B.;
RT   "Molecular cloning of the structural gene for porcine thyroid
RT   peroxidase.";
RL   J. Biol. Chem. 262:13885-13888(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 595-926.
RX   PubMed=3780975; DOI=10.1016/0014-5793(86)81055-9;
RA   Magnusson R.P., Gestautas J., Seto P., Taurog A., Rapoport B.;
RT   "Isolation and characterization of a cDNA clone for porcine thyroid
RT   peroxidase.";
RL   FEBS Lett. 208:391-396(1986).
RN   [3]
RP   PROTEIN SEQUENCE OF 110-115; 267-274; 301-308 AND 340-351, AND
RP   GLYCOSYLATION AT ASN-129; ASN-277; ASN-307 AND ASN-342.
RX   PubMed=1497352; DOI=10.1016/0003-9861(92)90679-Q;
RA   Rawitch A.B., Pollock G., Yang S.-X., Taurog A.;
RT   "Thyroid peroxidase glycosylation: the location and nature of the N-
RT   linked oligosaccharide units in porcine thyroid peroxidase.";
RL   Arch. Biochem. Biophys. 297:321-327(1992).
RN   [4]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=12325367;
RA   Coval M.L., Taurog A.;
RT   "Purification and iodinating activity of hog thyroid peroxidase.";
RL   J. Biol. Chem. 242:5510-5523(1967).
RN   [5]
RP   CATALYTIC ACTIVITY, AND CHARACTERIZATION.
RX   PubMed=7142155;
RA   Ohtaki S., Nakagawa H., Nakamura M., Yamazaki I.;
RT   "One- and two-electron oxidations of tyrosine, monoiodotyrosine, and
RT   diiodotyrosine catalyzed by hog thyroid peroxidase.";
RL   J. Biol. Chem. 257:13398-13403(1982).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, AND CHARACTERIZATION.
RX   PubMed=2996435; DOI=10.1016/0003-9861(85)90477-1;
RA   Virion A., Courtin F., Deme D., Michot J.L., Kaniewski J., Pommier J.;
RT   "Spectral characteristics and catalytic properties of thyroid
RT   peroxidase-H2O2 compounds in the iodination and coupling reactions.";
RL   Arch. Biochem. Biophys. 242:41-47(1985).
CC   -!- FUNCTION: Iodination and coupling of the hormonogenic tyrosines in
CC       thyroglobulin to yield the thyroid hormones T(3) and T(4).
CC       {ECO:0000269|PubMed:12325367, ECO:0000269|PubMed:2996435}.
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;
CC         EC=1.11.1.8; Evidence={ECO:0000269|PubMed:12325367,
CC         ECO:0000269|PubMed:2996435, ECO:0000269|PubMed:7142155};
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:0000269|PubMed:12325367,
CC         ECO:0000269|PubMed:2996435, ECO:0000269|PubMed:7142155};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thyroglobulin]-3-iodo-L-tyrosine + H(+) + H2O2 + iodide
CC         = [thyroglobulin]-3,5-diiodo-L-tyrosine + 2 H2O;
CC         Xref=Rhea:RHEA:48960, Rhea:RHEA-COMP:12275, Rhea:RHEA-
CC         COMP:12276, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:16382, ChEBI:CHEBI:90870,
CC         ChEBI:CHEBI:90871; EC=1.11.1.8;
CC         Evidence={ECO:0000269|PubMed:12325367,
CC         ECO:0000269|PubMed:2996435, ECO:0000269|PubMed:7142155};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 [thyroglobulin]-3,5-diiodo-L-tyrosine + H2O2 =
CC         [thyroglobulin]-dehydroalanine + [thyroglobulin]-L-thyroxine + 2
CC         H2O; Xref=Rhea:RHEA:48964, Rhea:RHEA-COMP:12276, Rhea:RHEA-
CC         COMP:12277, Rhea:RHEA-COMP:12278, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:90871, ChEBI:CHEBI:90872,
CC         ChEBI:CHEBI:90873; EC=1.11.1.8;
CC         Evidence={ECO:0000269|PubMed:12325367,
CC         ECO:0000269|PubMed:2996435, ECO:0000269|PubMed:7142155};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thyroglobulin]-3,5-diiodo-L-tyrosine + [thyroglobulin]-
CC         3-iodo-L-tyrosine + H2O2 = [thyroglobulin]-3,3',5-triiodo-L-
CC         thyronine + [thyroglobulin]-dehydroalanine + 2 H2O;
CC         Xref=Rhea:RHEA:48968, Rhea:RHEA-COMP:12275, Rhea:RHEA-
CC         COMP:12276, Rhea:RHEA-COMP:12278, Rhea:RHEA-COMP:12279,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:90870,
CC         ChEBI:CHEBI:90871, ChEBI:CHEBI:90873, ChEBI:CHEBI:90874;
CC         EC=1.11.1.8; Evidence={ECO:0000269|PubMed:12325367,
CC         ECO:0000269|PubMed:2996435, ECO:0000269|PubMed:7142155};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00298};
CC       Note=Binds 1 Ca(2+) ion per heterodimer. {ECO:0000255|PROSITE-
CC       ProRule:PRU00298};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00298};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group covalently
CC       per heterodimer. {ECO:0000255|PROSITE-ProRule:PRU00298};
CC   -!- PATHWAY: Hormone biosynthesis; thyroid hormone biosynthesis.
CC   -!- SUBUNIT: Interacts with DUOX1, DUOX2 and CYBA. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- PTM: Heme is covalently bound through a H(2)O(2)-dependent
CC       autocatalytic process. Heme insertion is important for the
CC       delivery of protein at the cell surface (By similarity).
CC       {ECO:0000250}.
CC   -!- PTM: Cleaved in its N-terminal part. {ECO:0000250}.
CC   -!- PTM: N-glycosylated; contains mannose and N-acetylglucosamine.
CC       {ECO:0000269|PubMed:1497352}.
CC   -!- SIMILARITY: Belongs to the peroxidase family. XPO subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00298}.
DR   EMBL; X04645; CAA28306.1; -; mRNA.
DR   PIR; A27416; OPPGIT.
DR   UniGene; Ssc.99; -.
DR   ProteinModelPortal; P09933; -.
DR   SMR; P09933; -.
DR   STRING; 9823.ENSSSCP00000027731; -.
DR   PeroxiBase; 3329; SscTPO.
DR   iPTMnet; P09933; -.
DR   PaxDb; P09933; -.
DR   PRIDE; P09933; -.
DR   eggNOG; KOG2408; Eukaryota.
DR   eggNOG; ENOG410XPZ3; LUCA.
DR   HOGENOM; HOG000016084; -.
DR   HOVERGEN; HBG000071; -.
DR   InParanoid; P09933; -.
DR   BioCyc; MetaCyc:MONOMER-14809; -.
DR   BRENDA; 1.11.1.8; 6170.
DR   UniPathway; UPA00194; -.
DR   Proteomes; UP000008227; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0004601; F:peroxidase activity; IBA:GO_Central.
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   Gene3D; 1.10.640.10; -; 1.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
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:SF60; PTHR11475:SF60; 1.
DR   Pfam; PF03098; An_peroxidase; 1.
DR   Pfam; PF00084; Sushi; 1.
DR   PRINTS; PR00457; ANPEROXIDASE.
DR   SMART; SM00032; CCP; 1.
DR   SMART; SM00179; EGF_CA; 1.
DR   SUPFAM; SSF48113; SSF48113; 1.
DR   SUPFAM; SSF57535; SSF57535; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS00435; PEROXIDASE_1; 1.
DR   PROSITE; PS50292; PEROXIDASE_3; 1.
DR   PROSITE; PS50923; SUSHI; 1.
PE   1: Evidence at protein level;
KW   Calcium; Complete proteome; Direct protein sequencing; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Heme; Hydrogen peroxide; Iron;
KW   Membrane; Metal-binding; Oxidoreductase; Peroxidase;
KW   Reference proteome; Signal; Sushi; Thyroid hormones biosynthesis;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     14       {ECO:0000255}.
FT   CHAIN        15    926       Thyroid peroxidase.
FT                                /FTId=PRO_0000023664.
FT   TOPO_DOM     19    844       Extracellular. {ECO:0000255}.
FT   TRANSMEM    845    869       Helical. {ECO:0000255}.
FT   TOPO_DOM    870    926       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      738    793       Sushi. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DOMAIN      794    837       EGF-like; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   ACT_SITE    239    239       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00298}.
FT   METAL       240    240       Calcium. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00298}.
FT   METAL       321    321       Calcium. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00298}.
FT   METAL       323    323       Calcium; via carbonyl oxygen.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00298}.
FT   METAL       325    325       Calcium. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00298}.
FT   METAL       327    327       Calcium. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00298}.
FT   METAL       493    493       Iron (heme axial ligand).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00298}.
FT   BINDING     238    238       Heme (covalent; via 2 links).
FT                                {ECO:0000250}.
FT   BINDING     398    398       Heme (covalent; via 2 links).
FT                                {ECO:0000250}.
FT   SITE        395    395       Transition state stabilizer.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00298}.
FT   CARBOHYD    129    129       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:1497352}.
FT   CARBOHYD    277    277       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:1497352}.
FT   CARBOHYD    307    307       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:1497352}.
FT   CARBOHYD    342    342       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:1497352}.
FT   DISULFID    142    158       {ECO:0000250}.
FT   DISULFID    259    269       {ECO:0000250}.
FT   DISULFID    263    286       {ECO:0000250}.
FT   DISULFID    596    653       {ECO:0000250}.
FT   DISULFID    694    719       {ECO:0000250}.
FT   DISULFID    740    780       {ECO:0000250}.
FT   DISULFID    766    792       {ECO:0000250}.
FT   DISULFID    798    812       {ECO:0000250}.
FT   DISULFID    806    821       {ECO:0000250}.
FT   DISULFID    823    836       {ECO:0000250}.
SQ   SEQUENCE   926 AA;  100443 MW;  8549FF6F0F742C5E CRC64;
     MGARAVLGVT LAVACAGAFF ASILRRKDLL GGDTEASGVA GLVEASRLLV DEAIHTTMRR
     NLRKRGIFSP SQLLSFSKLP EPTSRTASRA AEIMETAVQE VKRRVCRRRD TDQLPTDVLS
     EELLSTIANL SGCLPHMLPP SCPHTCLANK YRLITGACNN RDHPRWGASN TALARWLPPA
     YEDGVTEPRG WNPHFLYNGL PLPPVREVTR QVIHVSNEAV TEDGQYSDLL MAWGQYIDHD
     IAFTPQSTSK AAFAGGADCQ LTCENRSPCF PIQLPTNASG AAGATCLPFY RSSAACGSGR
     QGALVGNLSW AAPRQQMNGL TSFLDASTVY GSSPAQEQRL RNWTSAEGLL RVNTRHRDAG
     RAFLPFAPPP APPACAPEPG TPAARAPCFL AGDSRASEVP GLTALHTLWL REHNRLAAAF
     KALNAHWSAD TVYQEARKVV GALHQIVTLR DYVPKILGAE AFGQHVGPYQ GYDPAVDPTV
     SNVFSTAAFR FGHATIHPLV RRLDARFQEH PGSHLPLRAA FFQPWRLLRE GGVDPVLRGL
     LARPAKLQVQ DQLMNEELTE RLFVLSNSGT LDLASINLQR GRDHGLPGYN EWREFCGLSR
     LETWADLSAA TANGRVADRI LGLYQHPDNI DVWLGGLAES FLPGARTGPL FACIIGKQMR
     ALRDGDRFWW ENPGVFTEAQ RRELSRHSMS RVICDNSGLS HVPLDAFRVG QWPQEFEPCA
     SIQGMDLGAW REAPPSGDAC GFPDPVEDGG FLLCEERGQR VLVFSCRHGF RLRGPAQITC
     TPRGWDSPPP LCKDINECED ETDPPCHASA RCKNTKGGVL CECSDPLVLG EDGRTCVDAG
     RLPRASVVSI ALGAVLVCGL AGLAWTVVCR WTHADARPLL PVGEGEGDGK SPSLPLPGCG
     NRRDVGAAPA LEVEQDLSCG SRGLCE
//
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