GenomeNet

Database: UniProt
Entry: P35419
LinkDB: P35419
Original site: P35419 
ID   PERT_MOUSE              Reviewed;         914 AA.
AC   P35419; Q8C8B1;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   13-FEB-2019, entry version 179.
DE   RecName: Full=Thyroid peroxidase;
DE            Short=TPO;
DE            EC=1.11.1.8 {ECO:0000250|UniProtKB:P09933};
DE   Flags: Precursor;
GN   Name=Tpo;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Thyroid;
RX   PubMed=7916704; DOI=10.1016/0378-1119(93)90141-O;
RA   Kotani T., Umeki K., Yamamoto I., Takeuchi M., Takechi S.,
RA   Nakayama T., Ohtaki S.;
RT   "Nucleotide sequence of the cDNA encoding mouse thyroid peroxidase.";
RL   Gene 123:289-290(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Iodination and coupling of the hormonogenic tyrosines in
CC       thyroglobulin to yield the thyroid hormones T(3) and T(4).
CC       {ECO:0000250|UniProtKB:P09933}.
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:0000250|UniProtKB:P09933};
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:0000250|UniProtKB:P09933};
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:0000250|UniProtKB:P09933};
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:0000250|UniProtKB:P09933};
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:0000250|UniProtKB:P09933};
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   -!- SIMILARITY: Belongs to the peroxidase family. XPO subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00298}.
DR   EMBL; X60703; CAA43114.1; -; mRNA.
DR   EMBL; AK047843; BAC33171.1; -; mRNA.
DR   CCDS; CCDS25857.1; -.
DR   PIR; JN0550; JN0550.
DR   RefSeq; NP_033443.1; NM_009417.3.
DR   UniGene; Mm.4991; -.
DR   ProteinModelPortal; P35419; -.
DR   SMR; P35419; -.
DR   STRING; 10090.ENSMUSP00000021005; -.
DR   PeroxiBase; 3345; MmTPO.
DR   iPTMnet; P35419; -.
DR   PhosphoSitePlus; P35419; -.
DR   jPOST; P35419; -.
DR   PaxDb; P35419; -.
DR   PRIDE; P35419; -.
DR   DNASU; 22018; -.
DR   Ensembl; ENSMUST00000021005; ENSMUSP00000021005; ENSMUSG00000020673.
DR   GeneID; 22018; -.
DR   KEGG; mmu:22018; -.
DR   UCSC; uc007ngo.1; mouse.
DR   CTD; 7173; -.
DR   MGI; MGI:98813; Tpo.
DR   eggNOG; KOG2408; Eukaryota.
DR   eggNOG; ENOG410XPZ3; LUCA.
DR   GeneTree; ENSGT00940000158104; -.
DR   HOGENOM; HOG000016084; -.
DR   HOVERGEN; HBG000071; -.
DR   InParanoid; P35419; -.
DR   KO; K00431; -.
DR   OMA; MVWGQYI; -.
DR   OrthoDB; 276568at2759; -.
DR   PhylomeDB; P35419; -.
DR   TreeFam; TF314316; -.
DR   Reactome; R-MMU-209968; Thyroxine biosynthesis.
DR   UniPathway; UPA00194; -.
DR   PRO; PR:P35419; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   Bgee; ENSMUSG00000020673; Expressed in 31 organ(s), highest expression level in right lung.
DR   ExpressionAtlas; P35419; baseline and differential.
DR   Genevisible; P35419; MM.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
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:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
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:0035162; P:embryonic hemopoiesis; ISO:MGI.
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; IPR013032; EGF-like_CS.
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:SF60; PTHR11475:SF60; 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; SSF48113; SSF48113; 1.
DR   SUPFAM; SSF57535; SSF57535; 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; PS00435; PEROXIDASE_1; 1.
DR   PROSITE; PS50292; PEROXIDASE_3; 1.
DR   PROSITE; PS50923; SUSHI; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Complete proteome; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Heme; Hydrogen peroxide; Iron; Membrane; Metal-binding;
KW   Oxidoreductase; Peroxidase; Reference proteome; Signal; Sushi;
KW   Thyroid hormones biosynthesis; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     31       {ECO:0000255}.
FT   CHAIN        32    914       Thyroid peroxidase.
FT                                /FTId=PRO_0000023663.
FT   TOPO_DOM     32    834       Extracellular. {ECO:0000255}.
FT   TRANSMEM    835    859       Helical. {ECO:0000255}.
FT   TOPO_DOM    860    914       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      728    783       Sushi. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DOMAIN      784    827       EGF-like; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   ACT_SITE    233    233       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00298}.
FT   METAL       234    234       Calcium. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00298}.
FT   METAL       313    313       Calcium. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00298}.
FT   METAL       315    315       Calcium; via carbonyl oxygen.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00298}.
FT   METAL       317    317       Calcium. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00298}.
FT   METAL       319    319       Calcium. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00298}.
FT   METAL       482    482       Iron (heme axial ligand).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00298}.
FT   BINDING     232    232       Heme (covalent; via 2 links).
FT                                {ECO:0000250}.
FT   BINDING     387    387       Heme (covalent; via 2 links).
FT                                {ECO:0000250}.
FT   SITE        384    384       Transition state stabilizer.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00298}.
FT   CARBOHYD    123    123       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    271    271       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    299    299       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    334    334       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    603    603       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    136    152       {ECO:0000250}.
FT   DISULFID    253    263       {ECO:0000250}.
FT   DISULFID    257    278       {ECO:0000250}.
FT   DISULFID    586    643       {ECO:0000250}.
FT   DISULFID    684    709       {ECO:0000250}.
FT   DISULFID    730    770       {ECO:0000250}.
FT   DISULFID    756    782       {ECO:0000250}.
FT   DISULFID    788    802       {ECO:0000250}.
FT   DISULFID    796    811       {ECO:0000250}.
FT   DISULFID    813    826       {ECO:0000250}.
FT   CONFLICT    614    614       Y -> H (in Ref. 2; BAC33171).
FT                                {ECO:0000305}.
SQ   SEQUENCE   914 AA;  101342 MW;  595E9A0B71F3DD01 CRC64;
     MRTLGAMAIM LVVMGTVIFL SFILRSRDIL CGKTMKSHVI SAVETSQLMV DHAVYNTMKR
     NLKKREVLSP AQLLSFFKLP ESTSGAISRA AEIMETSIQV MKREQSQFST DALSADILGT
     IANLSGCLPF MLPPRCPDTC LANKYRPITG ACNNRDHPRW GASNTALARW LPPVYEDGFS
     QPKGWNPNFL YHGFPLPPVR EVTRHLIQVS NEAVTEDDQY SDFLPVWGQY IDHDIALTPQ
     STSTAAFWGG VDCQLTCENQ NPCFPIQLPS NSSGTTACLP FYRSSAACGT GDQGALFGNL
     SAANPRQQMN GLTSFLDAST VYGSSPGVEK QLRNWSSSAG LLRVNTLHLD AGRAYLPFAT
     AACAPEPGTP RTNRTPCFLA GDGRASEVPA LAAVHTLWLR EHNRLASAFK AINKHWSANT
     AYQEARKVVG ALHQIITMRD YIPKILGPDA FRQYVGPYEG YNPTVNPTVS NIFSTAAFRF
     GHATVHPLVR RLNTDFQEHT ELPRLQLRDV FFRPWRLIQE GGLDPIVRGL LARAAKLQVQ
     GQLMNEELTE RLFVLSNVGT LDLASLNLQR GRDHGLPDYN EWREFCGLSR LETPAELNKA
     IANRSMVNKI MDLYKHADNI DVWLGGLAEK FLPGARTGPL FACIIGKQMK ALRDGDRFWW
     ENTNVFTDAQ RQELEKHSLP RVICDNTGLT RVPVDAFRIG KFPQDFESCE DIPSMDLELW
     RETFPQDDKC VFPEEVDNGN FVHCEESGKL VLVYSCFHGY KLQGQEQVTC TQKGWDSEPP
     VCKDVNECAD LTHPPCHPSA QCKNTKGSFQ CVCTDPYVLG EDEKTCIDSG RLPRASWVSI
     ALGALLIGGL ASLTWIVICR WTHADKKATL PITERVTTQS GCRKSQGRGI SPHKAAAQDT
     GQEPASGSRV LLCE
//
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