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P35419

- PERT_MOUSE

UniProt

P35419 - PERT_MOUSE

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Protein

Thyroid peroxidase

Gene

Tpo

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

Iodination and coupling of the hormonogenic tyrosines in thyroglobulin to yield the thyroid hormones T3 and T4.

Catalytic activityi

2 iodide + H2O2 + 2 H+ = 2 iodine + 2 H2O.
[Thyroglobulin]-L-tyrosine + iodide + H2O2 = [thyroglobulin]-3-iodo-L-tyrosine + 2 H2O.
[Thyroglobulin]-3-iodo-L-tyrosine + iodide + H2O2 = [thyroglobulin]-3,5-diiodo-L-tyrosine + 2 H2O.
2 [thyroglobulin]-3,5-diiodo-L-tyrosine + H2O2 = [thyroglobulin]-L-thyroxine + [thyroglobulin]-aminoacrylate + 2 H2O.
[Thyroglobulin]-3-iodo-L-tyrosine + [thyroglobulin]-3,5-diiodo-L-tyrosine + H2O2 = [thyroglobulin]-3,5,3'-triiodo-L-thyronine + [thyroglobulin]-aminoacrylate + 2 H2O.

Cofactori

Protein has several cofactor binding sites:
  • Ca2+PROSITE-ProRule annotationNote: Binds 1 Ca(2+) ion per heterodimer.PROSITE-ProRule annotation
  • heme bPROSITE-ProRule annotationNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group covalently per heterodimer.PROSITE-ProRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei232 – 2321Heme (covalent; via 2 links)By similarity
Active sitei233 – 2331Proton acceptorPROSITE-ProRule annotation
Metal bindingi234 – 2341CalciumPROSITE-ProRule annotation
Metal bindingi313 – 3131CalciumPROSITE-ProRule annotation
Metal bindingi315 – 3151Calcium; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi317 – 3171CalciumPROSITE-ProRule annotation
Metal bindingi319 – 3191CalciumPROSITE-ProRule annotation
Sitei384 – 3841Transition state stabilizerPROSITE-ProRule annotation
Binding sitei387 – 3871Heme (covalent; via 2 links)By similarity
Metal bindingi482 – 4821Iron (heme axial ligand)PROSITE-ProRule annotation

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. heme binding Source: InterPro
  3. iodide peroxidase activity Source: UniProtKB-EC

GO - Biological processi

  1. embryonic hemopoiesis Source: Ensembl
  2. hormone biosynthetic process Source: UniProtKB-KW
  3. hydrogen peroxide catabolic process Source: UniProtKB-KW
  4. thyroid hormone generation Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide, Thyroid hormones biosynthesis

Keywords - Ligandi

Calcium, Heme, Iron, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_219697. Thyroxine biosynthesis.
UniPathwayiUPA00194.

Protein family/group databases

PeroxiBasei3345. MmTPO.

Names & Taxonomyi

Protein namesi
Recommended name:
Thyroid peroxidase (EC:1.11.1.8)
Short name:
TPO
Gene namesi
Name:Tpo
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 12

Organism-specific databases

MGIiMGI:98813. Tpo.

Subcellular locationi

Membrane By similarity; Single-pass type I membrane protein By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini32 – 834803ExtracellularSequence AnalysisAdd
BLAST
Transmembranei835 – 85925HelicalSequence AnalysisAdd
BLAST
Topological domaini860 – 91455CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. extracellular space Source: Ensembl
  2. integral component of membrane Source: UniProtKB-KW
  3. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131Sequence AnalysisAdd
BLAST
Chaini32 – 914883Thyroid peroxidasePRO_0000023663Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi123 – 1231N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi136 ↔ 152By similarity
Disulfide bondi253 ↔ 263By similarity
Disulfide bondi257 ↔ 278By similarity
Glycosylationi271 – 2711N-linked (GlcNAc...)Sequence Analysis
Glycosylationi299 – 2991N-linked (GlcNAc...)Sequence Analysis
Glycosylationi334 – 3341N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi586 ↔ 643By similarity
Glycosylationi603 – 6031N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi684 ↔ 709By similarity
Disulfide bondi730 ↔ 770By similarity
Disulfide bondi756 ↔ 782By similarity
Disulfide bondi788 ↔ 802By similarity
Disulfide bondi796 ↔ 811By similarity
Disulfide bondi813 ↔ 826By similarity

Post-translational modificationi

Heme is covalently bound through a H2O(2)-dependent autocatalytic process. Heme insertion is important for the delivery of protein at the cell surface (By similarity).By similarity
Cleaved in its N-terminal part.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiP35419.

PTM databases

PhosphoSiteiP35419.

Expressioni

Gene expression databases

BgeeiP35419.
CleanExiMM_TPO.
ExpressionAtlasiP35419. baseline and differential.
GenevestigatoriP35419.

Interactioni

Subunit structurei

Interacts with DUOX1, DUOX2 and CYBA.By similarity

Structurei

3D structure databases

ProteinModelPortaliP35419.
SMRiP35419. Positions 143-722, 726-831.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini728 – 78356SushiPROSITE-ProRule annotationAdd
BLAST
Domaini784 – 82744EGF-like; calcium-bindingPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peroxidase family. XPO subfamily.PROSITE-ProRule annotation
Contains 1 EGF-like domain.PROSITE-ProRule annotation
Contains 1 Sushi (CCP/SCR) domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Signal, Sushi, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG262194.
GeneTreeiENSGT00550000074325.
HOGENOMiHOG000016084.
HOVERGENiHBG000071.
InParanoidiP35419.
KOiK00431.
OMAiIMETSIQ.
OrthoDBiEOG7D2FD6.
PhylomeDBiP35419.
TreeFamiTF314316.

Family and domain databases

Gene3Di1.10.640.10. 2 hits.
InterProiIPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR010255. Haem_peroxidase.
IPR019791. Haem_peroxidase_animal.
IPR000436. Sushi_SCR_CCP.
IPR029589. TPO.
[Graphical view]
PANTHERiPTHR11475:SF60. PTHR11475:SF60. 1 hit.
PfamiPF03098. An_peroxidase. 1 hit.
PF07645. EGF_CA. 1 hit.
PF00084. Sushi. 1 hit.
[Graphical view]
PRINTSiPR00457. ANPEROXIDASE.
SMARTiSM00032. CCP. 1 hit.
SM00179. EGF_CA. 1 hit.
[Graphical view]
SUPFAMiSSF48113. SSF48113. 1 hit.
SSF57535. SSF57535. 1 hit.
PROSITEiPS00010. ASX_HYDROXYL. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
PS01187. EGF_CA. 1 hit.
PS00435. PEROXIDASE_1. 1 hit.
PS50292. PEROXIDASE_3. 1 hit.
PS50923. SUSHI. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P35419-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRTLGAMAIM LVVMGTVIFL SFILRSRDIL CGKTMKSHVI SAVETSQLMV
60 70 80 90 100
DHAVYNTMKR NLKKREVLSP AQLLSFFKLP ESTSGAISRA AEIMETSIQV
110 120 130 140 150
MKREQSQFST DALSADILGT IANLSGCLPF MLPPRCPDTC LANKYRPITG
160 170 180 190 200
ACNNRDHPRW GASNTALARW LPPVYEDGFS QPKGWNPNFL YHGFPLPPVR
210 220 230 240 250
EVTRHLIQVS NEAVTEDDQY SDFLPVWGQY IDHDIALTPQ STSTAAFWGG
260 270 280 290 300
VDCQLTCENQ NPCFPIQLPS NSSGTTACLP FYRSSAACGT GDQGALFGNL
310 320 330 340 350
SAANPRQQMN GLTSFLDAST VYGSSPGVEK QLRNWSSSAG LLRVNTLHLD
360 370 380 390 400
AGRAYLPFAT AACAPEPGTP RTNRTPCFLA GDGRASEVPA LAAVHTLWLR
410 420 430 440 450
EHNRLASAFK AINKHWSANT AYQEARKVVG ALHQIITMRD YIPKILGPDA
460 470 480 490 500
FRQYVGPYEG YNPTVNPTVS NIFSTAAFRF GHATVHPLVR RLNTDFQEHT
510 520 530 540 550
ELPRLQLRDV FFRPWRLIQE GGLDPIVRGL LARAAKLQVQ GQLMNEELTE
560 570 580 590 600
RLFVLSNVGT LDLASLNLQR GRDHGLPDYN EWREFCGLSR LETPAELNKA
610 620 630 640 650
IANRSMVNKI MDLYKHADNI DVWLGGLAEK FLPGARTGPL FACIIGKQMK
660 670 680 690 700
ALRDGDRFWW ENTNVFTDAQ RQELEKHSLP RVICDNTGLT RVPVDAFRIG
710 720 730 740 750
KFPQDFESCE DIPSMDLELW RETFPQDDKC VFPEEVDNGN FVHCEESGKL
760 770 780 790 800
VLVYSCFHGY KLQGQEQVTC TQKGWDSEPP VCKDVNECAD LTHPPCHPSA
810 820 830 840 850
QCKNTKGSFQ CVCTDPYVLG EDEKTCIDSG RLPRASWVSI ALGALLIGGL
860 870 880 890 900
ASLTWIVICR WTHADKKATL PITERVTTQS GCRKSQGRGI SPHKAAAQDT
910
GQEPASGSRV LLCE
Length:914
Mass (Da):101,342
Last modified:June 1, 1994 - v1
Checksum:i595E9A0B71F3DD01
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti614 – 6141Y → H in BAC33171. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60703 mRNA. Translation: CAA43114.1.
AK047843 mRNA. Translation: BAC33171.1.
CCDSiCCDS25857.1.
PIRiJN0550.
RefSeqiNP_033443.1. NM_009417.2.
UniGeneiMm.4991.

Genome annotation databases

EnsembliENSMUST00000021005; ENSMUSP00000021005; ENSMUSG00000020673.
GeneIDi22018.
KEGGimmu:22018.
UCSCiuc007ngo.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60703 mRNA. Translation: CAA43114.1 .
AK047843 mRNA. Translation: BAC33171.1 .
CCDSi CCDS25857.1.
PIRi JN0550.
RefSeqi NP_033443.1. NM_009417.2.
UniGenei Mm.4991.

3D structure databases

ProteinModelPortali P35419.
SMRi P35419. Positions 143-722, 726-831.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

PeroxiBasei 3345. MmTPO.

PTM databases

PhosphoSitei P35419.

Proteomic databases

PRIDEi P35419.

Protocols and materials databases

DNASUi 22018.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000021005 ; ENSMUSP00000021005 ; ENSMUSG00000020673 .
GeneIDi 22018.
KEGGi mmu:22018.
UCSCi uc007ngo.1. mouse.

Organism-specific databases

CTDi 7173.
MGIi MGI:98813. Tpo.

Phylogenomic databases

eggNOGi NOG262194.
GeneTreei ENSGT00550000074325.
HOGENOMi HOG000016084.
HOVERGENi HBG000071.
InParanoidi P35419.
KOi K00431.
OMAi IMETSIQ.
OrthoDBi EOG7D2FD6.
PhylomeDBi P35419.
TreeFami TF314316.

Enzyme and pathway databases

UniPathwayi UPA00194 .
Reactomei REACT_219697. Thyroxine biosynthesis.

Miscellaneous databases

NextBioi 301744.
PROi P35419.
SOURCEi Search...

Gene expression databases

Bgeei P35419.
CleanExi MM_TPO.
ExpressionAtlasi P35419. baseline and differential.
Genevestigatori P35419.

Family and domain databases

Gene3Di 1.10.640.10. 2 hits.
InterProi IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR010255. Haem_peroxidase.
IPR019791. Haem_peroxidase_animal.
IPR000436. Sushi_SCR_CCP.
IPR029589. TPO.
[Graphical view ]
PANTHERi PTHR11475:SF60. PTHR11475:SF60. 1 hit.
Pfami PF03098. An_peroxidase. 1 hit.
PF07645. EGF_CA. 1 hit.
PF00084. Sushi. 1 hit.
[Graphical view ]
PRINTSi PR00457. ANPEROXIDASE.
SMARTi SM00032. CCP. 1 hit.
SM00179. EGF_CA. 1 hit.
[Graphical view ]
SUPFAMi SSF48113. SSF48113. 1 hit.
SSF57535. SSF57535. 1 hit.
PROSITEi PS00010. ASX_HYDROXYL. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
PS01187. EGF_CA. 1 hit.
PS00435. PEROXIDASE_1. 1 hit.
PS50292. PEROXIDASE_3. 1 hit.
PS50923. SUSHI. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the cDNA encoding mouse thyroid peroxidase."
    Kotani T., Umeki K., Yamamoto I., Takeuchi M., Takechi S., Nakayama T., Ohtaki S.
    Gene 123:289-290(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6.
    Tissue: Thyroid.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Head.

Entry informationi

Entry nameiPERT_MOUSE
AccessioniPrimary (citable) accession number: P35419
Secondary accession number(s): Q8C8B1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: November 26, 2014
This is version 149 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3