Skip Header

Contribute Send feedback
Read comments (?) or add your own

P35419 (PERT_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thyroid peroxidase
Short name=TPO
EC=1.11.1.8
Gene names
Name:Tpo
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length914 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

Catalytic activity

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.

Cofactor

Binds 1 calcium ion per heterodimer By similarity.

Binds 1 heme B (iron-protoporphyrin IX) group covalently per heterodimer By similarity.

Pathway

Hormone biosynthesis; thyroid hormone biosynthesis.

Subunit structure

Interacts with DUOX1, DUOX2 and CYBA By similarity.

Subcellular location

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

Post-translational modification

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.

Cleaved in its N-terminal part By similarity.

Sequence similarities

Belongs to the peroxidase family. XPO subfamily.

Contains 1 EGF-like domain.

Contains 1 Sushi (CCP/SCR) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Potential
Chain32 – 914883Thyroid peroxidase
PRO_0000023663

Regions

Topological domain32 – 834803Extracellular Potential
Transmembrane835 – 85925Helical; Potential
Topological domain860 – 91455Cytoplasmic Potential
Domain728 – 78356Sushi
Domain784 – 82744EGF-like; calcium-binding Potential

Sites

Active site2331Proton acceptor By similarity
Metal binding2341Calcium By similarity
Metal binding3131Calcium By similarity
Metal binding3151Calcium; via carbonyl oxygen By similarity
Metal binding3171Calcium By similarity
Metal binding3191Calcium By similarity
Metal binding4821Iron (heme axial ligand) By similarity
Binding site2321Heme (covalent; via 2 links) By similarity
Binding site3871Heme (covalent; via 2 links) By similarity
Site3841Transition state stabilizer By similarity

Amino acid modifications

Glycosylation1231N-linked (GlcNAc...) Potential
Glycosylation2711N-linked (GlcNAc...) Potential
Glycosylation2991N-linked (GlcNAc...) Potential
Glycosylation3341N-linked (GlcNAc...) Potential
Glycosylation6031N-linked (GlcNAc...) Potential
Disulfide bond136 ↔ 152 By similarity
Disulfide bond253 ↔ 263 By similarity
Disulfide bond257 ↔ 278 By similarity
Disulfide bond586 ↔ 643 By similarity
Disulfide bond684 ↔ 709 By similarity
Disulfide bond730 ↔ 770 By similarity
Disulfide bond756 ↔ 782 By similarity
Disulfide bond788 ↔ 802 By similarity
Disulfide bond796 ↔ 811 By similarity
Disulfide bond813 ↔ 826 By similarity

Experimental info

Sequence conflict6141Y → H in BAC33171. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P35419 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 595E9A0B71F3DD01

FASTA914101,342
        10         20         30         40         50         60 
MRTLGAMAIM LVVMGTVIFL SFILRSRDIL CGKTMKSHVI SAVETSQLMV DHAVYNTMKR 

        70         80         90        100        110        120 
NLKKREVLSP AQLLSFFKLP ESTSGAISRA AEIMETSIQV MKREQSQFST DALSADILGT 

       130        140        150        160        170        180 
IANLSGCLPF MLPPRCPDTC LANKYRPITG ACNNRDHPRW GASNTALARW LPPVYEDGFS 

       190        200        210        220        230        240 
QPKGWNPNFL YHGFPLPPVR EVTRHLIQVS NEAVTEDDQY SDFLPVWGQY IDHDIALTPQ 

       250        260        270        280        290        300 
STSTAAFWGG VDCQLTCENQ NPCFPIQLPS NSSGTTACLP FYRSSAACGT GDQGALFGNL 

       310        320        330        340        350        360 
SAANPRQQMN GLTSFLDAST VYGSSPGVEK QLRNWSSSAG LLRVNTLHLD AGRAYLPFAT 

       370        380        390        400        410        420 
AACAPEPGTP RTNRTPCFLA GDGRASEVPA LAAVHTLWLR EHNRLASAFK AINKHWSANT 

       430        440        450        460        470        480 
AYQEARKVVG ALHQIITMRD YIPKILGPDA FRQYVGPYEG YNPTVNPTVS NIFSTAAFRF 

       490        500        510        520        530        540 
GHATVHPLVR RLNTDFQEHT ELPRLQLRDV FFRPWRLIQE GGLDPIVRGL LARAAKLQVQ 

       550        560        570        580        590        600 
GQLMNEELTE RLFVLSNVGT LDLASLNLQR GRDHGLPDYN EWREFCGLSR LETPAELNKA 

       610        620        630        640        650        660 
IANRSMVNKI MDLYKHADNI DVWLGGLAEK FLPGARTGPL FACIIGKQMK ALRDGDRFWW 

       670        680        690        700        710        720 
ENTNVFTDAQ RQELEKHSLP RVICDNTGLT RVPVDAFRIG KFPQDFESCE DIPSMDLELW 

       730        740        750        760        770        780 
RETFPQDDKC VFPEEVDNGN FVHCEESGKL VLVYSCFHGY KLQGQEQVTC TQKGWDSEPP 

       790        800        810        820        830        840 
VCKDVNECAD LTHPPCHPSA QCKNTKGSFQ CVCTDPYVLG EDEKTCIDSG RLPRASWVSI 

       850        860        870        880        890        900 
ALGALLIGGL ASLTWIVICR WTHADKKATL PITERVTTQS GCRKSQGRGI SPHKAAAQDT 

       910 
GQEPASGSRV LLCE

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X60703 mRNA. Translation: CAA43114.1.
AK047843 mRNA. Translation: BAC33171.1.
IPIIPI00118312.
PIRJN0550.
RefSeqNP_033443.1. NM_009417.2.
UniGeneMm.4991.

3D structure databases

ProteinModelPortalP35419.
SMRP35419. Positions 145-722, 724-831.
ModBaseSearch...

Protein family/group databases

PeroxiBase3345. MmTPO.

PTM databases

PhosphoSiteP35419.

Proteomic databases

PRIDEP35419.

Protocols and materials databases

DNASU22018.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021005; ENSMUSP00000021005; ENSMUSG00000020673.
GeneID22018.
KEGGmmu:22018.
UCSCuc007ngo.1. mouse.

Organism-specific databases

CTD7173.
MGIMGI:98813. Tpo.

Phylogenomic databases

eggNOGNOG262194.
GeneTreeENSGT00550000074325.
HOGENOMHOG000016084.
HOVERGENHBG000071.
InParanoidP35419.
KOK00431.
OMAIMETSIQ.
OrthoDBEOG415GD3.

Enzyme and pathway databases

UniPathwayUPA00194.

Gene expression databases

ArrayExpressP35419.
BgeeP35419.
CleanExMM_TPO.
GenevestigatorP35419.
GermOnlineENSMUSG00000020673. Mus musculus.

Family and domain databases

Gene3D1.10.640.10. 2 hits.
InterProIPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR010255. Haem_peroxidase.
IPR002007. Haem_peroxidase_animal.
IPR019791. Haem_peroxidase_animal_subgr.
IPR000436. Sushi_SCR_CCP.
[Graphical view]
PfamPF03098. An_peroxidase. 1 hit.
PF07645. EGF_CA. 1 hit.
PF00084. Sushi. 1 hit.
[Graphical view]
PRINTSPR00457. ANPEROXIDASE.
SMARTSM00032. CCP. 1 hit.
SM00179. EGF_CA. 1 hit.
[Graphical view]
SUPFAMSSF57535. Complement_control_module. 1 hit.
SSF48113. Peroxidase_super. 1 hit.
PROSITEPS00010. ASX_HYDROXYL. 1 hit.
PS00022. EGF_1. False negative.
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]
ProtoNetSearch...

Other

NextBio301744.
SOURCESearch...

Entry information

Entry namePERT_MOUSE
AccessionPrimary (citable) accession number: P35419
Secondary accession number(s): Q8C8B1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: May 1, 2013
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents