ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P35419


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name PERT_MOUSE
Primary accession number P35419
Secondary accession number Q8C8B1
Integrated into Swiss-Prot on June 1, 1994
Sequence was last modified on June 1, 1994 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 91)
Name and origin of the protein
Protein name Thyroid peroxidase [Precursor]
Synonyms TPO
EC 1.11.1.8
Gene name
Name: Tpo
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6;
TISSUE=Thyroid;
DOI=10.1016/0378-1119(93)90141-O; PubMed=7916704 [NCBI, ExPASy, EBI, Israel, Japan]
Kotani T., Umeki K., Yamamoto I., Takeuchi M., Takechi S., Nakayama T., Ohtaki S.;
"Nucleotide sequence of the cDNA encoding mouse thyroid peroxidase.";
Gene 123:289-290(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Head;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X60703; CAA43114.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK047843; BAC33171.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JN0550; JN0550.
RefSeq NP_033443.1; -.
UniGene Mm.4991
3D structure databases
HSSP P05164; 1D5L. [HSSP ENTRY / PDB]
ModBase P35419.
Protein family/group databases
PeroxiBase 3345; MmTPO.
Organism-specific databases
MGI MGI:98813; Tpo.
Gene expression databases
ArrayExpress P35419; -.
CleanEx MM_TPO; -.
GermOnline ENSMUSG00000020673; Mus musculus.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from MGI).
QuickGo view.
Family and domain databases
InterPro IPR016060; Complement_control_module.
IPR000152; EGF-type_Asp/Asn_hydroxyl_CS.
IPR000742; EGF_3.
IPR001881; EGF_Ca_bd.
IPR013091; EGF_Ca_bd_2.
IPR013032; EGF_like_reg_CS.
IPR002007; Haem_peroxidase_animal.
IPR002016; Haem_peroxidase_pln/fun/bac.
IPR000436; Sushi_SCR_CCP.
Graphical view of domain structure.
Gene3D G3DSA:2.10.70.10; Complement_control_module; 1.
G3DSA:1.10.640.10; Haem_peroxidase_animal; 1.
Pfam PF03098; An_peroxidase; 1.
PF07645; EGF_CA; 1.
PF00084; Sushi; 1.
Pfam graphical view of domain structure.
PRINTS PR00457; ANPEROXIDASE.
SMART SM00032; CCP; 1.
SM00179; EGF_CA; 1.
SMART graphical view of domain structure.
PROSITE PS00010; ASX_HYDROXYL; 1.
PS00022; EGF_1; FALSE_NEG.
PS01186; EGF_2; 1.
PS50026; EGF_3; 1.
PS01187; EGF_CA; 1.
PS00435; PEROXIDASE_1; 1.
PS50292; PEROXIDASE_3; 1.
PS50923; SUSHI; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P35419.
Genome annotation databases
Ensembl ENSMUSG00000020673; Mus musculus. [Contig view]
GeneID 22018; -.
KEGG mmu:22018; -.
Phylogenomic databases
HOGENOM P35419; -.
HOVERGEN P35419; -.
Other
SOURCE Tpo; Mus musculus.
ProtoNet P35419.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Calcium; EGF-like domain; Glycoprotein; Heme; Hydrogen peroxide; Iron; Membrane; Metal-binding; Oxidoreductase; Peroxidase; Signal; Sushi; Thyroid hormones biosynthesis; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    31  31     Potential. 
CHAIN   32   914  883     Thyroid peroxidase. PRO_0000023663
TOPO_DOM   32   834  803     Extracellular (Potential). 
TRANSMEM   835   859  25     Potential. 
TOPO_DOM   860   914  55     Cytoplasmic (Potential). 
DOMAIN   728   783  56     Sushi. 
DOMAIN   784   827  44     EGF-like; calcium-binding (Potential). 
ACT_SITE   233   233        Proton acceptor (By similarity). 
METAL   234   234        Calcium (By similarity). 
METAL   313   313        Calcium (By similarity). 
METAL   315   315        Calcium; via carbonyl oxygen (By similarity). 
METAL   317   317        Calcium (By similarity). 
METAL   319   319        Calcium (By similarity). 
METAL   482   482        Iron (heme axial ligand) (By similarity). 
BINDING   232   232        Heme (covalent; via 2 links) (By similarity). 
BINDING   387   387        Heme (covalent; via 2 links) (By similarity). 
SITE   384   384  1     Transition state stabilizer (By similarity). 
CARBOHYD   123   123        N-linked (GlcNAc...) (Potential). 
CARBOHYD   271   271        N-linked (GlcNAc...) (Potential). 
CARBOHYD   299   299        N-linked (GlcNAc...) (Potential). 
CARBOHYD   334   334        N-linked (GlcNAc...) (Potential). 
CARBOHYD   603   603        N-linked (GlcNAc...) (Potential). 
DISULFID   136   152        By similarity. 
DISULFID   253   263        By similarity. 
DISULFID   257   278        By similarity. 
DISULFID   586   643        By similarity. 
DISULFID   684   709        By similarity. 
DISULFID   730   770        By similarity. 
DISULFID   756   782        By similarity. 
DISULFID   788   802        By similarity. 
DISULFID   796   811        By similarity. 
DISULFID   813   826        By similarity. 
CONFLICT   614   614        Y -> H (in Ref. 2; BAC33171). 
Sequence information
Length: 914 AA [This is the length of the unprocessed precursor] Molecular weight: 101342 Da [This is the MW of the unprocessed precursor] CRC64: 595E9A0B71F3DD01 [This is a checksum on the sequence]
        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 

P35419 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!