[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=3654642 [NCBI, ExPASy, EBI, Israel, Japan] Magnusson R.P., Gestautas J., Taurog A., Rapoport B.; "Molecular cloning of the structural gene for porcine thyroid peroxidase."; J. Biol. Chem. 262:13885-13888(1987).
[2]	NUCLEOTIDE SEQUENCE [MRNA] OF 595-926. DOI=10.1016/0014-5793(86)81055-9; PubMed=3780975 [NCBI, ExPASy, EBI, Israel, Japan] Magnusson R.P., Gestautas J., Seto P., Taurog A., Rapoport B.; "Isolation and characterization of a cDNA clone for porcine thyroid peroxidase."; FEBS Lett. 208:391-396(1986).
[3]	PROTEIN SEQUENCE OF 110-115; 267-274; 301-308 AND 340-351, AND GLYCOSYLATION AT ASN-129; ASN-277; ASN-307 AND ASN-342. DOI=10.1016/0003-9861(92)90679-Q; PubMed=1497352 [NCBI, ExPASy, EBI, Israel, Japan] Rawitch A.B., Pollock G., Yang S.-X., Taurog A.; "Thyroid peroxidase glycosylation: the location and nature of the N-linked oligosaccharide units in porcine thyroid peroxidase."; Arch. Biochem. Biophys. 297:321-327(1992).

Comments

FUNCTION: Iodination and coupling of the hormonogenic tyrosines in thyroglobulin to yield the thyroid hormones T(3) and T(4).
CATALYTIC ACTIVITY: 2 iodide + H₂O₂ + 2 H⁺ = 2 iodine + 2 H₂O.
COFACTOR: Binds 1 calcium ion per heterodimer (By similarity).
COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group covalently per heterodimer (By similarity).
PATHWAY: Hormone biosynthesis; thyroid hormone biosynthesis .
SUBUNIT: Interacts with DUOX1, DUOX2 and CYBA (By similarity).
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein (By similarity).
PTM: Heme is covalently bound through a H(2)O(2)-dependent autocatalytic process. Heme insertion is important for the delivery of protein at the cell surface (By similarity).
PTM: Cleaved in its N-terminal part (By similarity).
PTM: N-glycosylated; contains mannose and N-acetylglucosamine.
SIMILARITY: Belongs to the peroxidase family. XPO subfamily.
SIMILARITY: Contains 1 EGF-like domain.
SIMILARITY: Contains 1 Sushi (CCP/SCR) domain.

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

X04645; CAA28306.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A27416; OPPGIT.

UniGene

Ssc.99

3D structure databases

HSSP

P05164; 1D5L. [HSSP ENTRY / PDB]

ModBase

P09933.

Protein family/group databases

PeroxiBase

3329; SscTPO.

Family and domain databases

InterPro

IPR016060; Complement_control_module.
IPR006210; EGF.
IPR000742; EGF_3.
IPR001881; EGF_Ca_bd.
IPR006209; EGF_like.
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.
PF00008; EGF; 1.
PF00084; Sushi; 1.
Pfam graphical view of domain structure.

PRINTS

PR00457; ANPEROXIDASE.

SMART

SM00032; CCP; 1.
SM00181; EGF; 1.
SMART graphical view of domain structure.

PROSITE

PS00022; EGF_1; FALSE_NEG.
PS01186; EGF_2; FALSE_NEG.
PS50026; EGF_3; 1.
PS01187; EGF_CA; FALSE_NEG.
PS00435; PEROXIDASE_1; 1.
PS00436; PEROXIDASE_2; FALSE_NEG.
PS50292; PEROXIDASE_3; 1.
PS50923; SUSHI; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

P09933.

Phylogenomic databases

HOVERGEN

P09933; -.

Other

ProtoNet

P09933.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Calcium; Direct protein sequencing; EGF-like domain; Glycoprotein; Heme; Hydrogen peroxide; Iron; Membrane; Metal-binding; Oxidoreductase; Peroxidase; Signal; Sushi; Thyroid hormones biosynthesis; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 14`	`14`	`Potential.`
`CHAIN`	`15 926`	`912`	`Thyroid peroxidase.`	`PRO_0000023664`
`TOPO_DOM`	`19 844`	`826`	`Extracellular (Potential).`
`TRANSMEM`	`845 869`	`25`	`Potential.`
`TOPO_DOM`	`870 926`	`57`	`Cytoplasmic (Potential).`
`DOMAIN`	`738 793`	`56`	`Sushi.`
`DOMAIN`	`794 837`	`44`	`EGF-like; calcium-binding (Potential).`
`ACT_SITE`	`239 239`		`Proton acceptor (By similarity).`
`METAL`	`240 240`		`Calcium (By similarity).`
`METAL`	`321 321`		`Calcium (By similarity).`
`METAL`	`323 323`		`Calcium; via carbonyl oxygen (By similarity).`
`METAL`	`325 325`		`Calcium (By similarity).`
`METAL`	`327 327`		`Calcium (By similarity).`
`METAL`	`493 493`		`Iron (heme axial ligand) (By similarity).`
`BINDING`	`238 238`		`Heme (covalent; via 2 links) (By similarity).`
`BINDING`	`398 398`		`Heme (covalent; via 2 links) (By similarity).`
`SITE`	`395 395`	`1`	`Transition state stabilizer (By similarity).`
`CARBOHYD`	`129 129`		`N-linked (GlcNAc...).`
`CARBOHYD`	`277 277`		`N-linked (GlcNAc...).`
`CARBOHYD`	`307 307`		`N-linked (GlcNAc...).`
`CARBOHYD`	`342 342`		`N-linked (GlcNAc...).`
`DISULFID`	`142 158`		`By similarity.`
`DISULFID`	`259 269`		`By similarity.`
`DISULFID`	`263 286`		`By similarity.`
`DISULFID`	`596 653`		`By similarity.`
`DISULFID`	`694 719`		`By similarity.`
`DISULFID`	`740 780`		`By similarity.`
`DISULFID`	`766 792`		`By similarity.`
`DISULFID`	`798 812`		`By similarity.`
`DISULFID`	`806 821`		`By similarity.`
`DISULFID`	`823 836`		`By similarity.`

Sequence information

Length: 926 AA [This is the length of the unprocessed precursor]

Molecular weight: 100443 Da [This is the MW of the unprocessed precursor]

CRC64: 8549FF6F0F742C5E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGARAVLGVT LAVACAGAFF ASILRRKDLL GGDTEASGVA GLVEASRLLV DEAIHTTMRR 

        70         80         90        100        110        120 
NLRKRGIFSP SQLLSFSKLP EPTSRTASRA AEIMETAVQE VKRRVCRRRD TDQLPTDVLS 

       130        140        150        160        170        180 
EELLSTIANL SGCLPHMLPP SCPHTCLANK YRLITGACNN RDHPRWGASN TALARWLPPA 

       190        200        210        220        230        240 
YEDGVTEPRG WNPHFLYNGL PLPPVREVTR QVIHVSNEAV TEDGQYSDLL MAWGQYIDHD 

       250        260        270        280        290        300 
IAFTPQSTSK AAFAGGADCQ LTCENRSPCF PIQLPTNASG AAGATCLPFY RSSAACGSGR 

       310        320        330        340        350        360 
QGALVGNLSW AAPRQQMNGL TSFLDASTVY GSSPAQEQRL RNWTSAEGLL RVNTRHRDAG 

       370        380        390        400        410        420 
RAFLPFAPPP APPACAPEPG TPAARAPCFL AGDSRASEVP GLTALHTLWL REHNRLAAAF 

       430        440        450        460        470        480 
KALNAHWSAD TVYQEARKVV GALHQIVTLR DYVPKILGAE AFGQHVGPYQ GYDPAVDPTV 

       490        500        510        520        530        540 
SNVFSTAAFR FGHATIHPLV RRLDARFQEH PGSHLPLRAA FFQPWRLLRE GGVDPVLRGL 

       550        560        570        580        590        600 
LARPAKLQVQ DQLMNEELTE RLFVLSNSGT LDLASINLQR GRDHGLPGYN EWREFCGLSR 

       610        620        630        640        650        660 
LETWADLSAA TANGRVADRI LGLYQHPDNI DVWLGGLAES FLPGARTGPL FACIIGKQMR 

       670        680        690        700        710        720 
ALRDGDRFWW ENPGVFTEAQ RRELSRHSMS RVICDNSGLS HVPLDAFRVG QWPQEFEPCA 

       730        740        750        760        770        780 
SIQGMDLGAW REAPPSGDAC GFPDPVEDGG FLLCEERGQR VLVFSCRHGF RLRGPAQITC 

       790        800        810        820        830        840 
TPRGWDSPPP LCKDINECED ETDPPCHASA RCKNTKGGVL CECSDPLVLG EDGRTCVDAG 

       850        860        870        880        890        900 
RLPRASVVSI ALGAVLVCGL AGLAWTVVCR WTHADARPLL PVGEGEGDGK SPSLPLPGCG 

       910        920 
NRRDVGAAPA LEVEQDLSCG SRGLCE

P09933 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 submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools