Thyroid peroxidase precursor - Sus scrofa (Pig)

Contribute

Send feedback

Read comments (1) or add your own

Reviewed, UniProtKB/Swiss-Prot P09933 (PERT_PIG)

Last modified June 16, 2009. Version 101. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein names

Recommended name:
    Thyroid peroxidase
      Short name=TPO
    EC=1.11.1.8

Gene names

Name:

TPO

Organism

Sus scrofa (Pig)

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Hide | Top

Protein attributes

Sequence length	926 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

Hide | Top

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.
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. N-glycosylated; contains mannose and N-acetylglucosamine. Ref.3
Sequence similarities	Belongs to the peroxidase family. XPO subfamily. Contains 1 EGF-like domain. Contains 1 Sushi (CCP/SCR) domain.

Hide | Top

Ontologies

Keywords
Biological process	Hydrogen peroxide Thyroid hormones biosynthesis
Cellular component	Membrane
Domain	EGF-like domain Signal Sushi Transmembrane
Ligand	Calcium Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
PTM	Disulfide bond Glycoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	hormone biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW heme binding Inferred from electronic annotation. Source: InterPro iodide peroxidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 14

Potential

Chain

15 – 926

912

Thyroid peroxidase

PRO_0000023664

Regions

Topological domain

19 – 844

826

Extracellular Potential

Transmembrane

845 – 869

Potential

Topological domain

870 – 926

Cytoplasmic Potential

Domain

738 – 793

Sushi

Domain

794 – 837

EGF-like; calcium-binding Potential

Sites

Active site

239

Proton acceptor By similarity

Metal binding

240

Calcium By similarity

Metal binding

321

Calcium By similarity

Metal binding

323

Calcium; via carbonyl oxygen By similarity

Metal binding

325

Calcium By similarity

Metal binding

327

Calcium By similarity

Metal binding

493

Iron (heme axial ligand) By similarity

Binding site

238

Heme (covalent; via 2 links) By similarity

Binding site

398

Heme (covalent; via 2 links) By similarity

Site

395

Transition state stabilizer By similarity

Amino acid modifications

Glycosylation

129

N-linked (GlcNAc...) Ref.3

Glycosylation

277

N-linked (GlcNAc...) Ref.3

Glycosylation

307

N-linked (GlcNAc...) Ref.3

Glycosylation

342

N-linked (GlcNAc...) Ref.3

Disulfide bond

142 ↔ 158

By similarity

Disulfide bond

259 ↔ 269

By similarity

Disulfide bond

263 ↔ 286

By similarity

Disulfide bond

596 ↔ 653

By similarity

Disulfide bond

694 ↔ 719

By similarity

Disulfide bond

740 ↔ 780

By similarity

Disulfide bond

766 ↔ 792

By similarity

Disulfide bond

798 ↔ 812

By similarity

Disulfide bond

806 ↔ 821

By similarity

Disulfide bond

823 ↔ 836

By similarity

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

P09933-1 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 8549FF6F0F742C5E
Show »

FASTA

926

100,443

        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

« Hide

Hide | Top

References

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

Hide | Top

Cross-references

Sequence databases
	X04645 mRNA. Translation: CAA28306.1.
PIR	OPPGIT. A27416.
UniGene	Ssc.99
3D structure databases
HSSP	HSSP built from PDB template 1D5L based on UniProtKB P05164.
ModBase	Search...
Protein family/group databases
PeroxiBase	3329. SscTPO.
Phylogenomic databases
HOVERGEN	P09933.
Enzyme and pathway databases
BRENDA	1.11.1.8. 249.
Family and domain databases
InterPro	IPR016060. Complement_control_module. IPR006209. EGF. IPR006210. EGF-like. IPR013032. EGF-like_reg_CS. IPR000742. EGF_3. IPR018097. EGF_Ca_bd_CS. IPR002007. Haem_peroxidase_animal. IPR019791. Haem_peroxidase_animal_sg. IPR019794. Peroxidases_AS. IPR019793. Peroxidases_heam-ligand_BS. IPR000436. Sushi_SCR_CCP. [Graphical view]
Gene3D	G3DSA:2.10.70.10. Complement_control_module. 1 hit. G3DSA:1.10.640.10. Haem_peroxidase_animal. 1 hit.
Pfam	PF03098. An_peroxidase. 1 hit. PF00008. EGF. 1 hit. PF00084. Sushi. 1 hit. [Graphical view]
PRINTS	PR00457. ANPEROXIDASE.
SMART	SM00032. CCP. 1 hit. SM00181. EGF. 1 hit. [Graphical view]
PROSITE	PS00022. EGF_1. False negative. PS01186. EGF_2. False negative. PS50026. EGF_3. 1 hit. PS01187. EGF_CA. False negative. PS00435. PEROXIDASE_1. 1 hit. PS00436. PEROXIDASE_2. False negative. PS50292. PEROXIDASE_3. 1 hit. PS50923. SUSHI. 1 hit. [Graphical view]
ProtoNet	Search...

Hide | Top

Entry information

Entry name

PERT_PIG

Accession

Primary (citable) accession number: P09933

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	June 16, 2009
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Hide | Top

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents