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Reviewed, UniProtKB/Swiss-Prot Q9MYY8 (TRXR1_PIG)

Last modified June 16, 2009. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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

Names and origin

Protein namesRecommended name:
    Thioredoxin reductase 1, cytoplasmic
      Short name=TR
    EC=1.8.1.9
Alternative name(s):
    Thioredoxin reductase TR1
Gene names
Name: TXNRD1
OrganismSus scrofa (Pig)
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length499 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Catalytic activity

Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.

Cofactor

Binds 1 FAD per subunit By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Miscellaneous

The active site is a redox-active disulfide bond. The selenocysteine residue is also essential for catalytic activity By similarity.

Sequence similarities

Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversitySelenocysteine
   DomainRedox-active center
   LigandFAD
Flavoprotein
NADP
Selenium
   Molecular functionOxidoreductase
   PTMDisulfide bond
Phosphoprotein
Gene Ontology (GO)
   Biological processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionFAD binding

Inferred from electronic annotation. Source: InterPro

NADP or NADPH binding

Inferred from electronic annotation. Source: InterPro

selenium binding

Inferred from electronic annotation. Source: UniProtKB-KW

thioredoxin-disulfide reductase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 499499Thioredoxin reductase 1, cytoplasmic
PRO_0000067983

Regions

Nucleotide binding42 – 5918FAD By similarity

Sites

Active site4721Proton acceptor By similarity

Amino acid modifications

Non-standard residue4981Selenocysteine
Modified residue111Phosphotyrosine By similarity
Modified residue131Phosphotyrosine By similarity
Modified residue1311Phosphotyrosine By similarity
Modified residue4221Phosphotyrosine By similarity
Disulfide bond59 ↔ 64Redox-active By similarity
Cross-link497 ↔ 498Cysteinyl-selenocysteine (Cys-Sec) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9MYY8-1 [UniParc].

Last modified February 26, 2008. Version 3.
Checksum: CFE9C9F51998FBB4

FASTA49954,904
        10         20         30         40         50         60 
MNGAEELPEM YDYDLIIIGG GSGGLAAAKE AARFNKRVMV LDFVTPTPLG TRWGLGGTCV 

        70         80         90        100        110        120 
NVSCIPKKLM HQAALLGQAL RDSRNYGWNV EETIKHDWER MTEAVQNHIG SLNWGYRVAL 

       130        140        150        160        170        180 
REKKVTYENA YGQFVGPHRI KATNNKGKEK IYSAEKFLIA TGERPRYLGI PGDKEYCISS 

       190        200        210        220        230        240 
DDLFSLPYCP GKTLVVGASY VALECAGFLA GIGLDVTVMV RSILLRGFDQ DMANKIGEHM 

       250        260        270        280        290        300 
EEHGIKFIRQ FVPIKVEQIE AGTPGRLRVV AQSTNSEEII EGEYNTVMLA IGRDACTRKI 

       310        320        330        340        350        360 
GLETVGVKIN EKTGKIPVTD EEQTNVPYIY AIGDILEDKV ELTPVAIQAG RLLAQRLYAG 

       370        380        390        400        410        420 
STVKCDYENV PTTVFTPLEY GACGLSEEKA VEKFGEENIE VYHSYFWPLE WTIPSRDNNK 

       430        440        450        460        470        480 
CYAKIICNTK DNERVVGFHV LGPNAGEVTQ GFAAALKCGL TKKQLDSTIG IHPVCAEVFT 

       490 
TLSVTKRSGA SILQAGCUG 

« Hide

References

[1]"Cloning and sequencing of thioredoxin reductase gene from porcine reticulocyte."
Lee K.S., Xu L., Xu J.Y., Cheung P.Y.
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

AF277894 mRNA. Translation: AAF78791.1.
RefSeqNP_999319.1.
UniGeneSsc.15974

3D structure databases

HSSPHSSP built from PDB template 1ONF based on UniProtKB Q94655.
SMRQ9MYY8. Positions 11-493.
ModBaseSearch...

Genome annotation databases

GeneID397299.
KEGGssc:397299.

Phylogenomic databases

HOVERGENQ9MYY8.

Enzyme and pathway databases

BRENDA1.8.1.9. 249.

Family and domain databases

InterProIPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR000815. Hg_reductase.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD_bd.
IPR006338. Reduct_Se.
[Graphical view]
Gene3DG3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
PANTHERPTHR22912:SF23. Reduct_Se. 1 hit.
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
PR00945. HGRDTASE.
ProDomPD000139. FAD_pyr_redox. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01438. TGR. 1 hit.
PROSITEPS00076. PYRIDINE_REDOX_1. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTRXR1_PIG
AccessionPrimary (citable) accession number: Q9MYY8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: February 26, 2008
Last modified: June 16, 2009
This is version 56 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

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