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O62768 (TRXR1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 104. Feed History...

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

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
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length499 AA.
Sequence statusComplete.
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
   Molecular functionOxidoreductase
   PTMAcetylation
Disulfide bond
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionNADP binding

Inferred from electronic annotation. Source: InterPro

flavin adenine dinucleotide binding

Inferred from electronic annotation. Source: InterPro

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_0000067981

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 residue2551N6-acetyllysine 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
O62768 [UniParc].

Last modified February 26, 2008. Version 3.
Checksum: B0F15494D1795AB3

FASTA49954,770
        10         20         30         40         50         60 
MNGSKDLPEP YDYDLIIIGG GSGGLAAAKE AAKYDKKVMV LDFVTPTPLG TRWGLGGTCV 

        70         80         90        100        110        120 
NVGCIPKKLM HQAALLGQAL RDSRNYGWNV EETVKHDWER MTEAVQNHIG SLNWGYRVAL 

       130        140        150        160        170        180 
REKKVTYENA YGEFVGPHRI KATNNKGKEK IYSAERFLIA TGERPRYLGI PGDKEYCISS 

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

       250        260        270        280        290        300 
QEHGIKFIRQ FVPIKVEQIE AGTPGRLRVI AKSTDSDQTI EGEYNTVLLA IGRDACTRKI 

       310        320        330        340        350        360 
GLENVGVKIN EKTGKIPVTE EEQTNVPYIY AIGDILEGKL ELTPVAIQAG RLLAQRLYGG 

       370        380        390        400        410        420 
STVKCDYENV PTTVFTPLEY GSCGLSEEKA VEKFGEENVE VYHSYFWPLE WTIPSRDNNK 

       430        440        450        460        470        480 
CYAKVVCNIK DNERVVGFHV LGPNAGEVTQ GFAAALKCGL TKDQLDSTIG IHPVCAEVFT 

       490 
TLSVTKRSGG NILQTGCUG 

« Hide

References

[1]Terashima H.
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Small intestine.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF053984 mRNA. Translation: AAC13914.1.
IPIIPI00685161.
RefSeqNP_777050.1. NM_174625.3.
UniGeneBt.5534.

3D structure databases

ProteinModelPortalO62768.
ModBaseSearch...

Protein-protein interaction databases

STRINGO62768.

Proteomic databases

PRIDEO62768.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID282388.
KEGGbta:282388.

Organism-specific databases

CTD7296.

Phylogenomic databases

eggNOGmaNOG06865.
HOVERGENHBG004959.
InParanoidO62768.
OrthoDBEOG4H463K.
PhylomeDBO62768.

Family and domain databases

InterProIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
IPR006338. Thioredoxin/glutathione_Rdtase.
[Graphical view]
Gene3DG3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
KOK00384.
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.
SUPFAMSSF55424. FAD/NAD-linked_reductase_dimer. 1 hit.
TIGRFAMsTIGR01438. TGR. 1 hit.
PROSITEPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTRXR1_BOVIN
AccessionPrimary (citable) accession number: O62768
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: February 26, 2008
Last modified: November 16, 2011
This is version 104 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families