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Q9N2I8 (TRXR2_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Thioredoxin reductase 2, mitochondrial

EC=1.8.1.9
Alternative name(s):
Thioredoxin reductase TR3
Gene names
Name:TXNRD2
Synonyms:TRXR2
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length511 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Maintains thioredoxin in a reduced state. Implicated in the defenses against oxidative stress. May play a role in redox-regulated cell signaling. Ref.1

Catalytic activity

Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.

Cofactor

FAD. Ref.1

Enzyme regulation

Inhibited by 1-chloro-2,4-dinitrobenzene and by zinc, calcium, magnesium and Fe2+ ions. Ref.1

Subunit structure

Homodimer. Ref.1

Subcellular location

Mitochondrion Ref.1.

Miscellaneous

The active site is a redox-active disulfide bond. The selenocysteine residue is also essential for catalytic activity By similarity. UniProtKB Q9Z0J5

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2121Mitochondrion Ref.1
Chain22 – 511490Thioredoxin reductase 2, mitochondrial Ref.1
PRO_0000030287

Regions

Nucleotide binding29 – 5830FAD By similarity

Sites

Active site4841Proton acceptor By similarity

Amino acid modifications

Non-standard residue5101Selenocysteine
Modified residue1401N6-acetyllysine By similarity
Disulfide bond74 ↔ 79Redox-active By similarity UniProtKB P00390
Cross-link509 ↔ 510Cysteinyl-selenocysteine (Cys-Sec) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9N2I8 [UniParc].

Last modified February 26, 2008. Version 2.
Checksum: CA74A147B32846ED

FASTA51154,670
        10         20         30         40         50         60 
MAALRGAAAR FRGRAPGGAR GAAGRQCYDL LVIGGGSGGL ACAKEAAQLG KKVAVLDYVE 

        70         80         90        100        110        120 
PSPQGTRWGL GGTCVNVGCI PKKLMHQAAL LGGMIRDAPH YGWGVAQAPH SWATLADAVQ 

       130        140        150        160        170        180 
NHVKSLNWGH RIQLQDRKVK YFNVKASFVD THTVCGVSKG GEETLLSAEH IVIATGGRPR 

       190        200        210        220        230        240 
YPTHIEGALE YGITSDDLFW LKESPGKTLV VGASYVALEC AGLLTGLGLD TTVMIRSVPL 

       250        260        270        280        290        300 
RAFDQQMASL VTEHMAGHGT RILRGCAPEK VEKLPGQQLR VTWVDLTSDR KDAGTFDTVL 

       310        320        330        340        350        360 
WAIGRVPETA SLNLEKAGVH TNPVTGKILV DAQETTSVPH IYAIGDVAEG RPELTPTAIM 

       370        380        390        400        410        420 
AGRLLAQRLS GRTSDLMDYS SVPTTVFTPL EYGCVGLSEE AAVARHGEEH VEVYHAFYKP 

       430        440        450        460        470        480 
LEFTVPQRDA SQCYIKMVCL REPPQLVLGL HFLGPNAGEV IQGFALGIKC GASYQQLMRT 

       490        500        510 
VGIHPTCAEE VAKLRISKRS GLDPTVTGCU G 

« Hide

References

[1]"Mitochondrial thioredoxin reductase in bovine adrenal cortex. Its purification, properties, nucleotide/amino acid sequences, and identification of selenocysteine."
Watabe S., Makino Y., Ogawa K., Hiroi T., Yamamoto Y., Takahashi S.Y.
Eur. J. Biochem. 264:74-84(1999) [PubMed: 10447675] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-35; 53-82; 160-181; 208-238; 292-316; 328-340; 420-436; 470-488 AND 499-510, SELENOCYSTEINE AT SEC-510, FUNCTION, SUBCELLULAR LOCATION, ENZYME REGULATION.
Tissue: Adrenal cortex.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB022283 mRNA. Translation: BAA82153.1.
IPIIPI00690111.
RefSeqNP_777051.1. NM_174626.2.
UniGeneBt.4008.

3D structure databases

ProteinModelPortalQ9N2I8.
ModBaseSearch...

Proteomic databases

PRIDEQ9N2I8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID282389.
KEGGbta:282389.

Organism-specific databases

CTD10587.

Phylogenomic databases

eggNOGmaNOG16321.
HOVERGENHBG004959.
InParanoidQ9N2I8.
OrthoDBEOG408N7T.

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 nameTRXR2_BOVIN
AccessionPrimary (citable) accession number: Q9N2I8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: February 26, 2008
Last modified: November 16, 2011
This is version 85 of the entry and version 2 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