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Reviewed, UniProtKB/Swiss-Prot Q9JLT4 (TRXR2_MOUSE)

Last modified November 3, 2009. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length524 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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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.

Catalytic activity

Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.

Cofactor

FAD By similarity.

Subunit structure

Homodimer By similarity. UniProtKB P38816

Subcellular location

Mitochondrion. Ref.2

Tissue specificity

Expressed in liver, heart, testis and kidney. Ref.2 Ref.1 Ref.3

Miscellaneous

The active site is a redox-active disulfide bond. The selenocysteine residue is also essential for catalytic activity By similarity. UniProtKB Q9ZOJ5

Sequence similarities

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

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Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9JLT4-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9JLT4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: MVAAMVAALRGPSRRFRPRTRALTRGTRGAASAAGG → MEG
Isoform 3 (identifier: Q9JLT4-3)

The sequence of this isoform differs from the canonical sequence as follows:
     318-356: RVPETRTLNL...EATSVPHIYA → KDAASHTDTV...TSWILHSAGS
     357-524: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q9JLT4-4)

The sequence of this isoform differs from the canonical sequence as follows:
     395-425: Missing.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3434Mitochondrion Ref.3
Chain35 – 524490Thioredoxin reductase 2, mitochondrial
PRO_0000030289

Regions

Nucleotide binding41 – 7030FAD By similarity

Sites

Active site4971Proton acceptor By similarity

Amino acid modifications

Non-standard residue5231Selenocysteine By similarity
Modified residue1531N6-acetyllysine By similarity
Disulfide bond86 ↔ 91Redox-active By similarity
Cross-link522 ↔ 523Cysteinyl-selenocysteine (Cys-Sec) By similarity

Natural variations

Alternative sequence1 – 3636MVAAM…SAAGG → MEG in isoform 2.
VSP_008293
Alternative sequence318 – 35639RVPET…PHIYA → KDAASHTDTVSSSRKPYFLG RRVFAFLPITSWILHSAGS in isoform 3.
VSP_008294
Alternative sequence357 – 524168Missing in isoform 3.
VSP_008295
Alternative sequence395 – 42531Missing in isoform 4.
VSP_008296

Experimental info

Sequence conflict4 – 63AMV → GRMW in AAF03359. Ref.1

Secondary structure

1 .................................................................................... 524
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 26, 2008. Version 4.
Checksum: 74D4713DC8EF6A80

FASTA52456,603
        10         20         30         40         50         60 
MVAAMVAALR GPSRRFRPRT RALTRGTRGA ASAAGGQQSF DLLVIGGGSG GLACAKEAAQ 

        70         80         90        100        110        120 
LGKKVAVADY VEPSPRGTKW GLGGTCVNVG CIPKKLMHQA ALLGGMIRDA HHYGWEVAQP 

       130        140        150        160        170        180 
VQHNWKTMAE AVQNHVKSLN WGHRVQLQDR KVKYFNIKAS FVDEHTVRGV DKGGKATLLS 

       190        200        210        220        230        240 
AEHIVIATGG RPRYPTQVKG ALEYGITSDD IFWLKESPGK TLVVGASYVA LECAGFLTGI 

       250        260        270        280        290        300 
GLDTTVMMRS IPLRGFDQQM SSLVTEHMES HGTQFLKGCV PSHIKKLPTN QLQVTWEDHA 

       310        320        330        340        350        360 
SGKEDTGTFD TVLWAIGRVP ETRTLNLEKA GISTNPKNQK IIVDAQEATS VPHIYAIGDV 

       370        380        390        400        410        420 
AEGRPELTPT AIKAGKLLAQ RLFGKSSTLM DYSNVPTTVF TPLEYGCVGL SEEEAVALHG 

       430        440        450        460        470        480 
QEHVEVYHAY YKPLEFTVAD RDASQCYIKM VCMREPPQLV LGLHFLGPNA GEVTQGFALG 

       490        500        510        520 
IKCGASYAQV MQTVGIHPTC SEEVVKLHIS KRSGLEPTVT GCUG

« Hide

Isoform 2.

Checksum: 7CADE2DB621459E5
Show »

FASTA49153,240
Isoform 3.

Checksum: D9DAA8F46B034082
Show »

FASTA35638,475
Isoform 4.

Checksum: 7BFA5DCA255CD55D
Show »

FASTA49353,279

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References

« Hide 'large scale' references
[1]"cDNA cloning, expression and chromosomal localization of the mouse mitochondrial thioredoxin reductase gene."
Miranda-Vizuete A., Damdimopoulos A.E., Spyrou G.
Biochim. Biophys. Acta 1447:113-118(1999) [PubMed: 10500251] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: Liver.
[2]"Molecular cloning of mouse thioredoxin reductases."
Kawai H., Ota T., Suzuki F., Tatsuka M.
Gene 242:321-330(2000) [PubMed: 10721726] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
Tissue: Thymocyte.
[3]"Redox regulation of cell signaling by selenocysteine in mammalian thioredoxin reductases."
Sun Q.-A., Wu Y., Zappacosta F., Jeang K.-T., Lee B.J., Hatfield D.L., Gladyshev V.N.
J. Biol. Chem. 274:24522-24530(1999) [PubMed: 10455115] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 35-44; 65-76; 255-277 AND 341-373, TISSUE SPECIFICITY.
Tissue: Liver.
[4]"Genomic organization and identification of a novel alternative splicing variant of mouse mitochondrial thioredoxin reductase (TrxR2) gene."
Miranda-Vizuete A., Spyrou G.
Mol. Cells 13:488-492(2002) [PubMed: 12132591] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 4), ALTERNATIVE SPLICING.
Strain: BALB/c.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
Strain: FVB/N.
Tissue: Limb and Mammary tumor.
[6]"Heterogeneity within animal thioredoxin reductases: evidence for alternative first exon splicing."
Sun Q.-A., Zappacosta F., Factor V.M., Wirth P.J., Hatfield D.L., Gladyshev V.N.
J. Biol. Chem. 276:3106-3114(2001) [PubMed: 11060283] [Abstract]
Cited for: ALTERNATIVE SPLICING.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AF136399 mRNA. Translation: AAF03359.1. Different initiation.
AF171053 mRNA. Translation: AAD51323.1.
AB027566 mRNA. Translation: BAA86986.2. Different initiation.
AF414359 expand/collapse EMBL AC list , AF414356, AF414357, AF414358 Genomic DNA. Translation: AAL90457.1. Different initiation.
AF412308 mRNA. Translation: AAQ03230.1. Different initiation.
BC013688 mRNA. Translation: AAH13688.1.
BC052157 mRNA. Translation: AAH52157.3. Different initiation.
IPIIPI00124699.
IPI00271280.
IPI00350590.
IPI00471266.
RefSeqNP_038739.2.
UniGeneMm.390906

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1ZDLX-ray3.00A31-524[»]
1ZKQX-ray2.60A31-524[»]
3DGZX-ray2.25A34-521[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ9JLT4. 1 interaction.
STRINGQ9JLT4.

Proteomic databases

PRIDEQ9JLT4.

Genome annotation databases

EnsemblENSMUST00000082425; ENSMUSP00000081006; ENSMUSG00000075704; Mus musculus. [Genome view]
ENSMUST00000115606; ENSMUSP00000111269; ENSMUSG00000075704; Mus musculus. [Genome view]
GeneID26462.
KEGGmmu:26462.
UCSCuc007ynx.1. mouse.

Organism-specific databases

CTD26462.
MGIMGI:1347023. Txnrd2.

Phylogenomic databases

HOVERGENQ9JLT4.
OMAIGMENEQ.

Enzyme and pathway databases

BRENDA1.8.1.9. 244.

Gene expression databases

ArrayExpressQ9JLT4.
BgeeQ9JLT4.
CleanExMM_TXNRD2.
GenevestigatorQ9JLT4.
GermOnlineENSMUSG00000075704. Mus musculus.

Family and domain databases

InterProIPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD_bd.
IPR006338. Thioredoxin/glutathione_Rdtase.
[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.
ProDomPD000139. FAD_pyr_redox. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01438. TGR. 1 hit.
PROSITEPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio304577.
SOURCESearch...

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Entry information

Entry nameTRXR2_MOUSE
AccessionPrimary (citable) accession number: Q9JLT4
Secondary accession number(s): Q6KG49 expand/collapse secondary AC list , Q80VZ4, Q91YX4, Q9JHA7, Q9JMH5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: February 26, 2008
Last modified: November 3, 2009
This is version 82 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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