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Protein

Thioredoxin reductase 2, mitochondrial

Gene

Txnrd2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.

Cofactori

FADUniRule annotationCurated

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei497 – 4971Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi41 – 7030FADBy similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • cell redox homeostasis Source: InterPro
  • cellular oxidant detoxification Source: MGI
  • heart development Source: MGI
  • hemopoiesis Source: MGI
  • response to oxygen radical Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

BRENDAi1.8.1.9. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin reductase 2, mitochondrial (EC:1.8.1.9)
Alternative name(s):
Thioredoxin reductase TR3
Gene namesi
Name:Txnrd2
Synonyms:Trxr2
OrganismiMus musculus (Mouse)Imported
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1347023. Txnrd2.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3434Mitochondrion1 PublicationAdd
BLAST
Chaini35 – 524490Thioredoxin reductase 2, mitochondrialPRO_0000030289Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei79 – 791N6-succinyllysineCombined sources
Disulfide bondi86 ↔ 91Redox-activeBy similarity
Modified residuei175 – 1751N6-succinyllysineCombined sources
Modified residuei329 – 3291N6-succinyllysineCombined sources
Cross-linki522 ↔ 523Cysteinyl-selenocysteine (Cys-Sec)By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

EPDiQ9JLT4.
MaxQBiQ9JLT4.
PaxDbiQ9JLT4.
PRIDEiQ9JLT4.

PTM databases

iPTMnetiQ9JLT4.
PhosphoSiteiQ9JLT4.

Expressioni

Tissue specificityi

Expressed in liver, heart, testis and kidney.3 Publications

Gene expression databases

BgeeiQ9JLT4.
CleanExiMM_TXNRD2.
GenevisibleiQ9JLT4. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

IntActiQ9JLT4. 3 interactions.
MINTiMINT-1862055.
STRINGi10090.ENSMUSP00000111269.

Structurei

Secondary structure

1
524
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi39 – 457Combined sources
Helixi49 – 6012Combined sources
Beta strandi65 – 684Combined sources
Helixi85 – 895Combined sources
Helixi91 – 11222Combined sources
Helixi125 – 14925Combined sources
Beta strandi153 – 1553Combined sources
Beta strandi158 – 17013Combined sources
Beta strandi176 – 18611Combined sources
Beta strandi190 – 1923Combined sources
Helixi201 – 2044Combined sources
Helixi208 – 2114Combined sources
Beta strandi220 – 2245Combined sources
Helixi228 – 23912Combined sources
Beta strandi244 – 2507Combined sources
Turni252 – 2554Combined sources
Helixi258 – 27013Combined sources
Beta strandi274 – 2774Combined sources
Beta strandi279 – 2868Combined sources
Beta strandi292 – 2987Combined sources
Turni299 – 3013Combined sources
Beta strandi304 – 31411Combined sources
Beta strandi318 – 3214Combined sources
Helixi323 – 3253Combined sources
Helixi327 – 3304Combined sources
Beta strandi336 – 3383Combined sources
Beta strandi345 – 3484Combined sources
Beta strandi354 – 3563Combined sources
Helixi358 – 3603Combined sources
Beta strandi361 – 3644Combined sources
Helixi368 – 38316Combined sources
Beta strandi397 – 3993Combined sources
Beta strandi401 – 4099Combined sources
Helixi412 – 4198Combined sources
Helixi421 – 4233Combined sources
Beta strandi424 – 4307Combined sources
Helixi434 – 4385Combined sources
Beta strandi447 – 4559Combined sources
Beta strandi459 – 4679Combined sources
Helixi470 – 48213Combined sources
Helixi487 – 4915Combined sources
Helixi502 – 5054Combined sources
Turni511 – 5144Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZDLX-ray3.00A31-522[»]
1ZKQX-ray2.60A31-522[»]
3DGZX-ray2.25A34-521[»]
ProteinModelPortaliQ9JLT4.
SMRiQ9JLT4. Positions 37-518.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9JLT4.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center, Transit peptide

Phylogenomic databases

eggNOGiKOG0405. Eukaryota.
COG1249. LUCA.
HOGENOMiHOG000276712.
HOVERGENiHBG004959.
InParanoidiQ9JLT4.
KOiK00384.
OMAiGLHFTGP.
OrthoDBiEOG779NXG.
TreeFamiTF314782.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
IPR006338. Thioredoxin/glutathione_Rdtase.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 3 hits.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01438. TGR. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9JLT4-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MVAAMVAALR GPSRRFRPRT RALTRGTRGA ASAAGGQQSF DLLVIGGGSG
60 70 80 90 100
GLACAKEAAQ LGKKVAVADY VEPSPRGTKW GLGGTCVNVG CIPKKLMHQA
110 120 130 140 150
ALLGGMIRDA HHYGWEVAQP VQHNWKTMAE AVQNHVKSLN WGHRVQLQDR
160 170 180 190 200
KVKYFNIKAS FVDEHTVRGV DKGGKATLLS AEHIVIATGG RPRYPTQVKG
210 220 230 240 250
ALEYGITSDD IFWLKESPGK TLVVGASYVA LECAGFLTGI GLDTTVMMRS
260 270 280 290 300
IPLRGFDQQM SSLVTEHMES HGTQFLKGCV PSHIKKLPTN QLQVTWEDHA
310 320 330 340 350
SGKEDTGTFD TVLWAIGRVP ETRTLNLEKA GISTNPKNQK IIVDAQEATS
360 370 380 390 400
VPHIYAIGDV AEGRPELTPT AIKAGKLLAQ RLFGKSSTLM DYSNVPTTVF
410 420 430 440 450
TPLEYGCVGL SEEEAVALHG QEHVEVYHAY YKPLEFTVAD RDASQCYIKM
460 470 480 490 500
VCMREPPQLV LGLHFLGPNA GEVTQGFALG IKCGASYAQV MQTVGIHPTC
510 520
SEEVVKLHIS KRSGLEPTVT GCUG
Length:524
Mass (Da):56,603
Last modified:February 26, 2008 - v4
Checksum:i74D4713DC8EF6A80
GO
Isoform 2 (identifier: Q9JLT4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: MVAAMVAALRGPSRRFRPRTRALTRGTRGAASAAGG → MEG

Show »
Length:491
Mass (Da):53,240
Checksum:i7CADE2DB621459E5
GO
Isoform 3 (identifier: Q9JLT4-3) [UniParc]FASTAAdd to basket

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.
Show »
Length:356
Mass (Da):38,475
Checksum:iD9DAA8F46B034082
GO
Isoform 4 (identifier: Q9JLT4-4) [UniParc]FASTAAdd to basket

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

Show »
Length:493
Mass (Da):53,279
Checksum:i7BFA5DCA255CD55D
GO

Sequence cautioni

The sequence AAF03359.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH52157.3 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAL90457.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAQ03230.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAA86986.2 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 63AMV → GRMW in AAF03359 (PubMed:10500251).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3636MVAAM…SAAGG → MEG in isoform 2. CuratedVSP_008293Add
BLAST
Alternative sequencei318 – 35639RVPET…PHIYA → KDAASHTDTVSSSRKPYFLG RRVFAFLPITSWILHSAGS in isoform 3. 1 PublicationVSP_008294Add
BLAST
Alternative sequencei357 – 524168Missing in isoform 3. 1 PublicationVSP_008295Add
BLAST
Alternative sequencei395 – 42531Missing in isoform 4. 1 PublicationVSP_008296Add
BLAST

Non-standard residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-standard residuei523 – 5231SelenocysteineBy similarity

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF136399 mRNA. Translation: AAF03359.1. Different initiation.
AF171053 mRNA. Translation: AAD51323.1.
AB027566 mRNA. Translation: BAA86986.2. Different initiation.
AF414359
, 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.
RefSeqiNP_038739.2. NM_013711.3.
UniGeneiMm.390906.

Genome annotation databases

GeneIDi26462.
KEGGimmu:26462.
UCSCiuc007ynx.1. mouse. [Q9JLT4-3]
uc007yny.1. mouse. [Q9JLT4-1]

Keywords - Coding sequence diversityi

Alternative splicing, Selenocysteine

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF136399 mRNA. Translation: AAF03359.1. Different initiation.
AF171053 mRNA. Translation: AAD51323.1.
AB027566 mRNA. Translation: BAA86986.2. Different initiation.
AF414359
, 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.
RefSeqiNP_038739.2. NM_013711.3.
UniGeneiMm.390906.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZDLX-ray3.00A31-522[»]
1ZKQX-ray2.60A31-522[»]
3DGZX-ray2.25A34-521[»]
ProteinModelPortaliQ9JLT4.
SMRiQ9JLT4. Positions 37-518.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9JLT4. 3 interactions.
MINTiMINT-1862055.
STRINGi10090.ENSMUSP00000111269.

PTM databases

iPTMnetiQ9JLT4.
PhosphoSiteiQ9JLT4.

Proteomic databases

EPDiQ9JLT4.
MaxQBiQ9JLT4.
PaxDbiQ9JLT4.
PRIDEiQ9JLT4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi26462.
KEGGimmu:26462.
UCSCiuc007ynx.1. mouse. [Q9JLT4-3]
uc007yny.1. mouse. [Q9JLT4-1]

Organism-specific databases

CTDi10587.
MGIiMGI:1347023. Txnrd2.

Phylogenomic databases

eggNOGiKOG0405. Eukaryota.
COG1249. LUCA.
HOGENOMiHOG000276712.
HOVERGENiHBG004959.
InParanoidiQ9JLT4.
KOiK00384.
OMAiGLHFTGP.
OrthoDBiEOG779NXG.
TreeFamiTF314782.

Enzyme and pathway databases

BRENDAi1.8.1.9. 3474.

Miscellaneous databases

EvolutionaryTraceiQ9JLT4.
PROiQ9JLT4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JLT4.
CleanExiMM_TXNRD2.
GenevisibleiQ9JLT4. MM.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
IPR006338. Thioredoxin/glutathione_Rdtase.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 3 hits.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01438. TGR. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 4), ALTERNATIVE SPLICING.
    Strain: BALB/cJ.
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Pancreas, Spleen and Testis.
  8. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-79; LYS-175 AND LYS-329, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiTRXR2_MOUSE
AccessioniPrimary (citable) accession number: Q9JLT4
Secondary accession number(s): Q6KG49
, Q80VZ4, Q91YX4, Q9JHA7, Q9JMH5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: February 26, 2008
Last modified: June 8, 2016
This is version 140 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.